ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
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stringlengths 117
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A0A9E0H175 | MSNFQLSLIIIGALVLIVVIAYNAWTTRRNTPKRASPREGDKGQEPAVRQEPAFDGAGLGQVDAAQASAAEPHFEGHAVDARDALDLPVPQPERRGGLDPLIDVIAPIVAEQQVSGDAALAALPPTRRAGSKPFAIEGLNLASNQWEQPQPGQRYVQFQAGVQLANRVGALNEIEFSEFVMKAQAFADAINATPDFPDMLHEVARARELDQFASDHDAQLSFMLRARQAAWSPGYVQQNAARCGFVAGAIPGRLVLAASGVGLPPMLTLGYDSQAAMSDDPEQSAVRDIMLSLDIAQVHRSEQPFARLREVAAQLAEAMDGVLCDQNGTPLPAMTMEPIAADLEQLYDQLDSHELSAGSVLARRLFS | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 367
Sequence Mass (Da): 39433
Location Topology: Single-pass type I membrane protein
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A0A945XAH6 | MRSSLQRLSIVVAVWLLVGCSMAPPHSTTAALQLDWETRKAQLQQLQQWQVDGRVALRMGKEGGQSGFSWKHKSALQQQFNLSGLLGAGAVELLVGGAGAQLTTAGESYRGDRASQLLFEVTGWKIPVEAAQYWIKGLPDPTLELESLVLDEANRLQQLQQAGWRIEIRRYQQLNQMELPAFVVMEQGDVRLKLRLNRWRLQS | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Subcellular Location: Cell outer membrane
Sequence Length: 203
Sequence Mass (Da): 22821
Location Topology: Lipid-anchor
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A0A8T7ACY8 | MPRIVVIAGESSGDRLGASFIRSAALSRPDLTFEGVAGPEMRAAGCKPWFDAHDLAVMGLFEVIRHLPRILRIKREIQKRLLADPPDVLLGIDAPDFNLRVEKVARRAGIPTVHYVCPSVWAWRESRVKTIRKACDRVLCLLPFEVPFLQRHEIDGRFVGHPLADDIGDSVDRRAARRKLALGDGPVVAILPGSRGSEVTRLGPVFAATAAWIERHKPGVTFAVPAATPALRGLIEQQFASSAPQCEVRIVDGNSCDVLAACDTALLASGTVTLESMLMKRPMVVAYKLSPLSYWVGRIFRLIKVKYMSLPNLLADAPLVPEFLQRDASPGALGGAVLELLDSPDGCAGLIETFGKLNRQMRRSAGERSAAEVLDVAGLAVANQVPSDDNESGDSGRAAMTPVTEKR | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Length: 407
Sequence Mass (Da): 44047
|
E3MA55 | MVSFVQLVVKIREIFEQKLIDIDEVMRLLASYNSNMREWRRFAIFDHNKYTRNLVDVGNGRYNLMILCWGPGMASSVHDHTEAHCFVKILDGELTETKFGWPRKRHVPLDVSENKTYKKNMVSYMNDDLGLHRMENLSHSNGAVSLHLYIPPYDTCNAFDERTGKKTKCTVTFYSKYGRKIDHRGSKNG | Cofactor: Binds 1 Fe cation per subunit.
Pathway: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.
EC: 1.13.11.20
Catalytic Activity: L-cysteine + O2 = 3-sulfino-L-alanine + H(+)
Sequence Length: 189
Sequence Mass (Da): 22040
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A0A956PZN6 | MQGQLFQQIRRTSDRVGLREIQFYAYHGHRREENSLGQRFLLSLDAWLDLSTAGHSDQLGDTLNYFELHRLVMEWVTAHRFSLLERLVEGLADAIFAAHPEVDALRLCVQKPQPPIPDFFGFVEVEICRVSPRLLTGKTAP | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 141
Sequence Mass (Da): 16218
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A0A2H0ZLI7 | MLLRCPLKSLLRPPRRSYATSVLQKLNPHPHIPEPFAYPQSQPEINDDIYVAMSSGVDSSVTAALLSKMHKNVCGVYMANWSQSAKCTEGEWSDVQRVCDHLQIPCERVNFEKEYWADVFTPMLEMYENGFTPNPDLGCNTYIKFGKMIEHLAARYDVNSKNWWLATGHYARVEKASANKYNLLRAYDGNKDQSYYLANIPGKVLPRILLPLGHYTKPQVRKMAAEFGLHTASKADSQGLCFVSPDHTKFRHFLDEFLPPKPGNIITEDGKVWGKHQGIWHATIGQRSGVSMPQGNPKYSGVWFVSEKRIATNEIVIVKGGQNEKLFSKLLEVSNWAWINCDPQEDLEELTLQFRSLQDPVEVSSISVGEKSVTIELKDPQRAMAPGQNAVLYKGNKVLGAGVLMKTFH | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
EC: 2.8.1.14
Catalytic Activity: 5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Length: 409
Sequence Mass (Da): 46144
|
Q5ZMF9 | MSDLGDWFRSIPLITRYWFAGSIAVPLIGKLGLVSPVYLFLWPDAFINRFQIWRPITATFFFPVGPGTGFLYLVNLYFLYQYSSRLETGAFDGRPADYMFMLLFNWICIVITGLVMDMQLLMIPLIMSVLYVWAQLNRDMIVSFWFGTRFKACYLPWVILGFNYIIGGSVINELIGNLVGHLYFFLMFKYPMDLGGRNFLSTPQFLYRWLPNRRGGVSGFGIPPASMRRAAEDQQGGGRHNWGQGFRLGDQ | Function: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 251
Sequence Mass (Da): 28909
Location Topology: Multi-pass membrane protein
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A0A2E1X5W2 | MLTFLMIVLGCVTVLLGLAILLQEPKQAGLSGAFGLGGSEQMLGTSTTSGIARFTMFLAVAFFLLCITVGLMAREDRDDTRLKPDPIEPGFGALEPGVGGVPGSENVGIGDAIGGAEAVIGGDAVNVGDAAGAVNNDTPVVDPPVVDPPVVDPPVADPPVVDPPVVDPPADGDPVGDTPVEIPAGGGAANENGGSGN | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 197
Sequence Mass (Da): 19431
Location Topology: Multi-pass membrane protein
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A0A5N5U6K3 | MRRLMSVFEHFEPMSDSAESREQSVFDRLREVYHIPLLALAVLFAAWVRTRGWQQYATDDGILFASNDPWYHYRAVQYTVEHWPFTIGFDPWSGYPEGVAVGQFGTLFDQLIATAALVIGLGSPSEQTVQMVHLFAPVVFGALALLPIYVLARGLSDRTGGLVSVLFLSLASGAFLQRGLVGSSDHHIAEVLFFAVAAATVAATLRVAMEEKPIFELLAQREFDALRRPLVWGCLSGLALALYVWTWPPAVFFVGLLGIFFALAASLYQVRGVSPDHVLFVGAIMGAVFALLTLVTIDVFTIDAVKLSLLQPLLGIGLAAGCGFLAAFARLWDDRDVDARLYPLGVLGVGVVGLGAFALVLPETFDYFLGQVSRIFGYTATEESRTVQEAQPIPLSEVGTRFYQSFGLGFYVALVGVAVALYRLATDDEPRSDVLFVLVLFVGMFLATITQQRFGYYLAVPVAALTGYAAAFSFGIVDVRERIAAMEQPTAYQVMAVVTVLLVVAAPLAVGTISQQTQAGTQRYNAVDIAQSSSNPGEVTRWTGTLDWMNENTPAIGAYGDGTASDLEYYGTYDRTDDFQYDEGEYGTLAWWDYGHWITVLGERIPNANPFQQNAGYAADVLLAPDEETATGLLDNGNGEETRYVMVDYQLGMPGTRKYSAPTRFTEYDVSATELQQYIYTASSIDQVIEQQDNSLARTLTLLSSQRAYESLRVRLYQGHGSRMSPINADGSVTVYDWDLNSGIPVASQGNLTRQFANMSAAQEFVEEDGTAQIGGVPGTPTETVEALERFRLVHASSESSARDPRRAAVKTFERVPGAEVTVEGPAETTVTAQVQMNMTARERQRPTVVDGQVQYASTGEPETFVYEQQVTTNADGEATFRLPYSTTGYEEYGVEAGYTNVSVRAAGPYQFTTPTETDEETLVTDRYNATADVTEGQVLGQEDGSTITLERTVIDRPEGAQESNTTEMIAPTPELSG | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Location: Membrane
