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stringlengths 6
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stringlengths 108
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P52045 | MSYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCIILRAPSGSKVFSAGHDIHELPSGGRDPLSYDDPLRQITRMIQKFPKPIISMVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRDAGFHIVKELIFTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEKAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSEDYQEGMNAFLEKRKPNFVGH | Function: Catalyzes the decarboxylation of (R)-methylmalonyl-CoA to propionyl-CoA. Could be part of a pathway that converts succinate to propanoate.
Catalytic Activity: (R)-methylmalonyl-CoA + H(+) = CO2 + propanoyl-CoA
Sequence Mass (Da): 29173
Sequence Length: 261
EC: 4.1.1.-
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P43471 | MIWNRKTRYTPYEQWPATKLPQLVAQARQSKWRMQHHIQPTSGLLNDPNGFSYFDGQWHLFYQVFPFGPVHGLKSWQHVTSKNLVDWHDEGLAIRPDTPYDSHGAYTGTALPIDDQLFIMYTGNVRTADWQRESYQLGAWMDTDNHIKKLSRPLIAHAPAGYTSSFRDPDLIRNDHGYYALIGAQTTTEIGAILVYFSKDLTTWTCQGELNVPANARGYMIECPNLVWIDQQPVLLFCPQGLSQATIPYQNIYPNMYLVADQLNLAQAQFTEPHALTQLDDGFDVYATQAINAPDGRALAVSWIGLPEISYPTDRENWAHCLSLVKELTLKDGHLYQNPVAAVDDLRTTAHDLVFEQQRATVAALNGSFELLLTVPADKTVTVNIADQQESGQLQVTVDANHGQVMIDRRHTGNSFAEDYGQTRQVELTAHKTIKIRLIIDVSVFECYIDNGYSVMTGRFFLNATPSRLNVQGDTTAVTGKVWEWRQSEHTGVDNNETKIK | Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 56690
Sequence Length: 501
Pathway: Glycan biosynthesis; sucrose metabolism.
EC: 3.2.1.26
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Q05936 | MSEWTKEQRYQKYEDVDQQTIEKLTEQVNQSEYRQTFHIQPQIGLLNDPNGLIYFKGNYYVSHQWFPLGPVHGLKYWYTYQSKDLVDFKAIGPTIKPDTKDDSHGVYSGSAFEYHDHLYYMYTANHRDSDWNRISTQHIAKMSKDGSINKFPKAVISAPPSGYTQHFRDPKVHVQDGVYYAMIAAQNIKKQGRILQYRSTDIVNWEFQGEVQTNLDDFGYMWECPDYFNLNGYDMLLFCPQGIDSEGERFKNIYQSGYIMGQYDINNLTMNHADFHELDYGFDFYAPQTFLDENGQRILIGWMGLPDINYPSDADGWAHCLTIPRVLTIESGNLKQRPIKALEKLRTNEETALGYANKFTRQLHPYEGKQFELIIDILENEATEVYFEVRTSKTESTLITYNKREQKLTLDRSESGQLPEPVEGTTRSTYLDTPLSKLQLFVDTSSVEIFCNDGERVMTARIFTDENATGIKTSTESGQTYLKFTKYDLKGDTI | Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 57371
Sequence Length: 494
Pathway: Glycan biosynthesis; sucrose metabolism.
EC: 3.2.1.26
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P13522 | MNLPQNIRYRRYQDWTEEEIKSIKTNVALSPWHTTYHIEPKTGLLNDPNGFSYFNGKFNLFYQNWPFGAAHGLKSWIHTESEDLVHFKETGTVLYPDTSHDSHGAYSGSAYEIGDQLFLFYTGNVRDENWVRHPLQIGAFMDKKGNIQKFTDVLIKQPNDVTEHFRDPQIFNYKGQFYAIVGAQSLDKKGFIKLYKAVDNDIKNWQEVGNLDFGGSKSEYMIECPNLVFINEQPVLIYSPQGLSKSELDYHNIYPNTYKVCQSFDTEKPALVDASEIQNLDFGFECYATQAFNAPDGRVYAVSWIGLPDIDYPSDSYDYQGALSLVKELSLKHGKLYQYPVEAVRSLRSEKEAVTYKPETNNTYELELTFDSSSVNELLLFADNKGNGLAITVDTKMGTILIDRSKAGEQYALEFGSQRSCSIQAKETVVNIFVDKSIFEIFINKGEKVFTGRVFPNDKQTGIVIKSGKPSGNYYELKY | Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 54672
Sequence Length: 479
Pathway: Glycan biosynthesis; sucrose metabolism.
Subcellular Location: Cytoplasm
EC: 3.2.1.26
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P13394 | MSLNNRWTVEQRYRRLEQIPQCDIEEMTLSRQQDKGFPSFHIAPKFGLLNDPNGLCYFNGEHHIFYQWTPVGPVHGMKYWYHLSTKDFIHFTDHGVGLHPDQDYDSHGVYSGGALVENNQVLLFFTGNKRDQNWNRIPTQCFATMDSDGSIEKHGVVIENEHYTEHFRDPKVWKKGDDYLMVVGAQTKTEHGSMALYQSKDLKTWQHKGPIKTKFSDLGYMWECPDFFEINGQSVMLFSPQGVSSSNPYDFKNIYSVAYIVGDQLNLESMTLENHQDILQPDYGFDFYAPQTYLDESGRRILIAWIGLPEIDTPSVTHQWAGMLSLPRELTLKDGFLVQTPLPELKSLRKEEVVFAQSHTLESTSCLIQLDLVGDGFELELSNLKGDNIVFSATEHEFMLDRRYMSHLYAEEFGGIRKAPRLDAKQTIDIYIDNSVIEIFINGGKHTMTSRFFIDDLNKVTLKGLEQARLFPLKGITGLFESAK | Function: Enables the bacterium to metabolize sucrose as a sole carbon source.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 55657
Sequence Length: 484
Pathway: Glycan biosynthesis; sucrose metabolism.
Subcellular Location: Cytoplasm
EC: 3.2.1.26
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A5EZZ8 | MLLDTLLELAGGINNVTRILAPQGQVVLALKHPPHAPHLPDDVSLQSVLGEWQLSVQRTAEVSDQQLAAIGKAIAERQKRATLPYQTALDCPYRPQWHISPPQGLLNDPNGFIYHQEEYHLFYQWHPFACEHKDKYWVHLKSLDLVHWQWQSVALTPSDWFDSHGVFSGHAVSHQQDLWLFYTGNTRLGTERQRQTMQCAARMNANGEFEKLGPVIRCLPEGVTEHIRDPKVIYTQGKWQMLLGAQTLAHQGRLAVYHSDDLLHWHFDKLYGDELGDYGYMWECPDWFELQGEAFFVFGPQGIASANPHHTIEHQNRIFRATQNAQGEIALLQGWPLDEGFDFYAPQTAQTADGRRVLCGWMGLPDETQHPSCDQGWIHQLTALRELEWREGKIYQHPLRELDTLQSEPHTLLLSDTVTELKTKSFDLQVTLPWGCELRLMQNAQYCVTLTLDAENRLLRLDRSATQIRQGDTIRELKLDSPTVELRILADQSSLEIFINQGEHVMTSRIFTPLDATGISLHGASVDAKLYYMAPASAPFNLEVNV | Function: Enables the bacterium to metabolize sucrose as a sole carbon source.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 62312
Sequence Length: 546
Pathway: Glycan biosynthesis; sucrose metabolism.
Subcellular Location: Cytoplasm
EC: 3.2.1.26
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A0A063CBJ7 | MLINAARLLLPAAALVHLSLAWATSDRCNGYSSTLIQIKHAGDIYKQPSVPGLPPPGVNPYSLIDTLLKNGEDWCKHCASPRVSVDAGRYKAQMDKLLSYAHPYSASSWDSVQSLGDALEHLCKASRKEN | Function: Secreted effector required for full virulence of U.virens . Inhibits host pathogen-associated molecular pattern-triggered immunity including flg22- and chitin-induced defense gene expression and oxidative burst .
Sequence Mass (Da): 14147
Sequence Length: 130
Domain: The Plant immunity suppression domain is sufficient to retain the ability to suppress immunity-associated responses.
Subcellular Location: Secreted
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Q9SID0 | MASNGDKGLIVSFGEMLIDFVPTESGVSLAEAPGFLKAPGGAPANVAIAVSRLGGRSAFVGKLGDDEFGHMLAGILRKNGVDDQGINFDTGARTALAFVTLRADGDREFMFYRNPSADMLLRPDELNLDLIRSAKVFHYGSISLIVEPCRSAHLKAMEVAKEAGALLSYDPNLREPLWPSKEEAKTQIMSIWDKAEIIKVSDVELEFLTGSNKIDDETALTLWHPNLKLLLVTLGEKGCRYYTKTFKGAVDPFHVNAVDTTGAGDSFVGALLNQIVDDRSVLEDEERLRKVLRFANACGAITTTKKGAIPALPSDAEVRSFLEKK | Function: May play an important role in maintaining the flux of carbon towards starch formation.
Catalytic Activity: ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+)
Sequence Mass (Da): 35275
Sequence Length: 325
Pathway: Glycan biosynthesis; starch biosynthesis.
EC: 2.7.1.4
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P01484 | MNYLVMISLALLFVTGVESVKDGYIVDDVNCTYFCGRNAYCNEECTKLKGESGYCQWASPYGNACYCYKLPDHVRTKGPGRCHGR | Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. The toxin principally slows the inactivation process of TTX-sensitive sodium channels . It is active on rat brain Nav1.2/SCN2A sodium channel (EC(50)=2.6 nM) and on rat skeletal muscle Nav1.4/SCN4A sodium channel (EC(50)=2.2 nM) , as well as on human neuronal Nav1.7/SCN9A (EC(50)=6.8 nM) . This toxin is active against mammals. In vivo, intraplantar injection into mice induces spontaneous pain responses .
PTM: The amidation of His-83 is not necessary for toxicity.
Sequence Mass (Da): 9548
Sequence Length: 85
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P08900 | KEGYLVSKSTGCKYECLKLGDNDYCLRECKQQYGKSSGGYCYAFACWCTHLYEQAVVWPLPNKTCN | Function: Beta toxin that binds site-4 of sodium channels (Nav) and reduces peak current (observed on Nav1.6/SCN8A (IC(50)=307 nM)), shifts the voltage of activation toward more negative potentials (observed on Nav1.6, Nav1.1 (weak), Nav1.2 (weak), and Nav1.7 (weak)), and induces resurgent currents at negative voltages following brief and strong depolarizations (observed on Nav1.6, Nav1.1 (weak), and Nav1.7 (weak)) . A reduction of peak current of Nav1.5/SCN7A has been observed in another study (IC(50)=35-40 nM) . This toxin is only active on mammals . It has been shown to bind phospholipids .
PTM: C-terminal amidation increases its affinity for sodium channels.
Sequence Mass (Da): 7547
Sequence Length: 66
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P18927 | KEGYIVNYHTGCKYTCAKLGDNDYCLRECK | Function: Binds to sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission.
Sequence Mass (Da): 3489
Sequence Length: 30
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P45668 | EDGYLLNRDTGCKVSCGTCRYCND | Function: Binds to sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active against mammals.
Sequence Mass (Da): 2686
Sequence Length: 24
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P86989 | KEGYPKNSEGCKITCLFNDPYCKGLCINLSTQADY | Function: Causes paralysis and death in insects (A.domestica).
Sequence Mass (Da): 3917
Sequence Length: 35
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P0DL23 | NKDGYLMEHDGCKLSCLMKKGTFCAEXCARLXGXDGYC | Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
Sequence Mass (Da): 4195
Sequence Length: 38
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P0DV30 | VRDAYIAKPENCVYHCAGNEGCNNLCTCNGAT | Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin dose-dependently delays inactivation of voltage-gated sodium channels (Nav) (EC(50)=0.91 uM), and shifts the steady-state activation and inactivation to hyperpolarized direction. In addition, it dose-dependently alters calcium dynamics and increases phosphorylation of MAP kinases 1/3 (MAPK1/MAPK3) and cAMP-response element binding (CREB) proteins in neocortical neurons. This effect is eliminated by tetrodotoxin, a Nav blocker.
Sequence Mass (Da): 3405
Sequence Length: 32
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P0C5J7 | KDGYPVDNANCKYE | Function: Binds to sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission (By similarity). Causes prolonged contractile paralysis in C.partellus larvae. It also has significant toxic effects on B.fusca larvae but not on mice.
Sequence Mass (Da): 1616
Sequence Length: 14
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P0DL24 | KDGYLVGSDGCKYSCLTRPG | Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
Sequence Mass (Da): 2119
Sequence Length: 20
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P0DL25 | GGKEGYPLNSSNGCKSGRFAGTNSNENTECKGXDAENGY | Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
Sequence Mass (Da): 4025
Sequence Length: 39
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P0C911 | GRDGYIAQPENXVYXX | Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission.