Sequence Length: 978
Sequence Mass (Da): 106826
Location Topology: Multi-pass membrane protein
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A0A355ASQ0 | MLSRQRFETDRRQRTEPVPGQGNRIARWVPSRILELSPYHADSADGLLKLDAMENPYTWPSEIKDQWLQIISTVPLNRYPDPQGTALRQDLKTWCGLDQAADLMLGNGSDELIQIIAMTLGGRGQVIMAPEPSFSMYSMIASVTGTRFLGVPRDTEFRIDLQACLDGIAEHQPCCVFLARPNNPTGSLCSNETVHAIIDAAPGLVVVDEAYHAFCGHTFLDRITDHDNLVVMRTFSKLGLAALRLGFLAGPKNWLDQFNKVRLPYNVNTLTQVSVRFALEHMEWFQGCAEQICNHREQLSIALLGLPDVQVYPSDGNFLLMRMPRGRGTEIFQCLRQSGILVKNLDGSHEALADCLRVSVSSTDDNQAFVAALRNSLETVDLRESS | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 386
Sequence Mass (Da): 43058
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A0A6L8A9N0 | MKITTSWLRRLAKYDCDDAELVNHFNSLGLEVDAIYEVPVPFTGVIVGQIKQLEQHPDRNDLLVCTVLTDSTHNKTVQVVCGDPSLKLEEKVVLAQDGAKLPDGRAIKKTNIHGVESDGMLCSGKELSISSEHETIWRMSSNQGKIGECLGQVLLGDEKVLDLDFTPNRGDCFSVLGLARELQLVTDGAFHNPLTGVDWECSQLHSDEVSIEVQAPEACPIYHGIVIKNVPRDATHLTRLRKDLTSCGLRPVNYVVDCLNYELFETGQPTHAFDLDKVKDGIVVRYSRAGEKILLLDGTDVTLDSSTLVITSGDKPVAIAGVMGSLDSAVTAETKDILLEVAYFTPDAVRGTARKYGVQTEASLRFERGVDFSIQLQALRCACKRLAEEVSPSLSGSEDIPRFGPVVSVVSESHLPPRPEIFLPKELPQKRIGYAHDPKEVNHMFERLEFGFRQEDNGWWITPPPHRYDIEIPEDFIEEICRIYGYDNIPSEPLQVATHFRGSKRIRGDVRELRANLSTLGYNEAMTYSFIKDDANALFSNSKKIPELANPISMDRSIMRCSIVPGLLTAAAYNIARQESALRIFEYGQCFEYEKSGELKQRDKLAGLSLGPRHPESWANNRETIDFYDLKADIESLLCFSDVVFDSAACKWLEAGHSASVKMMDRTVGVVGKVRRNVARYFELDQDVYAFELDAAQLLRSEFARFAEFSPFPSVRRDLAIVLDKSVTIREIETLVRVTLKSFLWDFVVFDVFGGTQFEDNQHSVAIGITLRHQSRTLQDEEVTGLMNEVVDKLTTQFNAKLRT | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 804
Sequence Mass (Da): 90083
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A0A661FKV5 | MRFNLPTTLTLLRIVLIPVLVLFCYLPVDWSNIACVVIFSIAALTDWLDGYLARRWQQMTAFGAFLDPVADKLMVAVALVLIVQNDPSPSLAIASAVIIGREITITSLREWMAELGERAKIKVSWLGKVKTTFQMLAIVVLLYGSDYENIPLRDIGYLLLFVAAVLTLWSMISYLRAALPLLKRGL | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 186
Sequence Mass (Da): 20799
Location Topology: Multi-pass membrane protein
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A0A0D8J1Z0 | MEYEIDEVRKISIGGVGQKIHIRGEKRTNPVLLFLHGGPGISNRDSVVNREKDLCDVFTIVAWDQRGTGGSYWGVKKETLNLEQLISDAAELVEYLCAALEKEKLFVWGGSWGTELGTYLCFRYPEHIAGYVGSGQLVNGVLNEELSYDFAMDEAKKAGDTKAVSTLERIGRPVDGCYREVFKGMMAQRRIMKKYGGHSMNKGTYWTDTALPLLRSREFSFTDKLGLALGYKRCLTYMWPTTSKCDFPRECTRFAMPYYIFQGAHDNNTPSALVQAYYDAIEAPDKDLIWFEHSAHGPLREEPETYKRLLREKLLQWI | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 318
Sequence Mass (Da): 36275
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A0A523MLI4 | MTSQQLQLGLCVPLAAAVVISGVWVVTTKHQARQLFGELEALNRERDRLQVDWGRLQIEESTWGTHSRVETLSRDRLSLDRPTPEQIVVVAAPGP | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 95
Sequence Mass (Da): 10613
Location Topology: Single-pass type II membrane protein
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A0A947N8Z8 | MAETKSNPTANLLAQLAGNDVLRQLLILVGIAASVAVGVAAVMWSQSSDFRTLYANVEPQRAAGVVDALTAAGIPYKIQDSTGSIMVPSKQLHDARIKLAGQGVMRDGSGMAMLEQEQGFGVSEFMQSKKFHYALEQELARTIESMHQVRKARVHLAIPKQSVFVRDRKAASASIMLDVFPGSVIDKQNVGAIVNLVASSITGLSPEQVTVVDQQGQQLSYQGEKDDLGLSSRQFTYRQRIENAYQENIEELLGPLADAGQVRVKVAADIDFSSNEESRESWTPESKVVRSEQINEQTNGDVNATASGIPGALSNQPPTGAAKAEERDPGNRSIVRNY | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 338
Sequence Mass (Da): 36512
Location Topology: Multi-pass membrane protein
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A0A946Q8Y2 | MSFLEKIKQTFAKPASEEESSVSPHDGRYDQHAPIDFGEWGQAEEPPLGLEMVAEDEPQMRSADGGREAANSKCSEPGAVLPIVLTVMAAEGDYFEGSDLLREFNAAGLHIGKDGLFHAFPEHGVRAPLFSISNVLNPGLFDAQKIMTLQTRGVALFAQLPAAHSGKACFSALVETANRLATGLGGQIMDSERRLLTNHTLQRMQEQVLEFEYCRELERRKAGQSGS | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 227
Sequence Mass (Da): 24775
Location Topology: Single-pass type I membrane protein
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A0A5F0K4D6 | MLERLLEAVRKYNKDLDVELITKAFNLAKEKHKGQVRNSGEEYIVHPLEVSIILASMQMDDQTICAGLMHDILEDTDYSKSDMEKEFGEEITALVDGVTKLKNLQYKTKEEAQIESIRKMVLAMANDIRVIIIKLSDRLHNMRTLEYKDRDKQIKTANETLEIYVPIAHRLGINAIKWELEDLCLRYIDPVSYYSVAQQIDQKRSEREKIIQHIMDKLSTELDKINIRFTMTGRPKGIYSIYNKMQKQETTIDNIFDLIAVRVIVKDINQCYAVLGIVHNLWKPIPGRFKDYIAMPKPNFYQSLHTTVIGEKGQIFEVQIRTEEMHRNAEYGIANHWQYKEGKKKASNFDNRLNWIRQVIEWGKDTSAYEFIDNFKNDLFNDEVYVFSPKGDVVDLQKGATPIDFAYRVHSEVGNKCVGAKINGKIQPLNYKLKTGDIVTILTSKNSTGPNLGWLDMAVTQHAKNKIRAFFKKKSREENIELGQELLEKELRKKGHDVSKLMVDEWLLNAAEKNNALSIESLYNLIGYGTVQVENVIKFLEKKYNDKYKKEEEISNLVNIEDKNPHKDKNINEAIIIDDITNLETKFAKCCNPVPGDKVIGYITHGNGVSVHRINCKNIINLKNKERLIEVKWSENNNSSFPVQVKVIIENRPAYLADLTKGLSKDGFDISAINTKQNHDSTINISLVILVKSNSDIDRIYNIIKKIDGTIKVFREKN | Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 1/2.
Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
EC: 2.7.6.5
Catalytic Activity: ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
Sequence Length: 718
Sequence Mass (Da): 82807
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A0A2E5J7F3 | MVMAEVVIIDYGMGNIHSVYKAVKNVLDKNSNVKVSTSFKDIKNSSHIILPGQGAVGSCMNNISQVFDLDEFKNHITKKPFLGICMGLQAVMSFSEEDEGVQCLDVITGKVTGFKSLGKNLKIPHMGWNKVEHTSNHNIWQDIENHSYFYFVHSYYVEPEDPKVVLGTTNYGKKFTSIIQKNSMIASQFHPEKSSKNGLQFLKNFLNWEGDIE | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
EC: 4.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 213
Sequence Mass (Da): 24028
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A0A2E1X6L8 | MNPEPFPTPPEDLPPLPERPNDSNKSMMGSVWIVGGSPGLSGAALLAAHAALRGGCGRATVAVPDCCASAAEERKPLEVMSWSPGNGKNHWSPDAIELLMDNSHPSSWVFGCGIGRELETTGALGSFLASRTGPTVIDADGLWHLCQEPKLLQQLGPETVLTPHWGELERLRDALDLKGSNREDLSVELQRVSQAVVVAKGPGTVTTGGSGSYRNQTGNPGMATAGSGDVLAGLIGALLARGDDAEVAARRGVWLHGRAGDLAAQQHGEESLVAGDIVEALGQAFREYSGSSHRQQEEPR | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
EC: 4.2.1.136
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Length: 300
Sequence Mass (Da): 31444
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A0A143HPZ6 | MSDQLERFIFSGHDIRGQVVTLTESYRAVLENNQLPPPVARVLGEFLAAACLLSTTLKFEGLLSLQARGNGDVPLILAECTHHSDLRGIARVAEGAQIDDGASLRQLMGSQGALAITIEPQDGERYQGIVPLEKDTLAECLEDYFAQSEQLATRFWIESSPHTVGGIMLQILPGNNAASEAENRDAWETAQHLAETVTAEELHSLPHDQLLHRLFHELRPSSLGTANIRFKCSCSRERSARALIALGPEEVYTLLEEQGGEITADCQFCNTRYQFDREQIETLFNAPPPTLH | PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
Subcellular Location: Cytoplasm
Sequence Length: 292
Sequence Mass (Da): 32275
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A0A957Y255 | MACANMLLISFAAAALLAACAPTAEPAATATAPAPATSAPTTTPVPTLAPQPSPTWSPLRTPPDNPSTPAKIELGRQLFYDPVLSASNDMSCATCHRPDRGFSNGETVSEARPGAPPRNVSGLWNTGFNAFLLWDGRETSLESQAILPLTLPNEMAETPEKLEAKLRDIPAYVDLFDAAFGGGADAVTFDNATRALAAFQRTLISDNSPYDRFVAGDASALTEQQQRGMDLFFSQRTHCSECHQPPLLANETFRVVGVDSEDPGRAGVSETGLYGAFKVPSLRNVALTAPYMHAGQFATLEEVVQFYADGAGRAHDFPRVDPLLKGFDLTAEEKSDLVSFLEALTDESRLPQVPDVALSGLPTATEENR | PTM: Binds 2 heme groups per subunit.
Cofactor: Binds 2 heme groups.
Subcellular Location: Periplasm
Sequence Length: 369
Sequence Mass (Da): 39355
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A0A6L7MX74 | MPTSNRSDRAQRDARLEAMLALARVLRGRSLDAALATARTHPQRALVFELVHGSLRHYLSLSEALKPRLRHAIKDVEVEAALLAGAYQLLHTRVKPYAAVSACVDGVRALGKSSAGGLVNAVLRSLVRLPPEPPTTRAGITEHPTWLAGRIEQDWGEKAEQVMEANIGRAPMALRVNERKVSTTEYAALLHAAKIDFRPGMFPATLVLCRAIPKSSLPGFADGLVSIQDESAQIAAHLVAPESGERVLDACAAPGGKAFHLVEQVPSCQLTAIDTDEKRLAFTRTEAVRLGHDIRLLQGDAMQENWWDGVPYDRILVDAPCSGTGTLRRRPDIKLHRTAADVRAHASQQGNMLDAVWPTLRPGGTLVYCTCSILVEENDDVVAAFLDRTANAAAPAISADWGLPTSYGRQTLPAPGQGDGFYFARLVKVDA | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 431
Sequence Mass (Da): 46621
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A0A957H310 | MKHVTELIVVSEARQQILLGVKQRGFGRGKVVGFGGKLEAGETVTEGAARELHEETGLRVTPDQLDDVAVLTFHFPARPDWDHHIHVFLVHAWSGEPAGSEEITAEWHDLDAIPYDKMWDDARLWLPRILAGERLQGTFIYADDNATVQEYEFTIAPSA | Catalytic Activity: 2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+)
EC: 3.6.1.56
Subcellular Location: Nucleus
Sequence Length: 159
Sequence Mass (Da): 17829
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A0A6B0ZAJ2 | MSVRTRFAPSPTGVLHLGGLRTALYNWLYSRRHGGEFLLRIEDTDRQRSSPEHIRALVEALQRFGLDPDEEPLLQSARVERHREVANQLLESGSAYHCYCTPDELAAMREEQRARGEVPRYDGRWRDNTGPPPAGVKPVIRFRRPDTEDVVVEDWLHGDVRYLNSQLDDLVLLRADGSPTYHLSCVVDDEDMGVRQVIRGDDHLNNTPRQLQLIQALGWTPPEYCHLPLLLAPDGRKLSKRDEATDALHYLRAGYLPDAVLNYLARLGWSHGDQEVFTIEELISRFGREGLGASASRLDPDKLNWINQQHMKTAAVEVLCEGLETQLEDIGLNPADGPPLEEVAEAWRERAETLAGVAEAARWAFSHEIELDEKAARKVLRPVVREPLGAVRAALAGVAAWTAADIHACIAETAETLGIGFGKLGQPLRVAVTGGGVSPPIDITLYLAGRVRTLERLDAALGYIDARIATAGSAPQG | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
EC: 6.1.1.17
Subcellular Location: Cytoplasm
Sequence Length: 477
Sequence Mass (Da): 52808
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A0A6N9D5M5 | MDTRLVALDTETTGLAVEEGHRIVEVGCVEFKETGEIVDRFSQYVNPEREIDEGAISVHGITNADLRGWPIFRDIAGELLDFIRDADVVIHNADFDVSFLDRELVRMKHHERINDVCHVIDSLELARERFKSNNSLDGLCKRFKIDYSHRTQHGALIDAELLARVYIKLVSREVELFADLEKEEKKTPIFGLSSAIRDPRAGTIIKATDSEKRAHQEYMNMIGNPSV | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 227
Sequence Mass (Da): 25848
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A0A3D3XKW6 | MKIGVVGCGALGSYYGGLLCKAGHETHFLLRSDYDTVQKQGVSIESPNGDFRFHPHAHNDPSEIGACDLVVIGLKTTANHAFSHLLPPLVSSRTSLLTLQNGLGNEEALEALFPDNTILGGLCFVCLNRIEPGRIRHMDHGLIMMGAYQDISSARALECVEVFDQAGIPCRYTDHLAKAHWEKLMWNIPFNGLGVAGSLGHDGFIVASSRLGSLPSSDCMDANALLGDAEWEARVRGLMREVASVANELGLSVNTDLESKLIARTRTMGPYKASTIIDFERGDPLEMNSLFLEPLKQAKEAGIETPLLERLTLILAELQGRQDRSK | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 326
Sequence Mass (Da): 35480
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A0A8B7P6X1 | MEGSEYEKRYQRLDEHHTYEGFNRLHDAPRVGFSGDGGLGSSEETRTSSDNVLMHRVPERVRDWHHVDDLDSFFKRIYRYHQSNGFTVMLLRDGLDLVQYLFMVFLTVLVLCGLNYEVLLGSESVSLNKNNTSGVVVKTTLSDGFYSFSETLSRISVMLGIVLFAALLFLLGRLVYTIHNATQYKDTKAFFSNALKIPDSALQNVTWDEVKKQLMEVQLQQRMCVHKDILTSLDIYQRILRHQNYMVALVNQGIIPVRFNLPFYGEMVFYTKGYEFNLQLLLFWGPLSLLQSITPESLRQPHRKKEIIASFEKKIVYLSIINFFSMFFVFVYQVLYSLYHNVERVKNEPGSLAGRCWSQYGRIYLRHYNELDHELNSRLNRAYKPSMAYLNSFSSPALSVIAGTLVFIASAIFAVIVAISLFDDDFLRVEHVINLLAVSVIVIAVCRNFIPDENLVWVPEMLMERIVTQIHYLPESWTGRFHTTQVRDEFSRLFQYKFVHLLEELISPLFVPFILFFSLRHRAKEIVDFFHMFTVSVEGIGDVCSFAQMDIKQHGSPNWQPDVRKANDGEETNPEQRLYAPDKGRTELSLMHFALTNPDWQPPKSGAAFLTAVKQRPHQECHGLTAVAETDLAHSINSLNLTGQDRIAHWMAPTVFGTRNVAGPSETGYVARGFNGGVAHVEGPMQSSVLSGAPSLQGSLHQSSLEMAASIHPALGHLDDGNNSFTQWLPQTQTVYDMGMSCLYLRGLSNRRRHQNQYYDEYGSGAYRDPRSDAGTGAGHPFQSQESSIYDPRSRMYQRTPSPPAMDPFRDAMVSHLGSSAQLPSGSISSQYQEMLHGASDMIQQQRSQTHAPQQPPPPTLEQPGSAAGMSDDTPLLRPNRR | Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion.
Subcellular Location: Membrane
Sequence Length: 882
Sequence Mass (Da): 100228
Location Topology: Multi-pass membrane protein
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A0A6B0Z6E3 | MPTCSRRPRSAWSDRRARRKCCRGPSRCPRTRTRMRKRKIRCRRPRTPPRTRPGKFGSRNRRPMRRLKKPPGPSRRFWPMIPPEMAENGDLLPSSVDAERALLGGLMLENDTWDEVADLLAGGDFSRDDHRLIFGAISDLINGGKHCDNLTVCEHLRSREQLDDAGGAGYVGNLLIGTPSAANVETYARIVRDMSILRQLARAGRRITGRVLKTGGREAEELLEEAEREIFQINEQSYKGDLDDLGMGEAFRAELVNWLREREKSGEAVTGVATGLTDFDNLTAGLQNGDLVILAGRPSLGKTSLALTIAQSAVLSQKPVSALLFSLEMPKKQIALRLLSSLGEIDHADLRIGKIGRNWSKVNSALNMLKEAPLLIDDSQLLTPDRIRSRARRVSRSESRAGRRLGLVLVDYLQLIDASPTERRDVNRAIELGAISKSLKALARELDVPVVVLSQLNREVERRPDRRVQLSDLRDSGAIEQDADVVAFVTLPESQEKQDLYHVNKRVLHVAKQRNGPTGECEVYFESACMRFRDLQPGDAEEELPPAPSVEY | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 552
Sequence Mass (Da): 61780
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A0A2E6M0P7 | MTSQKDPARYVGMLGGGQLGRMFAQAAHSFGYRTVALVPEEQPIIADVAQHITAEYTDTVALDKLVAAIGDAPVTLEFENIPVKTLEYLESKSVTVRPGIRALKIAQDRRLEKTFFREDAQVPTAPFFILEKDDDLKNEQLVSFSFPAILKTARDGYDGKGQVKVSSLDELAAAWESLRKVPAILESFVTFDRELSILVVRGADGDVAFYGPFHNEHEDHILATTWSGMPLADATVESAYELGQSVVEKLDYVGVLCIELFQCGDELVVNEMAPRPHNSGHLTIETYTASQFEQQARAALGLPLAPAVMRSPGAMINIVGFRPSEAALQQIMALPGVHWHWYAKDAIKEGRKLGHITLEASTFEKLEELFVEVKGLLKS | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
EC: 6.3.4.18
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate
Sequence Length: 379
Sequence Mass (Da): 41759
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A0A2M8Q0G4 | MLDLQKRVLDFCRAERLFVPAERVVVAVSGGADSLALLDILVALQGELDIALHVATLDHGLRGAQGAADAAYVAEIAARWQLPCTVGSVDVPSLAATWRLGTEAAARRARYAFLRDCAAQISATCIATAHQRDDQAETVLLHLIRGSGLAGLRGILPCTQRDGLRLVRPLLAIAHDELVAYLSARGIAPREDSTNYDLRYARNKVRHAIMPLLREINPSVAASLARTAETLRDDYAALMASLPSYAPPSIRREDFLRLLPAQQRLWLRAAVQHLAPDHELSFERVEAARRFVARLRTAGGVQLGNGLWLRANQARLRVQRG | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 321
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 35160
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A0A350HX96 | MGGLQGPELIFLLIVILVFFGAKKLPELAKGLGQGIKEFKKATKDVQQDLHQAMEEDSAASAPPRKAAEPAPIPQESESNEGSEVPVPSEESTKATDASKA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 101
Sequence Mass (Da): 10671
Location Topology: Single-pass membrane protein
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A0A2E4D2F0 | MSRIAVYPGTFDPITNGHLDLIKRALKIFDKIIVAVAENTQKKPLFPIEQRIHLVETVVSGHSFVDVCKLDKLVVELAKEHSANVILRGLRAVSDFEYEVQLAGINRSMEPSIESVFMSPADDFAFLSSSIVKDIARHRGKLGNYVHPEVEKCLIQKFK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
EC: 2.7.7.3
Subcellular Location: Cytoplasm
Sequence Length: 159
Sequence Mass (Da): 17874
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A0A843FK26 | MNSEKLEAFVDAVLAIILTVIVLELPQPETITFAGFWALKTNFFAYLTSFIVVLTNWYFFHIIFEIIKKIDGKVIAMTGLVVFVMSLLPYFTLLISNNFTNINAQLCYCIFFIVIELAYDVLFWMIINIEHNSDLKQLLNLKRTGLHLLLYAIGIILGYLFTAEIIVVFVFVVVLTWFIHVYMSIKSDNID | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 191