Sequence Mass (Da): 1816
Sequence Length: 16
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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Q7X279 | MTREGFVPWPKEAADRYREAGYWRGRPLGSYLHEWAETYGDTVAVVDGDTRLTYRQLVDRADGLACRLLDSGLNPGDAMLVQLPNGWEFVTLTLACLRAGIAPVMAMPAHRGHELRYLAAHAEVTSIAVPDRLGDFDHQALGREVAEDTPSVGLLLVAGGTVGTDATDLRALAEPADDPVTARARLDRIAPDSGDIAVFLLSGGTTGLPKLITRTHDDYEYNARRSAEVCGLDSDSVYLVALPAGHNFPLACPGILGTLMNGGRVVLARTPEPGKVLPLMAAEGVTATAAVPAVVQRWIDAVASGRHPAPPALRLLQVGGARLAPEVARRAEPVLGGTLQQVFGMAEGLLNYTRPDDPDDIKIETQGRPMCPDDEILVVDASDNPVPPGEMGALLTRGPYTPRGYYRAAEHNARAFTPDGWYRTGDVVRLHPSGNLVVEGRDKDLINRGGEKISAEEVENLIYRLPGVARVAAVAKADPDLGERVCAVVVVEPGTQLSLESVRAALTAMQVARYKLPEDLLVVDELPLTKVGKIDKKRLRDVVRGKADSVEAV | Function: Involved in the degradation of salicylate via a pathway involving coenzyme A derivative. Catalyzes the conversion of salicylate to salicyloyl-CoA via the formation of a salicylate-adenylate intermediate. The substrate specificity is strong, since benzoate, 3-hydroxybenzoate, 4-hydroxybenzoate, gentisate, 2-aminobenzoate, aminobenzoate, salicylamide, salicylaldoxime and 2-hydroxyphenyl acetate cannot substitute for salicylate.
Catalytic Activity: ATP + CoA + salicylate = 2-hydroxybenzoyl-CoA + AMP + diphosphate
Sequence Mass (Da): 59350
Sequence Length: 553
EC: 6.2.1.65
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A0A1U8QHS4 | MDKRSFKVIVVGGSIAGLTLAHSLDLAGIDYIVLEKHSDPLATVGGSVGLLPNGWRILHQLGLRHQLEQEACPVKVAHMTYPDGFVFSDNFPAAIQERQVPEIQFPIGYMPANDERFGYSLSVLTRQQLIEVLYLGLRDKSKIKVGQRVIKIQHHQNRRGVSVFTESGQEHVGDLVAGADGVHSITRSQMWLQLGQKLDAEKERRQLVAEYSCVFGISSPLKGIPPGEQLIACHDNATVLAFPGKDAHIGWGLIQKLNRPCNSPATTQSSDGETALIMAKSAAGLGLCKDLKFHDLWVNTPKYSFTILEEGLFQIWHHGRIMTPNMAQGANTAIEGAAALANTLRRISQIDKPSEDDINRLLQGYTVRQQKRLRAVHAISRSVTRVHARQGRIKKIIGRYVYPYTPGAALHTFSRIIAPAPCLDYVPMPFPGPGWTRALVSGWSPISGVLLLVIPIIALVYGYSVINFGRDSINN | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the polyenes aspernidgulenes . The carbon backbone of aspernidgulenes is synthesized by the HR-PKS sdgA, which accepts acetyl-CoA as the starter unit and performs malonyl-CoA extensions as well as regioselective methylation and reduction . The resulting nonaketide offloads the HR-PKS by intramolecular lactonization to yield the 5,6-dihydro-alpha-pyrone-containing hexaenoic acids preaspernidgulene A1 and A2 . The FAD-dependent monooxygenase sdgC then installs the first epoxide on the penultimate double bond . Subsequently, the FAD-dependent monooxygenase sdgF presumably generates a ketone intermediate through Meinwald rearrangement involving a hydride shift . Next, sdgC introduces another epoxide on the last olefin of the ketone intermediate after E/Z isomerization . The epoxide hydrolase sdgD then catalyzes stereospecific cyclization of the 5,6-dihydro-alpha-pyrone and opening of the epoxide ring to form an oxygenated trimethylcyclopentanone and an oxabicyclo[2.2.1]heptane unit . Finally, the bicyclic unit undergoes hydrolytic cleavage, either spontaneously or catalyzed by sdgD, to assemble the dimethyl-gamma-lactone moiety in aspernidgulene A1 .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 52305
Sequence Length: 475
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q7X281 | MKVACIGAGPGGLFFATLLKRSRPDAEVVVFERNRPDDTFGFGVVFSDATLDAIDAADPVLSEALEKHGRHWDDIEVRVHGERERVGGMGMAAVVRKTLLSLLQERARAEGVQMRFQDEVRDPAELDDFDLVVVCDGANSRFRTLFADDFGPTAEVASAKFIWFGTTYMFDGLTFVHQDGPHGVFAAHAYPISDSLSTFIVETDADSWARAGLDAFDPATPLGMSDEKTKSYLEDLFRAQIDGHPLVGNNSRWANFATRRARSWRSGKWVLLGDAAHTAHFSVGSGTKMAMEDAVALAETLGEASRSVPEALDLYEERRRPKVERIQNSARPSLSWWEHFGRYVRSFDAPTQFAFHFLTRSIPRGKLAVRDAAYVDRVDGWWLRHHEAGPLKTPFRVGPYRLPTRRVTVGDDLLTGTDGTGIPMVPFSGQPFGAGVWIDAPDTEEGLPLALDQVRETAEAGVLLVGVRGGTALTRVLVAEEARLAHSLPAAIVGAYDDDTATTLVLSGRADLVGGTK | Function: Involved in the degradation of salicylate via a pathway involving coenzyme A derivative. Catalyzes the aromatic hydroxylation of salicylyl-CoA to yield gentisyl-CoA.
Catalytic Activity: 2-hydroxybenzoyl-CoA + H(+) + NADH + O2 = 2,5-dihydroxybenzoyl-CoA + H2O + NAD(+)
Sequence Mass (Da): 56572
Sequence Length: 517
EC: 1.14.13.209
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A0A1U8QW16 | MSHQSTINFIRFTFVILSLLAIYTILIPSIRKGFFQHITECEVTGKLSRSSGADARMIESFTGVPVLDIFVKALVTSFWPVINGENPALSLLGVPAVASMGVSYLLLLLEARRTRSLLSVTWRLAWVGLLQTNFSQAIILPIYCAIAFSSSKKTNGFRPIPHVTISLILCVYTGMALVALPSPAVIPDGLKQVVVAFMVPWALWVFVMVFMASYLFPIEVEKEKSRRTIYIFALVIAATTHLGALLASLLHADLGPADVFLPPLPWYVTRFPSLEEGMASFLQWDYLIASVTLFLWAVAVYLRDCDEHVDWQRFGLEVCAISVIISPAAMAVLLIWRLDEMLSRRGIAKED | Function: Epoxide hydrolase; part of the gene cluster that mediates the biosynthesis of the polyenes aspernidgulenes . The carbon backbone of aspernidgulenes is synthesized by the HR-PKS sdgA, which accepts acetyl-CoA as the starter unit and performs malonyl-CoA extensions as well as regioselective methylation and reduction . The resulting nonaketide offloads the HR-PKS by intramolecular lactonization to yield the 5,6-dihydro-alpha-pyrone-containing hexaenoic acids preaspernidgulene A1 and A2 . The FAD-dependent monooxygenase sdgC then installs the first epoxide on the penultimate double bond . Subsequently, the FAD-dependent monooxygenase sdgF presumably generates a ketone intermediate through Meinwald rearrangement involving a hydride shift . Next, sdgC introduces another epoxide on the last olefin of the ketone intermediate after E/Z isomerization . The epoxide hydrolase sdgD then catalyzes stereospecific cyclization of the 5,6-dihydro-alpha-pyrone and opening of the epoxide ring to form an oxygenated trimethylcyclopentanone and an oxabicyclo[2.2.1]heptane unit . Finally, the bicyclic unit undergoes hydrolytic cleavage, either spontaneously or catalyzed by sdgD, to assemble the dimethyl-gamma-lactone moiety in aspernidgulene A1 .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39043
Sequence Length: 351
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 5.4.99.-
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Q7X284 | MTDTTSEQTERKLLDELYADFEDAGLIPLWTQVDGLMPMSPQPAAVPHLWRWAELLPIAQRSGELVPVGRGGERRAMALSNPGFPGLPYATPTLWTAIQYLGPREVAPSHRHSQGAFRFVVEGEGVWTNVDGDAVAMRRGDLLLTPSWAFHEHQNVTDEPMAWLDGLDIPLVSKLDAGFFEFGPDELSTRETPERSRGERLWGHPGLRPIGRPDQPNSPLNAYRWEHTDAALTAQLELEQEGVPGVLEPGHAGVRFSNPTTGRDALVTMRTEMRRLRAGTRTAPVRTVGSAIWQVFEGEAVARVGDKVFEIAKGDLFVVPSWCEVSLSARTQVDLFRFSDEPVYEALGLARTSRGEHK | Function: Involved in the degradation of salicylate via a pathway involving coenzyme A derivative. Catalyzes the oxygen-dependent ring fission of gentisate between the carboxyl and proximal hydroxyl groups at positions 1 and 2 of the aromatic ring to form maleylpyruvate. The substrate specificity is strong, since salicylate, catechol, protocatechuic acid, homogenetisate, 2,3-dihydroxybenzoate or 5-aminosalicylate cannot substitute for gentisate in the ring cleavage reaction.