Sequence Mass (Da): 22052
Location Topology: Multi-pass membrane protein
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A0A158R0Y4 | MAAVFRSNKRKREKVLIDNSHFESMPMCGIEVRLPPGLKPYPSQKLMMVRMITSISKRLNLLAESPTGSGKTLALLASSCAWLDDYRKKRQDARTKCPVHGENAALDSNDTEFFSDFESTPLGKQILLAVSFASQFIHFFPIIVFISFRRTRIYYGTRTHKQIGQVVKEFSRLPYGGIIRSSREQSCINLAARESRDVSAYCKELISAGGMGCRHKDAMKPRYEKPYNLRDALVQMGAVVFDIEQLVESLSSMPNPICPYFSSTRLLTQDADLIFCPFSYLVDPIIRNSSDVHLKNSVVILDEAHNIEDNCREAASFTFYEKEIADTLCNLREKETVTLKFIEKMAGNVELMDGMEKEATNATICSYTEDLNDMTTLALFVDDLYKWFRETASKLLENARSDEARRDGQAGGSKNVNYSQMGGGDPTDVWLSSTEGPSGYSPVRMGYRTSISMWCMSPELAFTSAFSDCRSVILASGTLCPVETLKTELGLKFHSQMEGDQVIPSDQIFAGVLPVGPSGYKLCATYRNVSDSNSQFISELALVIRAICMTVPCGILCFFPSYRMLTLVYEYMENTSILRQVQTRKVVVKEPRRSSDLPTVMEVYETGVRNPSHYGRHVDGALMFAVFRGKVSYSIEGIDFADDLARLVISVGIPFPNAMDDLVKEKKIYNDHFCKTKSLLSGDQWYISQAYRALNQALGRCLRHRNDWGALVLVDERLTEQASRSPASMVSSARVSKWIQKQLVVYPQFDIFESSLSDFVRRMQLRDDSKNCTENDH | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 777
Sequence Mass (Da): 87630
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A0A946VVF9 | MSFLSYIKNLFGRPEENSTQAGQGTTGEPSVPAHVAIIMDGNNRWAKQRGQGAGGGHRAGVEAIRAVLEVCQQQGIAVLTLFAFSSENWLRPESEVQELMKLLRNYLATEIDSLHKKGTRVRFIGRRDRLDADIVRLMQAAENKTTDNQAGTLVLAIDYGGRWDVAQAAAGLASQVAAGKLDAASIDESMLDAQMSLADLPTPDLCIRTGAEHRLSNFLLWQLSYAELYFCDCYWPDFDAREFNNALQVFASRQRRYGMSGQQPGVGNAPTAPRNGARFASMGRNA | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
EC: 2.5.1.31
Catalytic Activity: (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate
Sequence Length: 286
Sequence Mass (Da): 31358
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A0A8C4N4P4 | MTPGQTSLRGPDETCTTQESIVSTKAIALLLICGVLCFTYGLFTPLPSHPNIMSWYGNTSSQTSMLHPLPGVWISSTNGRLGNQMGAYAALFGLARMNGRKAYLSMNSANNLGAIFQLTLPPLPAGENKDFQNFRLHDWMEESYEHISLMRVHFTGYPNSWTFYDRYRDAIRREFTFRPMIREVADTFLRSVAAKSTSQLPGANITFVGVHVRRGDYVRVMPNVWKGVVADAQYVIEAMNVMRGSYPDSVFVVASDDVKWCRQNINITRGDVYFVADGIPHASPQQDLAVLAACNHTIMTIGTFGFWAGYLAGGDVIYLDKYVLPNSPFLKVFRYEAFYLPYWKGIPADLSPLKNG | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: ganglioside GM1 + GDP-beta-L-fucose = ganglioside Fuc-GM1 + GDP + H(+)
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 356
Sequence Mass (Da): 39838
Location Topology: Single-pass type II membrane protein
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A0A1N5TT98 | MHISDTHLGSVQYGIPERELDFYDAFREGIQIGIDRDVDFVVHSGDLFDSARPSNRALRVAEESMILLQKNNIPVFSIAGDHDRPKVRDNPSHLLFDLFGLKILGLEGFESTIFRKGNEEVFIGGVSNMKLFKREQLKNEYDRASREASEHKISVFMSHQAISPLFPPESSEAREEDLPVNYTYLAFGHIHQFIKKKFGRSLFCYAGSTEVKSTNEISGLTRQGKGVNIIDTDGDETEMERVILKSVRVQRDLTGTLDECLEKLDELNNQEFEKKPVITMHIHGKPNVKYMREKLGEYREKFIIRQPIIEENAEAVEMSPSFEESIESIFTKYFGDEKKGNMALSIYNLIKEGKHSDEDILKICEEILNDH | Cofactor: Binds 2 manganese ions per subunit.
Function: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity.
EC: 3.1.-.-
Sequence Length: 371
Sequence Mass (Da): 42542
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A0A6L8ADS5 | MCPVLEALAELELPVNSRLWIAYSGGIDSTVLLHASVQVFGASRCRAIHINHKLSAPSDRWVEHCLRSAVHLSVDLTVEEVEISEGNVEQQARLSRYAMFRHHLGPSEVLLTAHHRDDDIETLTWQLFSGRATIGIPASRPFGSGTLWRPLLHVEKQDIEAYAMQHELTWIEDESNTDTSFDRNWIRHELLPQLSSRFPQVKQRILDLKQATLSLIEREPLQLPVEEITIEKLRAWLLAYEVNPPTTVLNQIQKQISAKADANPEIKVADGLFVRRYRKRLHLVRNFEAFTPLNVEVGRPIQLSNGTLNWKNSLEGFEEGRTLLCTNRLHLKSGQRSIKDGGMHKKLANLFQESSIPPWLRDGWPVLCEGDTVVSLVDIVPDPSARKGQKSLALVPTWHPFD | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 402
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 45677
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G9LTR8 | LYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLSGVSSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 217
Sequence Mass (Da): 23121
Location Topology: Multi-pass membrane protein
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A0A6L7LWK2 | MTWFTERIVHWGREHGRSNLPWQRDRTPYRVWIAEIMLQQTQVATVTKHYDRFLQRFPTIATLAKSNQDEVLAAWHGLGYYRRALNIHATSKQVMQQYEGELPRTVQELEALPGIGRSTAGAILSLAYQIPAPILDGNVRRILARFQGVNGPPTTHIPDRRLWQIASEHTPNTDCRNYTQFIMDLGALVCTRTNPKCEQCPVHEKCLAYQNQETHLFPAKRIAKTKHDKAYYLVVFTDDDKILLNKRDQEGTFALLWDTPELNGSETLEPALADLNLNETKSFHQLQFTVEPYSISNKIVTETVFVAKYSLQAAKLGTPPNMQWFAMDELSTIGISVKARHRIELALTQGRN | Function: Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-dGTP).