Catalytic Activity: 2,5-dihydroxybenzoate + O2 = 3-maleylpyruvate + H(+)
Sequence Mass (Da): 39720
Sequence Length: 358
EC: 1.13.11.4
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P0CF23 | MEMTHYEKTPLIRQVFNNGKTNSWFYVKHEILQPGGSFKSRGIGHLIRKSNQQPLSEGSGKLAVFSSSGGNAGLAAATACRSMALNCSVVVPKTTKPRMVKKIQSAGAKVIIHGDHWGEADEYLRHKLMAQESQHGSKTLYVHPFDNETIWEGHSTIVDEIIEQLKENDISLPRVKALVCSVGGGGLFSGIIKGLDRNHLAEKIPVVAVETAGCDVLNKSLKKGSPVTLEKLTSVATSLASPYIASFAFESFNKYGCKSVVLSDQDVLATCLRYADDYNFIVEPACGASLHLCYHPEILEDILEQKIYEDDIVIIIACGGSCMTYEDLVKASSTLNVS | Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 36824
Sequence Length: 338
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.3.1.17
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P0DKI0 | MAATALFRSIRRRDVVSAPLSVYKSLAGNAQPSWGSSYIGQNYASFSRAFGSKPVVNDILGTGLGTNNAIREEREKSKSTEAAIVGAQLTRSFRALDVGTSKRLFSTISGDIKTTQEEPKIKSFRPLSPHLSVYQPQMNSMLSIFNRISGVYLTGVTFAGYLLYLKMGMICLTYPSFYQVLYHTQQQLPVITSVTALAAIYHTIKSTHSLLTH | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23454
Sequence Length: 213
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q6ZH92 | MEKYHSNSRFAPFRDAPFALRGALGSSGSSFSSIDSLRRSSTLEQARGYTSRPLGAVRPKMLPSGCRPLHTSHPLSAPVANRPLSPHLPLKKPQLSATFSISHRIFGAALGAAIISIPLATKFSLMFDV | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13873
Sequence Length: 129
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q84VK7 | MEKYQSKARFAPLSDAPFALRGALGSSNSSFNNIDHLRQSSSSGQARSYTSSPLGALRPKMFPSGNRLLHTSRPLSAPVANRPLSPHLPLKKPQLSATFSISHRIFGAALGAVIISIPLATKFSLMFDV | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13863
Sequence Length: 129
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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O74882 | MFATRSFCLSSSLFRPAAQLLRPAGRSTLRNVWRRSIATEHLTQTEANSRLASQRVHRPNSPHLTIYEPQLTWYLSSLHRITGCVVAGTLYAFAMGYLVAPLAGYSLDTATISGLIQQVPTWIKVPAKFVISYPLTFHIFNGIRHLIWDTTKELSLKGVYRTGYAVLALSVLTSGYFAMI | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20136
Sequence Length: 180
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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P33421 | MSAMMVKLGLNKSALLLKPSAFSRAAALSSSRRLLFNTARTNFLSTSPLKNVASEMNTKAAIAEEQILNKQRAKRPISPHLTIYQPQLTWYLSSLHRISLVLMGLGFYLFTILFGVSGLLGLGLTTEKVSNWYHQKFSKITEWSIKGSFAYLFAIHYGGAIRHLIWDTAKELTLKGVYRTGYALIGFTAVLGTYLLTL | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring mono-heme cytochrome b subunit of succinate dehydrogenase (SDH) that is involved in system II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH3 and SDH4 form the membrane dimer that anchors the catalytic dimer formed by SDH1 and SDH2 to the matrix surface of the mitochondrial inner membrane. Electrons originating from the catalytic dimer enter the membrane dimer for ubiquinone reduction.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22068
Sequence Length: 198
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q941A0 | MSLRRTILDLHRQTQRATLSKSLPFSMSHISSASATAAVRNPLGRDLSSIPFAQAQKLKPDSTNLVTDRSISSSIGQSELNKAAKFSRQSSSRGYTNGSFLRKIPVVFHIHEGMEEILADYVHQEMTRNLIVMSLGLFQIIVLKDIILFLL | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16842
Sequence Length: 151
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q942X4 | MASRLLARSKALALALSRADAAAPGPAAGVQWLRTLSSLPRDPAAAASPAPAPRQPAVGSPLGLSKIPGYEQTSRLSGTQVLPRWFSTGTSNGSSAQQEGATRKVMAFSPLEASIAKPRKGPLTSESWKVKQTELLTRSTYYMIPTLLLVSKNSISTSLLVASVFHQVYMFYKEILLDYVHHDITRKWVFIYFKILLIIMAKETVVYFDLF | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23130
Sequence Length: 211
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q9SX77 | MGTLGRAIHTVGNRIRGTAQAQARVGSLLQGSHHIEKHLSRHRTLITVAPNASVIGDVQINKGSFISYASVSRDLQYPRAMGMGQVRRFSEDVSHMPEMEDSDVLNAFKDLMAADWAELPSAVVKDAKTAISKNTDDKAGQEALKNVFRAAEAVEEFGGILTSIKMEIDDSIGMSGEGVKPLPNDITDALRTAYQRYAEYLDSFEPEEVYLKKKVEMELGTKMIHLKMRCSGLGSEWGKVTVLGTSGLSGSYVEQRA | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28106
Sequence Length: 257
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q0JDA2 | MAAALRSSCAAARRLLRISPAALSTLTAASSRPAAVAPLARPIAAAAVSGGNNAFSWNLRRLFSSNEKHLPAISDPEVESAFKDLMAASWTGLPDSLVIEAKKAASKATDDKAGKEALLNVFRAAEACEEFGGVLVTLRMALDDLCGITGENVGPLPGYIEDAVKSAYKRYMKYLESFGPEENYLRKKVENELGTKMIHLKMRCSGVGSEWGKITLIGTSGISGSYVELRA | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24583
Sequence Length: 231
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q941A6 | MGDSESFVGKNWNGLKDFWSDRLSFFENYTRFTKRDAPLPSWSSSDVEEFIASDPVHGPTLKTAREAVTFGVTGAALGAVSTAAFAWKYSRSPHGAALSFLGGGVFGWTFGQEVANHTLQLYKLDTMAAQVKFMEWWERKSQ | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15813
Sequence Length: 142
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q6ZCC4 | MGIHEHVEGIKAHWAKNFSFLDYFKKVYGRDKPLPKWTDADVDEFIASDPVYGPQLKAMRESRKFALGGALVGGAHLGGIALKYSKAPHGVVLATGFGAICGAVVGSEVAEHWYQLYKTDKQGANLRFIYWWEDKVAGNQKS | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15728
Sequence Length: 142
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q9C5E8 | MAFLLNTSISSHLRSSSQKTDGALAQSRRGFHVELGAREKALLAEDASLRRFKSHKKGVHRLKRIGDVLTVVVVAGCCYEIYARVMRKEAQAA | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10298
Sequence Length: 93
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q3E870 | MAFLLNNASISSHLRSSSSQKTGDALSISRRGFHIEPGTREKALLAEDSALKRFKSHKKSVHKLKRIGDVLTVVVVAGCCYEIYVKAVMKKEALAAGKSS | Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10860
Sequence Length: 100
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q86B06 | MGLKTTISPDSSFDKIINTKTSPPLHINSPMLESLALSKLFKEENAKVWMKVDALQPSGSFKIRGVGLLCNQLLKEKKSKNEEAHFICSSGGNAGKSVAYAGRKLNVKTTIVLPNTIPEATIEKIKDEGANVIVHGTIWDEANTFALELAEKEGCTDCYIHPFDHPLLWEGHSTMIDEIYQDVQNGVCEKPDVILFSVGGGGMMIGILQGLDRYGWNDIPIVTVETVGSHSFWKSFQEKQLTKLDVSEVTSVIKTLSTRSVCSEAWEISKRFNIKPILVTDRDAVDACLKFVDDERILVEPSCGATLSVLYSKKLSTLLDINSKNILTIVCGGNGTSILQLNDLLQTLPK | Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 38457
Sequence Length: 350
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.3.1.17
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P16095 | MISLFDMFKVGIGPSSSHTVGPMKAGKQFVDDLVEKGLLDSVTRVAVDVYGSLSLTGKGHHTDIAIIMGLAGNEPATVDIDSIPGFIRDVEERERLLLAQGRHEVDFPRDNGMRFHNGNLPLHENGMQIHAYNGDEVVYSKTYYSIGGGFIVDEEHFGQDAANEVSVPYPFKSATELLAYCNETGYSLSGLAMQNELALHSKKEIDEYFAHVWQTMQACIDRGMNTEGVLPGPLRVPRRASALRRMLVSSDKLSNDPMNVIDWVNMFALAVNEENAAGGRVVTAPTNGACGIVPAVLAYYDHFIESVSPDIYTRYFMAAGAIGALYKMNASISGAEVGCQGEVGVACSMAAAGLAELLGGSPEQVCVAAEIGMEHNLGLTCDPVAGQVQVPCIERNAIASVKAINAARMALRRTSAPRVSLDKVIETMYETGKDMNAKYRETSRGGLAIKVQCD | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Deaminates also threonine, particularly when it is present in high concentration.
PTM: Activated by post-translational modification by a system involving at least three gene products. Activation is mimicked in vitro by iron and dithiothreitol. There is considerable evidence for a free-radical activation mechanism.
Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 48907
Sequence Length: 454
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.3.1.17
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P71349 | MISVFDMFKVGIGPSSSHTVGPMKAGKQFIDDLIKRNQFEQTTEIHVDVYGSLSMTGRGHSTDIAIIMGLAGYLPHNVDIDMISGFIEKVKQTALLPINVGQKIVKFDFENNLIFHRTFLKLHENGMTITALDENRTELYRQTYYSIGGGFIVDEAHFGKEEKNTVQVPYPYKNAEDILKHCSDNGLMLSTVMLENEIALNGKEAVSAHLENVWKTMQACIEHGIHTEGILPGPLRVPRRAASLYRALQANTNLSNDPMRVIDWVNMFALAVNEENAAGGRVVTAPTNGACGIIPAVLAYYEKFISPLTPEIIERYLLAAGMIGSLYKMNASISGAEVGCQGEVGVACSMAAAGLAEILGGNPLQVCIAAEIAMEHNLGLTCDPVGGQVQVPCIERNAIASVKAINASRMALRRTTNPRVTLDKVIETMYETGKDMNAKYRETSQGGLAVKIVCN | Cofactor: Binds 1 [4Fe-4S] cluster.
Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 49538
Sequence Length: 455
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.3.1.17
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P56072 | MASFSILSIFKIGVGPSSSHTIGPMEAGARFCESLKGILEQVVRVQITLHGSLALTGKGHLSDEAVLIGLHGIYANELEVTTKKALLHEALENKVLKLANQHHIPFDYAKDLIFDNKPLTRHQNALILKAFNSKNEVLKEETYYSVGGGFVYTEKELDNLSEEDGNESIAYDFSSAKELLELCQKHQKSIAEIVRLRENALKNHPDATMVKIYHAMLECYDNGANSKERYLPGSLKVTRLAPSIKTRLEKHPTSGKDPLALIDYISLYARAIAEENASGGKVVTAPTNGACAVVPSVLLYAKNHLFENLSQKAINDFLLTSAAIGYLYKKNASLSGAEAGCQAEIGVASSMAAGGLAHLCQATTQQVLIASEIAMEHHLGLTCDPVGGLVQIPCIERNVLGAIKAISASKLALEDEYKPKVSLDEVIATMYATGKDMNEKYKETSLGGLAKTLKC | Cofactor: Binds 1 [4Fe-4S] cluster.
Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 49242
Sequence Length: 455
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.3.1.17
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P20132 | MMSGEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSVGGGGLLCGVVQGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEGNLRTPLPSLVVIVCGGSNISLAQLRALKEQLGMTNRLPK | Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 34625
Sequence Length: 328
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.3.1.17
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Q8VBT2 | MAAQESLHVKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSVGGGGLLCGVVQGLREVGWEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEGRLQTPLASLVVIVCGGSNISLAQLQALKVQLGLNGLPE | Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 34593
Sequence Length: 327
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.3.1.17
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P66774 | MTISVFDLFTIGIGPSSSHTVGPMRAANQFVVALRRRGHLDDLEAMRVDLFGSLAATGAGHGTMSAILLGLEGCQPETITTEHKERRLAEIAASGVTRIGGVIPVPLTERDIDLHPDIVLPTHPNGMTFTAAGPHGRVLATETYFSVGGGFIVTEQTSGNSGQHPCSVALPYVSAQELLDICDRLDVSISEAALRNETCCRTENEVRAALLHLRDVMVECEQRSIAREGLLPGGLRVRRRAKVWYDRLNAEDPTRKPEFAEDWVNLVALAVNEENASGGRVVTAPTNGAAGIVPAVLHYAIHYTSAGAGDPDDVTVRFLLTAGAIGSLFKERASISGAEVGCQGEVGSAAAMAAAGLAEILGGTPRQVENAAEIAMEHSLGLTCDPIAGLVQIPCIERNAISAGKAINAARMALRGDGIHRVTLDQVIDTMRATGADMHTKYKETSAGGLAINVAVNIVEC | Cofactor: Binds 1 [4Fe-4S] cluster.
Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 48576
Sequence Length: 461
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.3.1.17
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O86564 | MAISVFDLFSIGIGPSSSHTVGPMRAARMFARRLRNEELLDSVASVRVELYGSLGATGHGHGTPKAVLLGLEGDSPRTVDVESADDRVETIKSSGRISLLGDHEIAFAYDDDMVLHRRKALPYHANGMTLWAYDAEGAEVLTKTYYSVGGGFVVDEDAVGADRIVLDDTVLKYPFRTGDELLRLARETGLSISALMLENERAWRDEDEIREGLLEIWRVMRACVDRGMTREGILPGGLKVRRRAANTARKLRSEGDPQALAMEWITLYAMAVNEENAAGGRVVTAPTNGAAGIIPAVLHYYMNFVPGADEDGVVRFLLAAGAIGMLFKENASISGAEVGCQGEVGSACSMAAGALAEVLGGSPEQVENAAEIGMEHNLGLTCDPVGGLVQIPCIERNGMAAVKAVTAARMAMRGDGSHKVSLDKVIKTMKETGADMSVKYKETARGGLAVNIIEC | Cofactor: Binds 1 [4Fe-4S] cluster.
Catalytic Activity: L-serine = NH4(+) + pyruvate
Sequence Mass (Da): 48601
Sequence Length: 455
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.3.1.17
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Q59787 | MRLDGKTALITGSARGIGRAFAEAYVREGARVAIADINLEAARATAAEIGPAACAIALDVTDQASIDRCVAELLDRWGSIDILVNNAALFDLAPIVEITRESYDRLFAINVSGTLFMMQAVARAMIAGGRGGKIINMASQAGRRGEALVGVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKFADYENLPRGEKKRQVGAAVPFGRMGRAEDLTGMAIFLATPEADYIVAQTYNVDGGNWMS | Function: Catalyzes the oxidation of D-sorbitol (D-glucitol) to D-fructose. Can also catalyze the oxidation of galactitol to D-tagatose and the oxidation of L-iditol, with lower efficiency.
Catalytic Activity: H(+) + keto-D-fructose + NADH = D-sorbitol + NAD(+)
Sequence Mass (Da): 27014
Sequence Length: 256
EC: 1.1.1.-
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Q6P1D5 | MPVARPQAAGPDRISLFLVAFLLGSPAAAQAEDGGPEGEMHPSTAYLLPSASLESSLEEGVTSAAPGLLPSQEALEAMEESLPPALPDEASVQHTPALRKGLPSLKQLNSARRQLRPLATPTTLQRLGSPASATTKLREPEDPEQPTAPAPLQIAPFTALATTLPHSPQPAQAPDDSSPGSPLDKGDNELTGSASEESQETTTSTIVTTTIITTEQAPALCGVSFSDPEGYIDSSDFPPQPYSSFLECTYNVTVYTGYGVELQVKSVNLSEGELLSIRGVDGPTLTVLANQTLLVEGQVIRSPTNTISVYFRTFQDDGLGTFQLHYQAFMLSCPFPRRPDAGEVTVMDLHSGGVAHFHCHLGYELQGAKTLTCINASKPHWSSQEPVCSAPCGGAVHNATIGRVLSPSFPGTANGSQLCVWTIEAPEGQKLHLHLERLLLHEKDRMIVYSGRTNTSALLYDSLRTESVPFEGLLSEGSSIRIEFTSDQGQAASAFNIRFEAFEKGHCYEPYIQNGNFTTSDPTYNIGTIVEFTCDPGHSLEQGPAVIECVNVRDPYWNDTEPLCRAMCGGELSAVAGVVLSPNWPEPYAEGEDCVWKIHVGEEKRIFLDIQFLNLSNSDILTIYDGDEVVPHVLGQYFGHSSPQKLYSSTPDLTIQFHSDPAGLIFGKGQGFIMNYIEVSRNDSCSDLPEIQNGWKTTSHTELVRGARITYQCDPGYDIVGSDTLTCQWDLSWSSDPPFCEKIMYCTDPGEVEHSTRLISDPVLLVGTTIQYTCSPGFVLEGSSLLTCYSRETGTPIWTSRLPHCVSEESLACDNPGLPENGYQILYKRLYLPGESLTFMCYEGFELMGEVTIRCILGQPSHWSGPLPICKVNQDSFEHALEAEAAAESSLEGGNMALAIFIPVLLISLLLGGAYIYVTRCRQYSSLRLPLMYSHPYSQITVETEFDNPIYETGETREYEVSI | Function: Candidate tumor suppressor gene. May contribute to specialized endoplasmic reticulum functions in neurons.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 104827
Sequence Length: 963
Subcellular Location: Cell membrane
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Q4V9Z5 | MGTPKAQHPPPSQLLLLILLSCAWIEGLPLKEDEMMPEPGSETPTVASEDLAELLHGALLRKGPEIGFLPGSDPDPTLATPPAGQTLAAPSLPRATEPGTGPLTTAVTPKGVRGAGPTAPELLTPPPGTTAPPPPGPASPVPPLRPEGGEEETTTTIITTTTVTTTVTSPVLCNNNISEGEGFVESPDLGSTASRSVELLDCTYSIHVYPGYGIEIQVQTLNLSQEEELLVLAGGGSPGLAPRLLANSSMLGEGQVLRSPTNRLLLHFQSPRVPRGNGFRIHYQAYLLSCGFPPRPAHGDVSVTDLHPGGTATFHCDSGYQLQGEETLICLNGTRPAWTGEPPSCTASCGGTIHNATLGRIVSPEPGGAAGPNLTCRWVIEAAEGRRLHLHFERVSLDEDNDRLMVRSGGSPLSPVIYDSDMDDVPERGLISDAQSLYVELLSETPANPLLLSLRFEAFEEDRCFPPFLAHGNVTTTDPEFHPGALATFSCLPGYALEPPGPPNAIECVDPTEPHWNDTEPACKAMCGGELSEPAGVVLSPDWPQSYSPGQDCVWGLHVQEEKRILLQVEILNVREGDMLTLFDGDGPSARVLAQLRGPQPRRRLLSSGPDLTLQFQAPPGPPNPGLGQGFVLHFKEVPRNDTCPELPPPEWGWRTASHGDLIRGTVLTYQCEPGYELLGSDILTCQWDLSWSAAPPACQKIMTCADPGEITNGHRTASDAGFPVGSHVQYRCLPGYSLEGAAVLTCYSRDTGTPKWSDRVPKCALKYEPCLNPGVPENGYQTLYKHHYQAGESLRFFCYEGFELIGEVTITCVPGHPSQWTSQPPLCKVTQTTDPSRQLEGGNLALAILLPLGLVIVLGIGVYIYYTKLQGKSLFGFSGSHSYSPITVESDFSNPLYEAGDTREYEVSI | Function: May contribute to specialized endoplasmic reticulum functions in neurons.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 97504
Sequence Length: 910
Subcellular Location: Cell membrane
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P30650 | MNPSISTAGAVVDDFQMSCRFSNFGDHAPESFDSLSCGACFYFIFMLVEHYKDRYVASLCEDTFGVLVCPVDVSDKICNCYNREYVYNIPEFALNSSRIKPLNHLRLDPPLPFQFDLIVKDCCSAARYCCRNTLVKYHHRVDDSPCPPTWDGWNCFDSATPGVVFKQCPNYIYGGSNIKTDYDRLSQKVCRSNGWATPEVNAAAREHTDYTGCMSNGDVEARILAGLLTYSASVIFLIPAVFLLTLLRPIRCQPMFILHRHLLISCLLYGAFYLITVSLFVVNDAPLSSQVFQNHLFCRLLFSIQLRYLRLTNFTWMLAEAVYLWRLLHTAQHSEGETLRSYKVICWGVPGVITVVYIFVRSLNDDVGMCWIENSTVAWIEWMIITPSLLAMGVNLLLLGLIVYILVKKLRCDPHLERIQYRKAVRGALMLIPVFGVQQLLTIYRFRNVCLIYRLLHKSFCRRMCSEILVITSGEAGSRS | Function: Not known. Putative receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54808
Sequence Length: 480
Subcellular Location: Cell membrane
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P07560 | MSGLRTVSASSGNGKSYDSIMKILLIGDSGVGKSCLLVRFVEDKFNPSFITTIGIDFKIKTVDINGKKVKLQLWDTAGQERFRTITTAYYRGAMGIILVYDVTDERTFTNIKQWFKTVNEHANDEAQLLLVGNKSDMETRVVTADQGEALAKELGIPFIESSAKNDDNVNEIFFTLAKLIQEKIDSNKLVGVGNGKEGNISINSGSGNSSKSNCC | Function: Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP-bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as the attachment site for the SEC8/SEC15 particle.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23506
Sequence Length: 215
Subcellular Location: Cytoplasmic vesicle
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Q9Y7T6 | MYIMSKKCYDTSEKIDREQECVEVNYQHRNFESILEIFSVLFIPFLCNSGKKFLQISNASFFLPACFYLLGSSSIIQLYEPLLWLSSFPFCILYVGFGENSVLYHEMYTVCLYNALLSLTQRWKWLSIVLDGLGNSSVNLKLHETVILAFLEITQNSFTFIEGILICTGLTGLCFATFSYEVSPVVSVLSGVLLISLPTLILLNLCILKLAAKLHLSALFTTCLIYFFSALLVFLVSRSWVAGQLGQAPEVWLFNQIFSHRNSLTRIKIIIWWIICLGCFIFILLRSNRNNPLGKYFTTEDEVLNFRRKTYHALVVFLFLPVCCLDPHFLHLSFSGVLFIFLFVEGIRILRLKPFGKMIHEFLWEYTDNRDHKGPLIISHIYLLIGCAIPIWLSNALKGPVASVELLVGVLCLGCGDSMASIIGKRFGKHRISKTNKSIEGVFAFSISVFLVLHLTQAFHVCPSVTFWKTLFMSLCTAILEGVSTENDNLILPMYMWVLYQALD | Function: Involved in the synthesis of the sugar donor Dol-P-Man which is required in the synthesis of N-linked and O-linked oligosaccharides and for that of GPI anchors. It is required for spore germination. Has an essential role in cellular metabolism (By similarity).
Catalytic Activity: CTP + di-trans,poly-cis-dolichol = a dolichyl phosphate + CDP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57425
Sequence Length: 504
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.1.108
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P20048 | MVAIIPHASFTTIKLTQKTEGSQMPTEEICKINMRTRKFDVGGNSRDFECFYSNFVQTVILLGTFFYCVERLQPWSIVTADISYKQIFVNVFVVCLIMVGLIFTKYWQHGYKSLPKFDTIYSLYLPFMVSLLFDTSSTVINTILILSVLNSYRWRTQLVVIILQLCLIFFNFEAGDRLKNIISIVINSLLSLILKYIGQLKSLDNIDSNLFSILLTNILYVSEAGTVHFRILKGIILALTTIISINYVLKKVMHFKPFMLSISFAIGLPLFANTFIHLEDGENPLLWLVKYILESTIRQKILFAWSSILILSIPSILIEKDSLSLNTSRKLWHFIIFLLIIPSFQMDSNFVKIALSGTIPVFLSIEYIRFQNLPPLGSAIELQLRRFADDRDHSGPLIISYLYLLFGISTPLLMNNSPMGLIGLGIGDSLASIIGKRYGRIRWKGTQKTLEGTLAFIVTSFIVCLVLLRFDKAAIFNHLTTLQLLTLCTLSGVLEGNSVLNDNILIPAFMMICEKLITL | Function: Involved in the synthesis of the sugar donor Dol-P-Man which is required in the synthesis of N-linked and O-linked oligosaccharides and for that of GPI anchors. It is required for spore germination. Has an essential role in cellular metabolism.
Catalytic Activity: CTP + di-trans,poly-cis-dolichol = a dolichyl phosphate + CDP + H(+)
Sequence Mass (Da): 58906
Sequence Length: 519
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.1.108
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Q75D26 | MSDPESPLWVATLLRHHKELKQRQGMFQSRHMEFFRFKRFVRALNSDEYRAKSEREPEKYPPVRSEEDARDVFVSLIKAQLVLPCTKLHTAQCREHGLAPSKDYPHLLLSTKATLDADEYYVWTHNPKTLTDYLTVVGVIVGILAFVCYPLWPHSMKRVVYYLSLGLLGLLAVFSALALVRFVIYVLSLAFCSERGGFWIFPNLFEDCGVIASFKPLYGFGETECYGYIKKQKRRKRKLEKKKQ | Function: Required for preprotein translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28406
Sequence Length: 244
Subcellular Location: Endoplasmic reticulum membrane
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Q5AI21 | MSAPTPPQTGQFQVATSAQRSPVAVNIVNYLFQNPILKQRTGLLDNTNDIEFFRFKRLQRALLSDDYKQKQQNPKNGLIPVANNEDVQKVFVLLIQNQLLLPLQKLHYAEVKAVKGWKPNKEKPTLKRADKAVMDPDVYYGWLYQKPNPYILLYSFLAIAGVFAVILFPLWPNFMKRGVWYLSMGALGLIALFFATAIVRLIIYIISLVAFPKPFWLFPNLFEDCGVIESFQPVYAWEEPKKKKGKKKKEPKLEVVEEKVGSSSGDVKVTGSELSNGSSTTGKRKVTLEEVEE | Function: Required for preprotein translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33286
Sequence Length: 293
Subcellular Location: Endoplasmic reticulum membrane
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Q6FRU9 | MDQSAVLAIASFVRNRSELKARKGLFQDKPTDFFRYKRFVRCLKSDAYKKKSLKQPDLYPPLPEDEEKFAELARGIFVEFIKNQLVVPGQKLHSYECKEHGLKPSKDYPHLIMSTKATLDDNEYYLWHYNPKTLTDYLIVFGVIGVILAFVCYPLWPASMRRGTYYLSLAAFGFLGVFFGVAIIRLIVFLISMLFIREKGGFWLFPNLFEDCGFFDSFKPLYGFGDKETYTYIKKMKKQKKRQAKKEKLKKLKEKAN | Function: Required for preprotein translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30095
Sequence Length: 257
Subcellular Location: Endoplasmic reticulum membrane