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Sequence Length: 352
Sequence Mass (Da): 40341
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A0A6P7SRY7 | MTDIVELSNEKLNVEDVSKSVTLPNCGAVSLFIGTTRDHFDGKEVLSLQYEAYHTMAKKKMFEICQDIRNKWNVGKIALVHRLGEVPVAEASVIIAISSEHRKESLEAVQYAINTLKAVVPIWKKELYRNSSPEWKENTEYFWKKEGCCNFKML | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group.
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
EC: 2.8.1.12
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 17669
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A0A3B8SVD9 | MRYTLAELARLTATELVGEGSIEISELASLARATESSLSFLSNDSRRHELDATQAAAVVVSKALGDDIACGLISDDPYRTYAELSVLFDEKGIPFAQGVHSTAVIDPTAVIADHVSIGPGVVIGADVVVGAGSVIGPNVTVYPNTRIGLDCLIGAATVIGYDGFGFAKSSNGWVKIRQLGGVLIGDDVEIGAGCTIDRGALDDTVIDDGVKLDNQVHIAHGCHLGARTAMAGYVALAGGTIIGQDVTVGGMTGFTGHLSVCDKVHIGANALVTQSITTPGAYLGGAGGVMKAEDWRKNAVRFRQLDAMARRLQMLEKQLNTQSKDS | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.3.1.191
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Length: 326
Sequence Mass (Da): 33837
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A0A6A0H8A9 | MIGLIGSLAGLIKIHNSKTLVDDAVFRLHYRWTTSLCFLACALVAASDMFGEPIQCLMNGGEAPKPYTTFCWVSSTFTINTSNADGESGHYESYGSNYSGTGKYDSKTHEKRIHTYYQWVPFVLFALGALFYLPHLIWKEIEGKKVECLLQGLSVISMDDAAPAKKMNIVKYLFASHGRLNNRYAYGYFFSHVLNLVVVVSAMFILESFFGGVFLDYGSKTVRYLNGHADVAHNPLIFAFPRVAKCHFRMYGPSGSLENHDLMCLLPQNIINEKIFLFIWFWLLILTTATAMQIVYIAAIFLSPFLRLKLLETYGRVMSDAQLEDLVHRTYLGDWFLLRTLGKNVDALTFKDIMQELVKMIAAHSSSGSRGEPVTMFSPHAPSYRHFNIDEEDPLEHKRRMEEEDTRV | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 408
Sequence Mass (Da): 46393
Location Topology: Multi-pass membrane protein
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A0A3L7RNX6 | MAKSKSADQDDSSMSFEGAMASLEQVVRKLESGSLPLEQMLSEYAKAVEYVQVCHRQLEGARRRIAQLQSVDADGKAMTKEWDDTAPTVQENRDAPSRRKSSS | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 103
Sequence Mass (Da): 11437
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A0A7C4GIM3 | MMRELRTIWWDKNGVVIIDQRLLPHKLKYLKIRSYKEMAKAIKDMAIRGAPAIGVAAAMGLALAVVNAKTNNRELLMKRLEKAAETIKSTRPTAVNLFWAIDRIMSVVRETQSGEELREKVLMEAIRIADEDVEVNRKIGENGSKLIDDGDRILTHCNAGALATVGYGTALGIIRTAYSQGKKIQIYASETRPRLQGAKLTTWELTREGIPVRLITDNMASFLMQRGEITKVIVGADRIIAKTGHVINKIGTLTHAISAKYYNVPFIVAAPFSSIDFEHSIEEVVIEERDVREVLYIGNVRIAPKNIEAVNPAFDITPPDLVSYIVTEKGIYKPDELKHLAK | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
EC: 5.3.1.23
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Length: 342
Sequence Mass (Da): 38201
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A0A353R259 | MSDPSFSGNHLLGDIGGTHTRLTLYRDGRHGVIGRYRNREFTDLPAIVRHHLQTLDLPAPQTAVLAVAGPLERDGAVTLTNRGWRLEPTALAAELRLASVDLVNDFTAQALGIPHLESEECLALNSAEAWPHAPRAVLGPGTGLGVSGLLPTPNGWLALSGEGGHVTLPPADARESALLDALRVQWGHISAERVVSGPGLLALYNHLAVEAGAPGLSAPPEVTTRAGHDALADEALGYFFAFLGTIAGNLALTLGARGGVYLCGGILPDLQRPLRASAFHDRFCAKGRYRAYLEAVPIYLVTAPDTAFRGLISLLASRRP | Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
EC: 2.7.1.2
Subcellular Location: Cytoplasm
Sequence Length: 320
Sequence Mass (Da): 33832
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A0A846N9N6 | MIEMMVPGEDAEIGVRVYKTSSPPLTGRIKARLEDFAVKEKISPQLLASLRRLRSPTHRIQVYCAVRVGVDTLTLARIINFHSRIPRSRLRFLGLKDSRAVSSQIFSVVDGRKVPESIGGLSLLGWSEKIPSKESLMGNDFSVFIRNFEVSSQDVSNRLSRFIEELNVESLPNFYGYQRFGTYRRITHLVGKKIVTGEFKEAVMLYLTYTTPYEPEETRGWRKSLRDTGDLEGALKSAPKPLFYERKMLRELVKRPESYLKAIRSLPITLRRLFVNAFQSYLFNLVLSRRIREDMPITEPVIGDFVYDPIGSKIMRHRQRDRDSHHLMVAIPLFGYGYRSSEGRQGDIERDVLKEAAVTTRSFFVKEMHELSGKGGFRKADLDLDKLLFTHDIESNVVCSSFTLQRGQYATILLRELIKPSNPLQQGF | Function: Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
EC: 5.4.99.27
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Length: 428
Sequence Mass (Da): 49165
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A0A6N8US91 | MVVVFGGTFDPVHVGHLHGAHHVSKSLGGAIVTMMVAPNPQLRKPPVASLHDRWTMLLLACKSNPVLQASRFEDGRDGPTRTVETLRDLTRTNDVPIVWAIGMDAFQNVSSWYRAEELPEIVSFFVLKRMSPSSDEVPIGFSRVKEPGQLLESPGGVFVSFKPMLDVSATEIRRKVRDGCDVSESIHPEVCKHIIKNRLYRG | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 202
Sequence Mass (Da): 22440