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P82009 | MGHRVDYFIASKAVDXLLMKYDKDIKKEKEKGKAESGKE | Function: Mediates post-translational transport of precursor polypeptides across endoplasmic reticulum (ER). Proposed to act as a targeting receptor for small presecretory proteins containing short and apolar signal peptides. Targets and properly positions newly synthesized presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 4498
Sequence Length: 39
Subcellular Location: Endoplasmic reticulum membrane
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Q99442 | MAERRRHKKRIQEVGEPSKEEKAVAKYLRFNCPTKSTNMMGHRVDYFIASKAVDCLLDSKWAKAKKGEEALFTTRESVVDYCNRLLKKQFFHRALKVMKMKYDKDIKKEKDKGKAESGKEEDKKSKKENIKDEKTKKEKEKKKDGEKEESKKEETPGTPKKKETKKKFKLEPHDDQVFLDGNEVYVWIYDPVHFKTFVMGLILVIAVIAATLFPLWPAEMRVGVYYLSVGAGCFVASILLLAVARCILFLIIWLITGGRHHFWFLPNLTADVGFIDSFRPLYTHEYKGPKADLKKDEKSETKKQQKSDSEEKSDSEKKEDEEGKVGPGNHGTEGSGGERHSDTDSDRREDDRSQHSSGNGNDFEMITKEELEQQTDGDCEEDEEEENDGETPKSSHEKS | Function: Mediates post-translational transport of precursor polypeptides across endoplasmic reticulum (ER). Proposed to act as a targeting receptor for small presecretory proteins containing short and apolar signal peptides. Targets and properly positions newly synthesized presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45862
Sequence Length: 399
Subcellular Location: Endoplasmic reticulum membrane
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Q6CLZ9 | MSEPSPQSTIAIANLLRTHSDLKQRQGLFQSRLVDFFRYKRFVRALKSDKYKAKSKKQPELYPAVTSDEDARNIFVSLIKAQFVVPAVKLHSAECKEHGLKPNKSYPNLLLSNKATLQPDEYYVWSYNPKSIYDYLTVIGIIVGVLAFVCYPLWPPYMKRGTYYLSIAALALIGVFFGIAIVRLIVYLLSLAAVSEKGGFWLFPNLFEDCGVIESFKPLYGFGEKECYSFLKKEKRKHRSVAKKQK | Function: Required for preprotein translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28172
Sequence Length: 246
Subcellular Location: Endoplasmic reticulum membrane
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O13787 | MDSSNVPVLKDEDKCKFSMRFTNFLKSRPELKTKPAILNGKRVYYFRVKRVLRFLTSEAYTPKKYKGFPEISSREEAIEVLKLLIMNSMLVRVDKLPPKQRKQKLVELQINRNQDFQDDMHYVWLYEPLPKRVMALAVLFALVVLALVLFPLWPMFMRKGAWYLSMGGLGVIGLFFVLVILRFFLFCITAVIVRPGIWLFPNLLADVGFCDSFKPLWSWHNSKSEVKKTRKSKKLSKKATSPAASATPEKSSTSTTSLKNLRHRNPTVEEVSE | Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and bip1 in a channel-forming translocon complex. In an initial step, the signal sequence seems to bind simultaneously to sec61 and sec62. sec62 and sec63 are required for interactions between sec61 and translocating polypeptides. sec62 may affect sec61-polypeptide interactions by increasing the affinity of targeting pathways for sec61 and/or by modifying sec61 to allow more efficient polypeptide interaction. A cycle of assembly and disassembly of Sec62/63 complex from sec61 may govern the activity of the translocon (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31586
Sequence Length: 273
Subcellular Location: Endoplasmic reticulum membrane
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Q99161 | MTENVPQGQITMPLQQGGAREISPQALAVADYLRSHKLLKQRPGILNGKRSDFFRVKRAIRALEDPKYKQLQSKPNSKLPPINSRNEAISIFRLMPINQMALRVDKLPTQTALMMKQKPEQGVPVLQVNPQQEFGDDMYYTWFYNPVPLTTYLYGALGVAAIFAGVLFPLWPIFLRQGVWYLSVGMLGLIGVFFGIALVRLVIFVLTWPTVKPGIWIFPNLFADVGFVDSFIPLWAWHGTPERDLLPQKFKNKKKKKNAGTVIESKEPPRKLTKEEKQKQKEANAQMEQMQAAFQTQLSSFATQMQQIKEMSDSGIDPQIIAAQLQAQYPPDKQAAIKLENEQAQAKLDERIRELAAQIQDKTNANKTGDKIEEVADKENKEAPKRIVTLEDANDE | Function: Required for preprotein translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44902
Sequence Length: 396
Subcellular Location: Endoplasmic reticulum membrane
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Q8DYM7 | MIAFNSLFSLDKKRLKKLQRTLNTINSLKGQMATLSNEELQAKTTEFRKRLVNGETLDDICAEAFAVVREADERVLGLFPYDVQVIGGLVLHQGNTAEMKTGEGKTLTATMPLYLNALEGKGAMLLTNNSYLAIRDAEEMGKVYRFLGLSVGVGVSDNEEEDRDAATKRAVYSSDIVYSTSSALGFDYLIDNLASSKSQKYMPKLHYAIVDEADAVLLDMAQTPLVISGSPRVQSNLYKIADELILSFEEQVDYYFDKERQEVWIKNQGVREAERYFRIPHFYKQSNRELVRHLNLSLKAHKLFERGKDYVVDDGEIKLLDATNGRVLEGTKLQGGVHQAIEQKEHLNVTPESRAMASITYQNLFRMFTKLAGMTGTGKTAEKEFIEVYDMEVVRIPTNSPVRRIDYPDKIYTTLPEKIHATIEFVKQVHDTGQPILLVAGSVRMSELFSELLLLSGIPHSLLNAQSAVKEAQMIAEAGQKGAVTVATNMAGRGTDIKLGKGVSELGGLAVIGTERMKSQRMDLQLRGRSGRQGDIGFSQFFVSFEDDLMIESGPKWAQDYFRKNRDKVNPEKPKALGQRRFQKLFQQTQEASDGKGESARSQTIEFDSSVQLQREYVYRERNALINGESGHFSPRQIIDTVISSFIAYLDGEVEKEELIFEVNRFIFDNMSYNLQGISKEMSLEEIKNYLFKIADEILREKHNLLGDSFGDFERTAALKAIDEAWIEEVDYLQQLRTVATARQTAQRNPVFEYHKEAYKSYNIMKKEIREQTFRNLLLSEVSFNENGDLQIYFI | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 90178
Sequence Length: 795
Subcellular Location: Cell membrane
EC: 7.4.2.8
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Q9AET6 | MVKNFFHIRRLKKILAKIKSFEKEMSSLSDLDLQKKTDEFKKRLADGENLDQLLPEAYAVVREVDKRILGLFPYDVQVMGAIVLHEGNIAEMATGEGKTLTATMPLYLNALSGQGAMLVTPNSYLALRDAKEMGPVYRFLGLTIETAVRADESKPLETKEKRRIYQADIIYTTNSALGFDYLIENLAENKKNQFLREFNYVIIDEIDSILLDSAQTPLIISGAPRVQSNFYDMMNTLVQTLYEDEDYCYDDEKNEVWLTQKGIRAAESFLGLNHLFSKENQELVRHLNLALRAHMVYKKDQDYVVRQSENEAEVVLLDRATGRLMELTRLQGGQHQAIEAKEHVKLTQETRAMASITYQNLFKLFRKLSGMTGTGKVVESEFLETYSMSVVKIPTNCPVIRRDYPDQIYQTLPEKVFASLDEVKHYHAKGNPLLIFTGSVEMSEIYSSLLLREGIAHNLLNANNVAREAQMIAESGQLGAVTVATSMAGRGTDIKLGPGVADLGGLVVIGTERMENHRIDLQIRGRSGRQGDPGISKFFISLEDDLLKKWGPDWIKNFYRDYSPEDFKNNPILLKQRRFKKLVSKAQKASEGNAKLSRRLTLEYAQSMKIQRELTYAERNRLLEDTNEMEEEINRVIEYVIKQVAYEQSFENRADFYRFILHHFSNRAERIPQEFDIHSPKEVSHLLQAIAEQELLAKKSYLKSDKLYSQFQRLAILKAIDENWVEQVDYLQQLKSALSGFHTSNKKPIVEYYQEAYDGFEYMKERMKHQIVKNLLMSELALNPKGEVVMYFP | Function: Part of the accessory SecA2/SecY2 system specifically required to export GspB, a serine-rich repeat cell wall protein encoded upstream in the same operon.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 91152
Sequence Length: 793
Subcellular Location: Cell membrane
EC: 7.4.2.8
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Q47RW8 | MAEGVRRLLGKPGSVSLQPYIKLLKTIEEREEALRKLSDAELTEVATELGNAELPYDRDDLAELCALGREAARRTLGERPFDTQLIGMMALLDGHVAEMATGEGKTLTGALAAVGFALRGQRVHVLSVNDYLARRDAEWMRPLYTLLGVEVGWISQESTTEERRAAYAADITYASVSELGFDVLRDRLATDVSELVVPEPNVAIIDEADSVLVDEARVPLVLAGAAEPAESDAAMAELVRRLRPGIDYKVDDDGRNVHLTDTGINVVEKALGGVDLFSAEDTTLLSRVNLALHAHALLHRDVHYVVRDGKVRLINESRGRIALLQRWPDGLQAAVEAKEHLTPSETGEVLDSITVQSLVLRYPIRCGMTGTAMAVAEQLREFYELEVAVIAPNKPNIRIDEEDRLYATAEEKEEAVVEKVKEVHATGRPILIGTQDVAESERLAKRLRRAGLECVVLNAKNDAEEAAVIAEAGTYGRITVSTQMAGRGTDIRLGGSDMRDRDRVVKTGGLYVIGYGRYPSSRLDDQLRGRAGRQGDPGGSVFYVSVEDDLITTNLPEAKGYRVSSADGEITDPAWKEMVNHAQRIAEGQLLELHRNTWRYNQIIDVQRSVVLEQRRAVLHEDLGSRQLAVDCPETYQRLVEEVGEEEVARAARLVTLYHLDRGWADHNAFLADLREGIHLRFLGRRDPLDEFNRDAVPAFKGFLDEARARAAEMFEKLEVVDGRLDVAAAGVKRPSTTWTYMVQDQPFSTDLENIVGRVKNLMGRD | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84833
Sequence Length: 766
Subcellular Location: Cell membrane
EC: 7.4.2.8
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A0L9N3 | MFNLSLHGDPYPQQPGHLQLSWLDRMGERVRLAWMRHKQVNGWVLGRMAKRVLKAQTERESMTPEALREDLQRLTLALRRDGLEDALVEQAFAHVRLTAQRVLGMAHFPVQLKGGYIMLMGYLAEMDTGEGKTLTATLPAATAALAGFTVHVVTVNEYLARRDAQLMTPLYRALGVTTGVVTESMDSDEKQLGYRANVVYCTSKTLVFDYLRDRIQLGERMKPMAMAFDALVGGGRGQVMLQGLQYAIVDEADSIFVDEARTPLIISAPSKDASELAFLHTAWSLSQQLQQGQDYTLSGEEPPRITEAGSAQLAQLCVDLPPVWQGQHRREEAVAQALTAQHSFDRDVHYIIRDDKVMVVDETTGRVMPDRAWERGLQQLIEIKEGVAVTPPKETLAKISFQLFFRRFLRLSGMSGTCREVGGEIAEVYGLGVVRVAPNRPSKRKNLPIALYAWRAQADAAVVQAVRRCHMLGQPVLVGTRSIAASELLSQSFSEAGLPHRVLNAKQDQEENTIIAEAGYKGGITIATNMAGRGTDIKLSKEVQACGGLHVILTERHDNRRVDRQLAGRCARQGDPGSWQEILSLEDELTQKFLPLLGRTLRAWLALMPHFFLARWLGMVYYRWAQSYADRGHRRVRRQLMKTDFQLRQSLSFTGEME | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73776
Sequence Length: 658
Subcellular Location: Cell inner membrane
EC: 7.4.2.8
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A3DF88 | MLKVFEKIFGSYSDREVKRIKPIIDRIEALEPEMQALSDEQLKAKTPEFKRRLSQGETLDDLLPEAFAVVREASRRVLGMRHFRVQLIGGVVLHQGRIAEMKTGEGKTLVATLPVYLNALEGKGVHVVTVNDYLATRDSEWMGKLYNFLGLSVGLIVHGLTNEERKKAYSCDITYGTNNEFGFDYLRDNMVIYKEDMVQRDLHFAIVDEVDSILIDEARTPLIISGVGDKSTDLYTRADAFVRRLKVKVFTELDDKEQTDDIEADYIVDEKANTATLTASGVKKAEEFFGIQNLSDPDNMTISHHINQALRAHGLMKRDRDYVVKDDQVIIVDEFTGRLMYGRRYSNGLHQAIEAKEGVKVERESKTLASITFQNYFRMYRKLSGMTGTAQTEEQEFRSIYNLDVVVIPTNMPVIRVDHPDSVYKNERGKFNAVINQVIECHKKGQPVLIGTISIEKSELLSSMLKRHGIPHQVLNAKYHEKEAEIIAQAGKLGAVTIATNMAGRGTDILLGGNPEFMAKQEMRKRGFREDVINQATGFNDTNDPEILEARKVYRELYEGFKKITDAEREKVVAAGGLFIIGTERHESRRIDNQLRGRAGRQGDPGESRFYISLEDDLMRLFGSDRLMGMVEALGLEEDQPIEHKMLSNAIENAQKRVESRNFAIRKSVLEYDDVMNKQREVIYAQRRKVLNGENLKENIVKMMENIADYIVNLFCSENPHPDFWDWEGIRSYTEKAYVPEGTLDFSKEQMEDLNKEKLRQIILDSMLKRYEEKEKEFGSELMRELERVVLLRVVDQKWMDHIDDMDQLQHGVRLRAYGHKDPVIEYKFESFEMFEEMNRNIQSDVVRIILNTHIDRNRMPQRQKVAEPVTASHGEEVRKPVVKRNKVGRNELCPCGSGKKYKKCCGIDE | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 104612
Sequence Length: 910
Subcellular Location: Cell membrane
EC: 7.4.2.8
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A5N3B2 | MKLFQKIFGSYSQREVKRIMPIVDKIDALDSKVQALSNEQLRNKTDEFKERLDKGESLDSILPEAFAVVREVGFRTVGLKQYREQLIGGIVIHQGRIAEMKTGEGKTLVATAPAYLNALTGKGVHIVTVNDYLAKRDRDTMAPIYEALGLKVGVILHDMSQSQRQEAYNCDITYGTNSEFGFDYLRDNMVIYKEERVQRKLNFAIVDEVDSILIDEARTPLIISGEGEKSTEFYNIANGFAKSLEKEDYKVDEKANAVMLNDTGIKKAETFFSLENYADPENMEIQHYVVQALKANYIMKRDKDYMVKNGEVLIVDEFTGRMMEGRRYSDGLHQAIEAKEGVKVERESKTLATITYQNYFRIFNKLSGMTGTAQTEENEFRHIYGLDVIVVPTHKPIAREDFPDVVYKSAKGKFKAIADEIYETYKKGQPALVGTVSIEKSELLSDMLKRKGVPHQVLNAKFHEKEADIISYAGQKGTVTIATNMAGRGTDIKLGKGVVALGGLKIIGTERHESRRIDNQLRGRSGRQGDPGMSRFYVSLEDDLMRIFGSDRLQGIVEKLGLKDDEAIESKMVSNAIENAQKKVEGNNFDIRKTLLQYDDVINKQREIIYKQRSQVLEGEDLKNDVQDMIKSLINSIVDSHISGIEEEFEDEIVKLIEYMEDVYVPKDSVKKEDIINLSNEAIKDKFIDIAQKIYEQKEIEFTSEQMREIERVILLRVVDTRWMDHIDDMEHLKRAIGLRAYRQQEPAQAYQFEGSEMFEEMIYNIKLDTVKYLMHVQIERAPERERVVKNVITNQESDSIKKTPVKREKTVGRNDLCPCGSGKKYKNCCGRTV | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 95305
Sequence Length: 834
Subcellular Location: Cell membrane
EC: 7.4.2.8
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A0Q2X7 | MGLFEKIFGTYSSREIKKIIPIINKIDSYEEEFKKLTDEELRNKTDEFKDMLAKGKTLDDILPEAFAVAREASARVLGMRHFREQLIGGIVLHQGRISEMKTGEGKTLVATLPAYLNALSGKGVHVITVNDYLAKRDRDQMSQLYGFLGLTTGVIVHDLDNEQRREAYNCDITYGTNNEFGFDYLRDNMVIYKEERVQRKLNFCIVDEVDSILIDEARTPLIISGEGDNSTDFYKVADFFAKTLKEDDYTVDEKTNSVILTEQGIEKAEKFFHIDNYGDGDNMQIQHHVVQALKANYTMKRDKDYMVKDNEVIIVDEFTGRLMEGRRYSDGLHQAIEAKENVKIQKESKTLATITFQNYFRMYTKLSGMTGTAQTEEAEFREIYGLDVIVIPTHRPIARIDAPDVVYKSEKAKFKAIVNEIAETYKKQQPVLVGTVSIEKSELLSDMLKRKGVPHQVLNAKYHEKEAEIISHAGEKGMVTIATNMAGRGTDIKLGEGVEEVGGLKVIGTERHESRRIDNQLRGRSGRQGDPGYSRFYVSLEDDLMRIFASDRLQGVVEKLGLTDEDAIESRMVSNAIENAQKKVEGNNFDVRKSVLQYDDVMNQQREVIYKQRSQVLEGESLKEDIQEMIRSVISEAVDAHMSGLDETLEEDLEKLLAYLQEIYLPKNVVTVDELKIKSDDEIKEILIDIAEKMYSEKEEEVTPERMREIESVILLRIVDTKWMDHIDNMDHLRQGMGLRAYRQQDPVQAYQFEGSEMFDEMINGIKTDTVKYLFHIQVEKNIERERVARETSTNINDGEGGSHEPIKRKEEKIGRNDLCPCGSGKKYKNCCGR | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 95455
Sequence Length: 834
Subcellular Location: Cell membrane
EC: 7.4.2.8
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Q0SR11 | MGLFDKIFGSYSDREVKRITPIVDKIDSLGPEMEKLSDEELKQKTFEFKDRYAKGESLDDMLPEAFAVCREASTRVLGMKHYREQLIGGIVLHQGRIAEMKTGEGKTLVATLPVYLNAIAGKGVHVITVNDYLATRDKEWMGQLYEFLGLTTGVIVHGLTNDQRREAYNADITYGTNNEFGFDYLRDNMVIYKEERVQRPLHYCIVDEVDSILIDEARTPLIISGAGSKSTDLYKIADFFVKKLREEEDYTIDEKAHAAMLTDKGVAEAEKAFGIENYADANNMELQHHITQALKANYVMKRDKDYMVKDDEIAIVDEFTGRLMEGRRYSDGLHQAIEAKEGVKVQRESKTLATITFQNYFRMYTKLAGMTGTALTEETEFREIYGLDVVVIPTHRPVQRQDHSDLVFKTAKGKYDAIVEEIIETHKTGQPVLVGTTSIEKSEYLSSLLKKKGVPHKVLNARYHEQEAEIVSHAGELGNITIATNMAGRGTDIKLGEGVLEVGGLKIIGTERHESRRIDNQLRGRSGRQGDKGHSRFYISLEDDLMRIFGSEKLQAVVDRLGLEETEAIESKMVTKSIENAQKKVEGNNFDIRKTLLGYDDVMNKQREVIYKQRSQVLEGENLEDSVQAMIEDVITNAVQAHLGNIDEDDFEKELGDLIKYLEDIMLPHGKFTVEELKTNSNEEITRKFIECAREIYKEKEEFVGSEQMREIERVIILRVVDTKWMDHIDDMDHLKQGIGLRAYKQQDPIQAYQMEGSAMFDEMINNIKIDTVRYLFHVKVEAEKPQRERVAKETGASHGGDSQEIKKKPVKKEPKVGRNDLCPCGSGKKYKSCCGREVV | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 95560
Sequence Length: 840
Subcellular Location: Cell membrane
EC: 7.4.2.8
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Q7NC50 | MLINWFKLISPKNRILKRATLAAKQVDALKDEMRALSDEQLFNKTEYFINELKNNKTTDDILVEAFAVIREVVYRETGNFAYLVQLIGAYVVHQGDFSEMMTGEGKTLTLVLAAYLNMLEKKGVHIVTVNEYLAERDAEQARRIFARLNLTVGCNKANLAPHLKKEAFDCDLTYTTNSELGFDYLRDNMVRNYRDKKIRGLHFAIVDEGDSILIDEARTPLIISGQPKKDFRMYFDADKFVETLSESDYKIDPESRSPSLTEKGITKAEKHFKINNLFDLENSDLFHKIGNALTARKIFQNGKEYIVRDDKILIVDHFTGRILEGRSYNGGLHQAVQAKERVPIEAENVVVATVTYQSFFRMYKKLAAVSGTALTESEEFLKIYNMVVVPVPTNRPVIRKDHPDFMFGNLKTKWEAVVNEIEKIHKTGQPILVGTGSVEDSETLHQMLLEKNIMHEVLNAKNHAREAHIIAKAGEVGSVTISTNMAGRGTDIKLGKGAKELGGLYVIGTERHESRRIDNQLRGRSGRQGDIGESRFFISFGDPLFKRFAQDRILKAQEKLASDYFDSKFFSRFLTMTQKKVESVNFDMRKNLIDYDHVLANQRELIYKQRDKILIASDLTEVVDRMAQNFVEGFVETFKDQANQTMVNPIELSIAVQKELLQGEEVTASQFYNQTLLAAKQTVLKLVKDAISKKIEVMTVGIANNVFRDIIIQQMDDAWIHHLDQMLKLREGVSLRSLEQTSPLNIYVEESKKLFDLMLNKIAKNVILAVCAIINPTRNVDINVEQEHRRLEALKRLEEIKKLEELQNNNNEPAKVLFKFPDQHGNMIEREVPVDNLIQLVDGQIIQAQVAEEPKQELNQLEKADQLDQTLIEAKLAEQQEQKNNSATDK | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 101679
Sequence Length: 890
Subcellular Location: Cell membrane
EC: 7.4.2.8
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P47318 | MAIFNFLKLISPKNRILSKANRIASEVESYKNYYRNLTDQQLFEESNKLVDLVTKQNYTILDVCVAALALIREVVYRETGEFAYRVQIIGAFIVLSGDFAEMMTGEGKTLTIVLAAYVSALEKRGVHVVTVNEYLAQRDANNAMKILKRVGMSVGCNFANLSPQLKQAAFNCDVTYTTNSELGFDYLRDNMVHSYQDKKIRELHFAIVDEGDSVLIDEARTPLIISGPSKNEFGLYVAVDRFVKSLTEQEFKIDPESRAASLTELGIKKAEQTFKKENLFALENSDLFHKIMNGLTAVKVFEQGKEYIVRDGKVLIVDHFTGRILEGRSYSNGLQQAVQAKEYVEIEPENVIVATITYQSFFRLYNRLAAVSGTALTESEEFLKIYNMVVVPVPTNRPNIRKDRSDSVFGTPQIKWMAVVKEIKKIHETSRPILIGTANIDDSELLHNLLLEANIPHEVLNAKNHSREAEIVTKAGQKNAVTISTNMAGRGTDIRLGEGVAEMGGLYVLGTERNESRRIDNQLRGRAARQGDKGETKFFISLGDSLFKRFAHDKIERAISKLGNETFDSAFFSKMLSRTQKRVEAINFDTRKNLIDYDHVLASQRELIYKQRDKFLLANDLSEMIDKMLEKFVQQFCDQYRNQKNQNLINHIALAEALNLEMNMQNTINPKVFENMTFDVAVDKTRNLVAKKISDKVNVLTKPIALNRFRDIIITSMDKHWTEHLDSVFKLREGVVLRSMEHTSPLNVYIKETDILFKTMLQKIAQDVIVQIANLTTPDEFDHSLMQANALKKLAAIKADEKSNQE | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 91585
Sequence Length: 806
Subcellular Location: Cell membrane
EC: 7.4.2.8
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Q6MUE3 | MVSDRRLLKKFGKIADKIIALEPQMRQLKDEDFILKTQEFKQMLENGKSLDDILIEVYAVAREAARRVLGLNAYKMQLIGGIILNSGDIAEMRTGEGKTLTGIFPAYLNALSGKGVHIVTVNEYLSRRDSEINGKVFDLLGISVGLNGSSLTKTEKREAYNKDITYTTNAELGFDYLRDNMVSDYSLKVQRKLNYCIIDEADSVLIDEARTPLIISGGTSTRINLYKAANNFALTLKEHDDLDIDLESKQVYLNEQGMKKANEFFSLKNLFAIENTEIFHLIMNALKAQFAFKEGVEYTVRDNEILLIDQFTGRIMHGRSYSDGLQQALQAKENVDIEEETVTLATITYQNFYRLYSKIAGMTGTAKTEEEEFIKIYNTRVIQTPTNKPVIRKDEPDLTFGTKNAALKKLVEDVLEAHKKGAPILIGTTSVESSEQIARYLKKANLKFETINAKNHDREAEIVAKAGEIGAITLATNMAGRGTDIKLAKGVAELGGLRVFGVERNEARRIDNQLRGRSGRQGDPGLSRFYISMDDDLMMRFTAPKTRQRFKALGDDYIKSKMFTRAVTNAQKKLEGMNFDQRKNVLDYDNILAQQREIIYAQRDDILEANDLSVVIEKMQITAAYELIEKHSTLVHGEKTINKKELLEVIDGILVPKNKFRIDDFNNKEKMDLAVEIAEAMMQLYKARISDIPDDVIIVMERKIILDAFDKHWTKHLDIAGKLKSGIYLQQYAQNNPLAIYIEQATNLFNKMKINIANEVVENLANVILRVVEDEEQREERIEVTDKDIEEILFETGLQPSDINNKAINQRFDELEEEFKDDKQKLRRLRIQRDVMLGLVLELERRAEMIISPQNDQQAITQLIKELQNDIDIASITIDQIHQNFNNMVEQINDPEKLKHLVIAKDVLLQLVARMDDIKEQEKQTRKKKKKKPHEDESSKTKIG | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 107797
Sequence Length: 944
Subcellular Location: Cell membrane
EC: 7.4.2.8
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Q98RA6 | MIKKLKEIPFFKSTEMKIAEKTLQQINDLEPSVVNLTDEELQNKTDEFVRRIQEGETLEHIRPEVFAVSREATKRVLKKRPYDVQMLGGIILDLGSVAEMRTGEGKTITSIAPVYLNALEKKGVIVSTVNEYLAERDAAEMGEVFSFLKMTVGVNKPSMSPEEKKQIYQCDITYSIHSELGFDYLRDNMVTNINDKVQRGLNYILLDEVDSILIDEARTPLIISGGESSSSYMYEVANQFARTLQPGDYEIDEESKTIKLVDSGIDKANKFFTLSNLYDIKNSELVHRIQNALRANFIMKKDVEYIVKDEKIELIDAFTGRIMEGRAYSEGLQQAIQAKEFLEIESETKTLATITYQNFFRMFKKLSGMTGTAKTEEQEFIDIYNMRVNPIPTNLPNIRVDDEDSIYWGTRQKLNAILKEVKQVSKTGQPILIGTSQIEQSEQLHQLFDQNGIVHTVLNAKQNEQEANIISQAGQLNAITIATNMAGRGTDIKPSKEALAVGGLYVLGTDKSESRRIDNQLRGRSGRQGDIGYSKFFLSLDDQLILRFAGADKLKEIFPKSEEALNSKQLKRHFSNAQKKIEGFNYDSRKTVLNYDDVIRQQRELMYSQRDLILVSEDLLFVIERMVFRSVDDVLKNSMFLLKNGGFDYTKLTEYINDQWLKPFDFKFEESKLSHLHEKDLAEYIFQNLMEQYMIVRQRLIDSFGEDSILYHERSILISTIDSYWQNHINSMDKLRSNSNMVQYAQKNPYQVYTQKGSKKFERLIVEIALQSSVKLFNNPSAYRQDQMEEVMIEGYTQEFIDKIPESEREYFKTLPQDLKSKIVKNLIQLEQSIAMVESNDQSQDLQSITIDILPDQNLNNSSDEAK | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 99775