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A0A356NNM6 | MDDKILKLLGRRDYVPANIPELLRGLRLSANQQQKLQKDLRILERSGQVARIKGNRYILPAEADLISGRIQITRQGRGFLTPDDPSISEISIPANSTSTAMHEDLVLVRRDIRVKHGSISREAPCTGTVVRVLERRRKNIVGTLKRGKQFLYVIPDDTRMPQDIYVPPPKDVGRSAREGDKVVVELLHWESRHTNPEGQITEVLGPPTAEGVDMLGVLRQYELPLKFPRKVLQEVRHFGNEVAPSEFADRVDCRKHQVITIDPHDARDFDDAFFLKKIETGWKLWVHIADVSHYVKPGSALDVEARKRGNSTYLVDRVIPMLPEALSNELCSLKPEVDRLTKCVEFQLNQQGHVKRFTCYAAIIHSKRRYAYEQALSIIRAKPKDSIERMLHDAHKLAQKVRQLRFKAGALELDFPETKIRLNDKGFVQDIELSRSDESHQLIEEFMLLANEAVALRSSKLRRTTIHRVHEKPDPIRLQEYRENVLAHDVPCGNLTKPVEVQKLLKRLGKLSIGPALKIGFLKSLMRACYSVESLGHYGLAKSNYTHFTSPIRRYADLVVHRTLFDYSKTPLTALKQTAEHLSVTERNSSDAERDSKSVKLFAYLTSQLASGKPVHYDAMVTEIRNFGFFVEVPNLGMSGLVPLSILDDDFYEIDQRGTQITGRRNRRTIRLGQDIKVVIAKVDPFKKQVDFRLLQSGKKSSGKRRLSGNQPKKVKKKSSSQNRRRTGPDKKTLTKRKSKSRKSSS | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 746
Sequence Mass (Da): 85041
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G8YJ51 | MLRFSKNKLIFRILICCLVYLIILNVTTRRSYRPIGDSDTDTLSNIELKQYHRSEKLSKIHTYSTNYDNLIRKYGMSAITRHFSLTQRCNAYFNLLMANDSLLIEPNTDLPFFRDDYEGNDPEVWGRVRNIEQRMHDQISHMRLFTKCFLQEDSPIKQQTTTESTGKPASRFLGKAKFKWPSVFRMEHSCKSIESKIYPWLSGAMPTYTRWDGTKKLANSGFDTVQKFFGECFLNLFESKLEGKGIVLTISDDHVDSTIRLFKVFRTLENTLPIEIVYWKDLSDESKNRLIKASRDPFIVDNMEKPAQDLWFVDVAPAVQSDYLNKFEGFGNKILATFFNSFAETMLIDADAVIFKRPEYFFEREKYKKAGTLFFKDRLAVEYRPDHDVVFFEKLCPSLMDTAFFGIPQVTDYSLDRQLFKGLNHYMESGLVLMNRRRHFTQPLIMAQLSFHPPVQFRLYGDKELFWLSFVISGEESYAFNEHFSAAIGFYTPTDERPDSKAGSKEICSNHPAHISDEDNHTLLWINSGFRYCGNADFVNYEEEFNAKDRYRHIQNIKDFETFFKGKLIIKNALIPPYRVLEANNLDDEANMAWINMRQYCAGYTWCAYSKIGGRYEQDGQIFYNNDEGYTIDFTPEETSLYERLGDVWISDEFL | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 655
Sequence Mass (Da): 76744
Location Topology: Single-pass type II membrane protein
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A0A967QPS8 | SGKTPVAAEVARVLVSLGERPAVLSRGYGRARKVAGALVVSDRGAVQAEVDVAGDEPLMLARRLPDTS | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
EC: 2.7.1.130
Sequence Length: 68
Sequence Mass (Da): 7013
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C5J048 | MRQLSIAGAWVHEPKIFPDSRGSFHEWFRAPEFTEAAGHGLNLAQANCSVSSRGTLRGIHFADVPPSQAKYVKCVRGAVLDVIVDIRVGSPTFGQWEAVRLDDADHHSVYLSEGLGHAFMALTDDATVVYLCSEGYSPGREHGITPLDPELGIEWPEGITPLLSEKDEAAPTLAEAKAQGLLPSYEDCQAYYAQLRERG | Pathway: Antibiotic biosynthesis.
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Length: 199
Sequence Mass (Da): 21750
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A0A6N9D2S0 | MNFNLPTFVGTLVVFVIFVWFVTKFIWPPLINAMQARRERIAEGLETADKADVKLAESETHAQQLLQEAKSEGQKVIDQARAQAANIVEDAKVKAREEGERLLDAARVEIEQESNRAREKLRTEISDLAILAAEQILEAEVDPKKHELMLNSISQRL | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Cell membrane
Sequence Length: 157
Sequence Mass (Da): 17778
Location Topology: Single-pass membrane protein
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A0A0D3QED5 | MEKVVLSILLAFLLGFVLLFVGLFLGASFYMGREKISPFECGFDPMGSSRVPFSLRFFLLAVIFVVFDVEIVLLFPVVMVMGSSWMWFKSYL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion membrane
Sequence Length: 92
Sequence Mass (Da): 10491
Location Topology: Multi-pass membrane protein
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A0A6B1EHD6 | MKRGFTLLEVLVALAVVALGLSAAFAATGQSARTAEQLRVRTLAQWAAADALTALRLAGELPRGQSRREEEIAGRVWWVEYRVRQSAAETLRDVEVRVGPERDAPVLAAARGVVRVRVEAEDAEEEE | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 127
Sequence Mass (Da): 13879
Location Topology: Single-pass membrane protein
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A0A661CBT9 | MTIALHGMGVSRGIAIGKAHVVKRDQLDIREYSIKKNRLDDEVKRFEDALTNARQQLRAIREHIPESTSADIEAFIDTHLLMLDDAALTKEPMRLIKELSCNAEWALKLQRDALVAVFDEMDDAYLRTRKDDVDYVVNRIQRLLLNQTPLIHEKADQRLTGYIIMANDLTPADTVLMQHNGIAAFATEFGGPTSHTAILARSLGIPAIVGLQNALRYIKDDEEIILDGSRGIILVDPERHELLHYQHLQKEEKRYFSKLGKLKNKPAITLDEVSIALDANIELPKDFETVVEVGAAGVGLYRTEFLYMNRETPPDEEEHYATYKGVIDVLKGLPLTIRTLDLGADKQVDGGRQSGPVTTNPALGLRAIRLCLKEPALFRPQLRAIIRASVHGPVRILIPMLSNVHEMQQVLQMVDDIKKELDEQNIPYDHELQIGGMIEVPAAAVCADIFAKYLDFLSIGTNDLIQYTMAIDRVNDEVNYLYDPLNPAVLRLVHTTIKAGKKENIPVAMCGEMAGETKYTRLLLGLGLREFSIHPATLLEVKQIIIDSNVSELQTLANKALKASNGIDVANIMRETTD | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
EC: 2.7.3.9
Subcellular Location: Cytoplasm
Sequence Length: 578
Sequence Mass (Da): 64680
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A0A183T5G0 | MNPDDQPTDFSEIEIAPSQSPEIYYYKLHPGRNIFFCRGHGVMSRQMGVFYLTVFLIVGVSALFFAFDCRYLAVTLSPAIAAVGVLLFVFVLAVLLRASCIDPGIIPRATVEELKWTEAESAESGDIYSAPANMVQNREMLIRNYPYKQVYCHTCRIHRPPRASHCSICDNCVERFDHHCPWIGNCVGKRNYRYFTVFILSVAVYCCYVLTFAVVNIILIVAFFSMLSVVGLSCFHVSISCREFSTHEDIRGLPRLLKQANRSNPFSQGSGCRNMCYVLCGPAPPSFLQPWKKVSTDSWRSSELAALVDPSIAVRSLHIPPTEANMESPPSQDWRSTVGGYPRDPTIPVQDELAAETLLGTQSNSVRNGKSHLPLPCRSPQIPFASYMPHFRRSASF | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 397
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 44515
Location Topology: Multi-pass membrane protein