Sequence Length: 867
Subcellular Location: Cell membrane
EC: 7.4.2.8
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A3QIL3 | MFGKLLTKIFGSRNDRTLKTLGKIVTKINALEADFEKFSDEELKAKTAEFKQRLESGQTLDDVMPEAFAVVREASKRVFEMRHFDVQLLGGMVLDSNRIAEMRTGEGKTLTATLPAYLNALTGKGVHVITVNDYLARRDAENNRPLFEFLGMTVGVNIAGMGQAEKKMAYASDITYGTNNEFGFDYLRDNMAFSPNERVQRPLHYALIDEVDSILIDEARTPLIISGAAEDSSELYIKINTLIPHLIRQDKEDTEEEIGDGDYSIDEKAKQVHMTERGQEKVEVLLTERGMLAEGDSLYSAANISLLHHVNAALRAHTLFEKDVDYIVQDNEVIIVDEHTGRTMPGRRWSEGLHQAVEAKEGVHIQNENQTLASITFQNFFRQYEKLAGMTGTADTEAFEFQHIYGLDTVVIPTNRPMVRKDHADLVYLTAEEKYDAIIKDIIDCRDRGQPVLVGTVSIEQSELLHSMLKKAKIPHEVLNAKFHEREAEIVAQAGRSGAVTIATNMAGRGTDIVLGGNWNMEIDALENPTAEQKAKIKADWQVRHDEVVAAGGLHILGTERHESRRIDNQLRGRSGRQGDAGSSRFYLSMEDSLMRIFASERVSSMMKKLGMEKGEAIEHPWVSRAIENAQRKVEARNFDIRKQLLEFDDVANDQRQVVYAQRNELMDAESIQDTIVNIQADVVNGLIDQYIPPQSVEELWDIAGLETRLEQEYALRMPVQEWLDKEDDLHEETLRERIVEIWVKAYKAKEEMVGAQVLRQFEKAVMLQTLDGLWKEHLAAMDHLRQGIHLRGYAQKNPKQEYKRESFELFQQMLESLKHDVISILSKVQVQAQSDVEEMEERRRQEEAKVRRDYQHAEAEALVGAEEAQALAATQPVVREGEKVGRNDPCPCGSGRKYKQCHGKLS | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 102863
Sequence Length: 907
Subcellular Location: Cell inner membrane
EC: 7.4.2.8
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Q8E9Q5 | MFGKLLTKVFGSRNDRTLKGLQKVVNKINALEADYEKLTDEQLKAKTAEFRERLAAGASLDSIMAEAFATVREASKRVFEMRHFDVQLLGGMVLDSNRIAEMRTGEGKTLTATLPAYLNALTGKGVHVITVNDYLARRDAENNRPLFEFLGLTVGINVAGLGQQDKKDAYNADITYGTNNEFGFDYLRDNMAFSPQERVQRPLHYALIDEVDSILIDEARTPLIISGAAEDSSELYIKINTLIPNLIRQDKEDSEEYVGEGDYTIDEKAKQVHFTERGQEKVENLLIERGMLAEGDSLYSAANISLLHHVNAALRAHTLFERDVDYIVQDGEVIIVDEHTGRTMPGRRWSEGLHQAVEAKEGVRIQNENQTLASITFQNYFRLYEKLAGMTGTADTEAFEFQHIYGLDTVVVPTNRPMVRKDMADLVYLTANEKYQAIIKDIKDCRERGQPVLVGTVSIEQSELLARLMVKEKIPHQVLNAKFHEKEAEIVAQAGRTGAVTIATNMAGRGTDIVLGGNWNMEIDALENPTPEQKAKIKADWQLRHDAVVAAGGLHILGTERHESRRIDNQLRGRAGRQGDAGSSRFYLSMEDSLMRIFASDRVSGMMKKLGMEEGEAIEHPWVSRAIENAQRKVEARNFDIRKQLLEFDDVANDQRQVVYAQRNELMDAESIADTIQNIQDDVISAVIDQYIPPQSVEELWDVPGLEQRLHQEFMLKLPIQEWLDKEDDLHEESLRERIITSWSDAYKAKEEMVGASVLRQFEKAVMLQTLDGLWKEHLAAMDHLRQGIHLRGYAQKNPKQEYKRESFELFQQLLNTLKHDVISVLSKVQVQAQSDVEEMEARRREEDAKIQRDYQHAAAEALVGGSDEDDAIAAHTPMIRDGDKVGRNDPCPCGSGRKYKQCHGKLS | Cofactor: May bind 1 zinc ion per subunit.
Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 102623
Sequence Length: 908
Subcellular Location: Cell inner membrane
EC: 7.4.2.8
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Q57575 | MDISKLLKDRKILILIIFVTLSVFLIVFKGLDFGIDLSGGTIIVLKAEKPMSDKEIEATIKIITERLNYNGLNDVVIYPRGNDEIIVEIPKSCDTDRIIKILKQQGVFVAKIDNITAYTGSDVQNVELPTKIPQGETWAYGVPFELTLEGAKKFAEVAKGKAYHKVELYMDGKLISAPVLSPDLADGKPHPQQVITVGAYPPTKEEIDEAMAIYSALKSGALPVKLDIEYISTISPEFGKEFLKGTAIALLLAFIAVGIIVSIRYKQPKIAIPILITCISEVIIILGFASLIDWKLDLPSIAGIIAAVGTGVDNQIVITDEALKRGAGKIRASIKRAFFIIFASAATSIAAMLPLFVLGVGMLKGFAITTIAGVLIGIFITRPAFARIIEEMFKKF | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43052
Sequence Length: 396
Subcellular Location: Cell membrane
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Q8TWM4 | MSGLGWMKENWRLLVITAVWIVAATSLAVKGVNLGLELKGGTMVIAKTDHPVSKKEMDQTVTVLESRLSTFGFKGIKIQPVGRDHIIVMLPGTPPKEAVELITKPGRFEAKYKGKTVITGQDIESVESPRIERVEGGYQWSVPFRLTAEGARKFAEVAKNAPGQPIDMYLDNKKVSSPRISEDLAMAAASGHMEREIEIVGGAKTKEQAEREAKEIMAVLRSGQLPAKLVPEGVYSVSATLGQNFLKMAMIAGAIAFAAVSVIIALRYRDIRISGPILFTGSSEVVFLIGLASLTGFTIDLPALAGIILSIGSGVDDLIVITDEIVRGERRKEEVTLRQRIKRAFSVVLASFATLAAAMAVLFVAGMGLLKGFAIMTIAGAFYGVVITRPVYADLLKKILGTE | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43385
Sequence Length: 403
Subcellular Location: Cell membrane
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E1RHR1 | MAEEKSTLGKIFTDWQVLIVLVLVILSVLSIYAIPPALDKGISGNLQLGLDLVGGSWIQLSFKSEVIGYESDMSQSDFITQLSEKLDADVIPVTSSSVEIREYYTKEELESVLAGMGAKLVTYEQGISKETADTVKGILEDKVNTLGTKDVQINTLTGANDVTKYVRVELAGTDINTAQEIVSSQGKFEIRIVTSGNETERVLSGDAVTSVSTPSQRNNYWGVGFTLSAEGAEALRDACIQYGAVTDPDSHNLVMLLDGEQVYSAPLSSDLAAKLSKGPVNDLSASTGYGEEGYNDAEVLEIHLRAGALPVDVEIAGSSSVTAERGEFIQIVCIAAAILGLLAVAFMVYYRYREPSIVVPMILVNLSEIIILLGIARYIQQLDLASIAGLIAVIGTGIDQLVVITDEVLHEGRVPSPSLYLKRFKRALGIITVSASTTIFAMLPLALMDLSTLKGFAIITILGVLIGVIFTRPAYGKIIMAILSKKPAK | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52404
Sequence Length: 489
Subcellular Location: Cell membrane
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O26937 | MNRKVSKFLKDYRVILLIVLVAASITAISTMGIQQGLDLQGGSLIQIQLERPVDAATMNTVTSVLDKRLNIFGVKDVKVRASGDQNVIVEIAGVQPDQVADIVGKPGKFEAKIGNETVLTGTDIVSVQPPIITGNEWEVPFRLSTDGARKFAEAARGKAGEPVKMYLDDRLITAPEISAEVATGKPVTDVRITGAENSKAEAEVQAKEIETLLKSGSLPVKVKIVGVSSVSPELGKQFAEGAVIAGLLAVLAIAVILIVRYRSPILVLPIFFTTLAELLLILGAAAVIRWNIDLAAIAGILAAIGTGVDDQIIITDEVLSGEGRRTRRKFRIKDAFFIIFASAGTLIAAMLPLAYIGFSRGATGIGLLAGFAFTTVLGVIIGVFITRPVYARFIETFNVAGRK | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42862
Sequence Length: 403
Subcellular Location: Cell membrane
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P38387 | MASSSAPVHFGRYLSMFLVLFIGVYLLAFLTGDKRVVPRLGIDLQGGTRVTLTARTPDGSRPSREALSQAQQIISSRVNGLGVSGSEVVVDGDNLVITVPGNDGNEARNLGQTARLYIRPVLNSLPVQRGQDPKPGSPAGTLPNFAPMPPDHPGAQPRPYLQDPTSSPSSDPMPSPVPTGAALPGEVPSVEQPAPPDPRKDLAERIAEEKKWRQSTKQSIQFLALQFESTHCDKDDILAGNDDPNLPLATCSTDHNMAYLLAPSIISGDQIQNSTSGMNQRGVGYVVDLQFKSAAADVWADFTAAHIGTQTAFTLDSEVVSVPVINEAILGGRTQISGGDPPFTAATARQLANVLKYGSLPLSFEPSEAQTVSATLGLTSLRAGLIAGAIGLSLVLLYSLLYYRVLGLLTAFSLFCSGTIIFAILVLLGRYINYTLDLAGIAGLIIGIGTTADSFVVFFERIKDEIREGRSFRSAVPRGWVRARKTIVSGNAVTFLAAAVLHFLAIGQVKGFAFTLGLTTILDLVVVFLVTWPLVYLASKSPLLARPAYNGLGAVQQVARERRASAKTGRG | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60719
Sequence Length: 571
Subcellular Location: Cell membrane
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P9WGP0 | MASSSAPVHPARYLSVFLVMLIGIYLLVFFTGDKHTAPKLGIDLQGGTRVTLTARTPDGSAPSREALAQAQQIISARVNGLGVSGSEVVVDGDNLVITVPGNDGSEARNLGQTARLYIRPVLNSMPAQPAAEEPQPAPSAEPQPPGQPAAPPPAQSGAPASPQPGAQPRPYPQDPAPSPNPTSPASPPPAPPAEAPATDPRKDLAERIAQEKKLRQSTNQYMQMVALQFQATRCESDDILAGNDDPKLPLVTCSTDHKTAYLLAPSIISGDQIQNATSGMDQRGIGYVVDLQFKGPAANIWADYTAAHIGTQTAFTLDSQVVSAPQIQEAIPGGRTQISGGDPPFTAATARQLANVLKYGSLPLSFEPSEAQTVSATLGLSSLRAGMIAGAIGLLLVLVYSLLYYRVLGLLTALSLVASGSMVFAILVLLGRYINYTLDLAGIAGLIIGIGTTADSFVVFFERIKDEIREGRSFRSAVPRGWARARKTIVSGNAVTFLAAAVLYFLAIGQVKGFAFTLGLTTILDLVVVFLVTWPLVYLASKSSLLAKPAYNGLGAVQQVARERRAMARTGRG | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60267
Sequence Length: 573
Subcellular Location: Cell membrane
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A9BG79 | MRNRRIRILFTVIVFVFALLGLILPLSGNVNDISILRFFPNINLGLDIQGGVLLEYSFDVPEGVNTSEVVDNVITVLRRRMDNAGYTEAIVSEVVSGGESRVRVEIPGISDTQRAEELIGSKGKLYFAEVLEVVESTTTPEITRNRTIQINGEEIEMYSYVKDSNNPNLWYRVKNVFEFGDAPFQITGLDVTDAVASLNSQGAGFVVNLNFSNEGRQKFELATANLVNERIAIILDDEVIIAPVVRERISQGRAEISGIESMEEAQNIAVLIKSGNLPVDLVKYQERTLGPTLGRDIVTTIINAGIIGLIIVMIYMIIFYRWMGVIADIALIYNTFLLMGILSWTGAILTLPGIAGIILTFGTTVDGNIIIYERIKEELRIGRPPLTAVKFGFNKVFSTIFDANITTILAGLVLFFVTSGSIRGFAVTLIIGVLGAMFTNLVVSRLLLESTSHFLKPEKYVKGIVVEKGGTK | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51980
Sequence Length: 472
Subcellular Location: Cell inner membrane
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Q7VCH3 | MARQQGWFALLIALVISAFLLCINLPFQLGLDLRGGSQLTLEVQALNPNEQIKSEQLEAVQSVLDRRVNGLGVAESSLRTIGTNQLILELPGEQEPSKAARVLGKTALLEFRKQKINTKSEMQRLQRIRSQVNNIDLYKKASKDNKSELIENKKIGEQVNDLRVALGLANSSLNEHDQIDQIRQKVNSEIVELFEPSSLTGSDLVSAGRRQEQNLTSWEVTLAFNQDGGEKFASLTKSIAGSDRLLGIILDGESISEASVGEQFKVAGITGGSATISGNFTAESARELEVQLRGGSLPLPVSIVQVRTIGPTLGVDNIRRSLIAALLGLSLVAIFMVSFYRLAGFIAIFALSFYALFNIAIYALIPVTLTLPGVAGFVLSIGMAVDANVLIFERVKDELRRGNTLIRSIETGFSQAFSSIIDGHITTLISCISLFYLGTGFVKGFAATLGIGVFISLFTALSCTRVLLRFFMSYKSLRKTTNFLSENQLPKQLT | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53851
Sequence Length: 494
Subcellular Location: Cell inner membrane
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Q9HXI1 | MLNKYPLWKYLLILAVLAVGFIYSAPNLYPDDPAVQISGASTALQVTQADVDRAAKALTDAGIAVKADSLSKKGGLIRLVKQDDQLPAKEVVRRTLGDDYVVALNLAQTTPEWLRKLGGSPMKLGLDLSGGVHFLLEVDMDKAVDARLKVYESEVKSLLRKERVRYRSLPIQDRAIQLGFTDSESLDKARSLIAKDFRDFEVVPEERNGLQVLRVALTQAKLAEIREYSIKQNLTTVRNRVNELGVSEPLVQRQGANRIVVELPGVQDTAEAKRILGKTANLEFRLAAEPDALKSATETFEFREPRRPPVPLERGVIITGDQVTDASASFDENGRPQVNIRLDGHGGELMNRATRNNVGRSMAVVFIEQKPVTRYTKQMVDGVEKEVAVPAFKEEKQIISLATIQSPLGNQFRITGLDGPGESSELALLLRAGGLAAPMYFAEERTIGPSLGADNIAKGIDASLWGMLFVSLFIIVIYRFFGVIATVALAFNMVMLVALMSILGATLTLPGIAGIVLTMGMAVDANVLIFSRIREELANGMSVQRAIHEGFNRAFTAILDANLTSLLVGGILYAMGTGPVKGFAVTMSLGIITSMFTAIMVTRAMVNLIFGGRDFKKLWI | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67675
Sequence Length: 620
Subcellular Location: Cell inner membrane
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Q8U4B4 | MKWRRILLNFRVIVLIFFLLISITALATRGLTFGLDISGGISITVKLEKPVDSQTMEQVKIALEQRLNTLGVKNIVVEPWGDQFVIVKVANVTEEEADQLIKTIERQGVFYAEFQGIIFATGKDILNVGSVSYDPQHSAWVVPFRLSKEAAEKFAQLALGKAGYPVDMFLDPPVNSTLVVSNRVYEAMLSKTFMLEGDMTLVERIEKAFGIKVVPYANVTPEEIAEIAKGSERIILLDVDGNLSKALKEMGFEVETRSMRSDEDVYDFIKRSLGLYGPYRVSEGLATGNPSTEVMISITAPKTDIQARQDAQVVSVVLRSGSLPVKLSIERIDYISPKLGENFKRQVLVAGIAALLVVGLIVFLHYRKIKIAIPVMFTSFSEVLIILGIAALIRWNLDLPSIAGIIAAIGTGVDQQIVITDELLGEEESRRRVKRSGVLRRMGRAFFIILASATTTIVAMSFLFKFFVGGLRGFAFTTILGVLVGIFITRPAYGEIAKVLIGERR | Function: Involved in protein export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55814
Sequence Length: 505
Subcellular Location: Cell membrane
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O33517 | MLQISLWKRLVILGLCLAALITAAPNMFYARVEGHNDAVSAFEKTGAMTETQEAAKAAWPDWAPSALVNLGLDLRGGAHLLAEVHLGEVYKARMDALWPEVRKVLAAERATIGAIRRVPSPEGELRIQIGERAQIARAVEVARTLASPVVSLTGVGQTDYEVTGEGDTVVFRLSEAEKKATDDRTMQQSLEIVRRRVDAAGTREPTIMREGTDRILIEVPGIGSAQELKDLIGTTAKLTFHPVLSTTSNPNAPVASGNELLPDAERQGLYHLLDEVPVVTGDDLTDARPTTDDNGAPAVSFRFNVSGARAFGDYTAGHIGEPFAIVLDGKVISAPTIQAHIAGGSGIITGRFSIEEATDLALLLRAGALPAGMTFLEERTIGPELGADSVKAGMVASVIGFVAVVAYMIASYGLFGFFSSVALFINIAFIFAVMGAIGGTMTLPGIAGIVLTIGTSVDANVLIYERMREEIRSGKSPVRAIELGFDKAMSAIIDANVTSFLSSAILFVLGAGPVRGFAVTTMIGIAASIFTAIWVVRLMIVIWYGWRRPKTIVI | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58943
Sequence Length: 554
Subcellular Location: Cell inner membrane
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D0MIN4 | MKRNGFKIGVTLALLLLCGYYLYPTVRYALLQRKLNRMSEEERAAFIEANYGTIQSLRERALKLGLDLQGGMHVTLEVRVDALIRELATDVDETFEEVLAAARERARSGDVSLIDAFVEEFERRDPNARLSRYFRNPDAGITRRSSNEEVAAYLRQQAEEAVNRAIEIIRDRVDRYGVTEPVIQKQGTRRIVVELPGVDDPERVRRLLRGTARLEFRLMADPQLLQAALQDIIAYYEPDTTAASETSAVTDTATADTSLAALLGEQPSPERPRNPLLAVMQPVGQGVVFGIVAGPDTAQVNRLLRNPEVQALLPSGIELLYTANPVGTDEQGRPLYYLLGVRKEVELTGEVITDARVEFDELNRPQVSMTMNSEGARIWARLTGANVGKHIAIVLDNVVYSYPVVNERIPSGRSSITGLDSREEAQDIVTVLKSGALPAPVDIIEERTVGPSLGEASIRAGLRSVLTGLLLVALFMIFYYRTGGMIADLALVLNIIFILGILAAFNATLTLPGIAGIVLTIGMAVDANVLIFERIREEQATGKTLRAAIDLGYSKAFSAIFDANITTFFTAAILYSFGVGPIQGFAVTLMAGIAASLFSAIVITRIIFDYLVLERKLMVSVG | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68193
Sequence Length: 622
Subcellular Location: Cell inner membrane
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Q9ZCW8 | MQNLPKWKIVLSIICTVFAIICALPNFIQINSKFLPHDSINLGLDLRGGANLLLDVDFDTYLNDSMENLADTLRKNLRKHKIGYKNLLVRHNNIQLEVRSPEVLKSLKKIINKIDPEIIIGVNKNKIKLRYSESRFNDLLNKVVEQSIEIVRMRVDSTGTKEPTLQRQGNKHILLQVPGSENPSYLKNILGKTAKLTFHLVDENANIEDAIKGHVPLGSMLIKGDSKHHGEYYIVIKKKVLLSGAHLTKASASFDQNSQPIVAFSFNNLGSKIFGEITKNNTGKRLAIVLDNKLLSAPIINGAIIGGNGIITGNFTIESANELALLLRVGSLPTPLKIIEERSIGPNLGADSIESGKKAGLIGFVAVCIFMILSYGVIGLFANIALILALLYILALLSLFQATLTLPGIAGIILTIGMAVDANVLIYERIKEELHKGVSNLYAIRTGFESAFATIIDSNITTLIVAFALYIFGVGAIKGFAVALTIGIISSMFSAIIITKLLIDVWVKYFKPKKLGLL | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56712
Sequence Length: 518
Subcellular Location: Cell inner membrane
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D1AMK9 | MEIKTSRIVILILVVVIPAILIFRNPINLGLDLRGGTSVVLEAQEEDGKKLQPDTMDKVREIVQRRVDGLGVSEPVIQKSGENRLIVELAGVKDAQEAIDLIGTTAKLEFKIKTGDNSYGPTVLDGSAIKNAYVQQDQFGKPMIGFELNDEGAVKFAEITRTNMGKQLAIMLDGKEQSAPVIQSEIPGGKGSISGSFTYESAQNLANLLKAGALPVNIQIMETRSVDASLGAESIKATKMAAMIALVLVSLFMLAVYRVAGFVADLALCVFGILTAGLMCAIGTTLTLPGIAGFILSLGMAVDANVIIFERIKDEIMEGKRFQDCIDDGFNRAFPAILDGNITTLLITMVLFFFGTGPVRGFAVILTIGVLVSMFTAIFITKIIVKIFVNIFHLNGEKLFGLKGVE | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43634
Sequence Length: 406
Subcellular Location: Cell inner membrane
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Q9HMD1 | MSSGQNSGGLMSSAGLVRYFDSEDSNALQIDPRSVVAVGAFFGLVVLLAQFFA | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5528
Sequence Length: 53
Subcellular Location: Cell membrane
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O25847 | MTSALLGLQIVLAVLIVVVVLLQKSSSIGLGAYSGSNESLFGAKGPASFMAKLTMFLGLLFVINTIALGYFYNKEYGKSVLDETKTNKELSPLVPATGTLNPALNPTLNPTLNPLEQAPTNPLMPQQTPNELPKEPAKTPSVESPKQNEKNEKNDAKENGIKGVEKTKENAKTPPTTHQKPKTHATQTNAHTNQKKDEK | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21460
Sequence Length: 199
Subcellular Location: Cell membrane
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A8ABD7 | MARKRRKGGEGLVTAIGLVRFYEEVEEKIKVPPEAVIGAAFALSIMTIALDLLLKAAR | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6312
Sequence Length: 58
Subcellular Location: Cell membrane
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A6UWW7 | MSKNKQDAGLSTSAGLVRYMDEDASKIKIAPEKVLGITISIMVLLFILNYGLLA | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5842
Sequence Length: 54
Subcellular Location: Cell membrane
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P60459 | MAKRSGSGLQSSAGLMRYYEADKNAVHIQPKTVLIVGALAGIAVLFLSAVNGFWP | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5806
Sequence Length: 55
Subcellular Location: Cell membrane
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Q12U86 | MAQKKKSSGSGLMSSAGLMTYYDADKKAIHVQPKTVFIFGAICGIVILAFSAGFGLWP | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6140
Sequence Length: 58
Subcellular Location: Cell membrane
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P60460 | MSKREETGLATSAGLIRYMDETFSKIRVKPEHVIGVTVAFVIIEAILTYGRFL | Function: Subunit of the protein translocation channel SecYEG. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5959
Sequence Length: 53
Subcellular Location: Cell membrane
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Q8TYT4 | MGKKMEKKRAEMPPARAGILSFWDEEAPGIKIDPDYILYACFAVAVLLIIAHTMAAV | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6293
Sequence Length: 57
Subcellular Location: Cell membrane
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P60461 | MAKKDKKTLPPSGAGLVRYFEEETKGPKLTPEQVVVMSIILAVFCLVLRFSG | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5724
Sequence Length: 52
Subcellular Location: Cell membrane
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A0B9N5 | MAKKKGEGPGLMSSAGLMRYFESEETSIKLDPKMVIGAGIASGVAIMALNITFGLWP | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6002
Sequence Length: 57
Subcellular Location: Cell membrane
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P66792 | MELALQITLIVTSVLVVLLVLLHRAKGGGLSTLFGGGVQSSLSGSTVVEKNLDRLTLFVTGIWLVSIIGVALLIKYR | Function: Involved in protein export. Participates in an early event of protein translocation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8163
Sequence Length: 77
Subcellular Location: Cell membrane
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