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A0A846QCW0 | MPFYIEVNDRNVLLVGGGEEATRRAIRLLRVGASVKVLSKQFSQELEQEAKGEHLELIKGDAKDGDLLKQLIAWCDLLIIATNDKDANDLAYRIGRRLKKLVNLTTDAEKTDVVVPFEAKVHGLRITVTSEGKSGFVVRDALNKIVELLKEDENLPLLLDSMYHLKKELKKITKDARKRIKVYKTVYQDPFFRELIHEGRLEESKKYAMDIALRRLQGEH | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 220
Sequence Mass (Da): 25195
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A0A7J3PM60 | MIRKNLRLIAGIDEAGRGSLVGPLVVAAVALPPNSVRTLRTLGVRDSKQLSRNNREKIYREIINLCPFVESIEIPPSVIDRYTKRSGGPGINALEAAAAASLIEKIRPDIVYIDSPTRIAREFAKMINSRLEEARCVIVCEHGADVSRPVVSAASIIAKVVRDNAIKSLKNRLGDFGSGYPSDKKTISAIKEILTCGKEMTKYIRMSWKTLNSIQPSLDDYKED | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence Length: 224
Sequence Mass (Da): 24678
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A0A1Q9A0W6 | MGIVSAFRNRNPKWAAGLALFLSPSVATFYLGRGRLGLLYVLADLLVGNVFLFALKYYGIFQPALIFAAVIIAYRAGASVHVYMIASRQPPLGRYPWFARFHNVLLLLYIAPLVIALAIRNIVVQPFTIPSGSMLPTAQVGDYVFAEKLTYGMSQYSVFGGLGPGIRIGGRLPGRGEIVAFALPSNPRQDWISRVIGLPGDRIQMRGGRLFING | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 214
Sequence Mass (Da): 23403
Location Topology: Single-pass type II membrane protein
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A0A135YZE3 | MWSISIALNKISQIALKISINDAIDMLIIAYIFYKMLMFIKDTRAEQLFKGVIMLLVATQLSGMLKLHTLYWILVKILEVGFILPFIIFQPELRAGLEHIGRNTSIIKFGGHGDSDIDKDQDLVIAEMVDALYDLASRKIGALVVLEGKTKINEIVDTGTKIEGRVTKQLLCNIFIPNTPLHDGAVVVRDKKIKSAACILPLTQRKDISKELGTRHRAAIGVSEMSDCLTLVVSEETGSVSITRSGKIYRDVTRERLTNILKNFYKTKSENTNIFKELMKKQK | Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 283
Sequence Mass (Da): 31825
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A0A6L8AU57 | MSGPGAIETGLSRMLERFLALLLLAIFGTVVLLVILRYVFNTTVVGGNEGALIAFVYTTAIGGALAVARREHIEIRYFVDLMPAGIQRFLDVLQLALVAIVNFAIVWYSIVWIASTGSYLMPALQIPQIMAQLSVCIGSSLAFVYCLLGIFHARGAPSRSPAEGSLPARGSPSRSPAEGSRRCTAGH | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 187
Sequence Mass (Da): 19982
Location Topology: Multi-pass membrane protein
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A0A9E1Y7E8 | MIKQWKFPGGVVLDGHKQLADISEPTLPPELTYPLLQRSDYYVEPVVKPGQRVLKGEVIANSQNPLATPVHAASSGVITAIASRLIAHPSGLSDTCIIIQTDGLDTVCPGNPCPNYQLETPAELRHKTALAGIVGLGGAAFPTAVKLKNRLPTHTLIINGAECEPYISCDISLIQANAQQIIQGALIMQYILQAERCIIAIENTMPVAHQALLSAASEVDIQIITVPAIYPTGGEKQLIEVLTGVKIPAKALPADHGLVCQNVGTAYAVYQAICLGLPLTDRIITLTGKGIKYPKNIRARIGTPIKHLVELCGGYTPDVQRLIMGGSMMGIALSTDDIAVIKATNCVLAMTSSELSVNQAAMPCIRCGDCATVCPAELLPQQLYWHSRSKQFEQCQDYQLFNCIECGCCDIVCPSQIPLVQNFRAAKGELTNKEKQAAQAILAKKRHQNQKQRRGKEEQEKLGKAEKRQAMIDKMKSAATNRKTV | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 485
Sequence Mass (Da): 52454
Location Topology: Peripheral membrane protein
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A0A6N8VUM0 | MTPPTDVARRTGRGRVRRIIFTREQIALRVRELGDEISACYEAREELLVLGLLKGSFMFLADLVRCIHHPVQVDFIVTSSYGSGMVSSGNVQLLYDPEVSLEGRHVILVDDIIDSGRTMASLVPIIQARGPASLELCTFLHKRRDGIAHEPRWVGFDAPPEFVVGYGLDYSENFRHLPYVASI | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Function: Purine salvage pathway enzyme which catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP (inosine 5'-monophosphate). To a lesser extent, can also act on guanine leading to GMP, but shows a highly less efficient activity with xanthine.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 183
Sequence Mass (Da): 20496
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A0A182ETE8 | MVYHFRYNDIPLQYDDKIYKQLIDGGIDDLLAQHIAHMFIRDPLQVFRERIEQDDTKSTEHFETVQSSNWMNMRFKPPPPDSEIGWRVEFRPSEVQLTDFENAAYCCFVVLLTRVMISFRITLILPISAVTENMKRAQRRNAVLEQKLLFRKGIATCNSPPCARGAGCTLESDDVVEMTVNEIINGNGNDFPGLIPLMRQYLDSADVDVDSRCTVSQYLSFIQKRASGELQTLAAWMREFISEHPEYKHDSYVGDRIIYDMLKEMDRISKGEISCPKLLGDYCTKTDSRIPMAVRRAEEKLIVSTKKQS | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 309
Sequence Mass (Da): 35669
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A0A3L7Q7S1 | MSASNTNSHATTPNTGAGVLPRSILVLKGGPDAEREVSMKSGGMVAAALRRAGMDVNEVTIDRPSLEELRGMRGEVVFPVLHGSWGEGGPLQELLEADGRPYVGCGPKAARLAMDKITSKALVSEFGVPTPRSQELRNNVEFSLDFPVVLKPADDGSSVDLRICHSMQEVMRARLEIGPRRERILAEEFITGRELTVGLIDGECLPIIEIRPREGTYDYEAKYNRDDTQYILDPELPVGVADAVRAFSRAAWHAVGCRDVARVDFMLDERGPWFLEINTMPGFTDHSLVPKAAHHAGISMEELVTGLVRRALARACARRVAA | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 322
Sequence Mass (Da): 35168
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A0A2E6LSP2 | MTQSMPLRLAGAIALGAVTTTLVLLLMQALIESDAAPPDAETPAPPLTFVRLLDDEPPDTGRNPPEPPRPPDEPPPPPKLTPDRDTGPMTVATFTPPVTDKPRGPGAGAMSEGEALSIVKVRPVYPQSAVNRGIEGYVLVQFTIDTLGRVTDVEVLESSPRGVFERAAVQAVERFRYKPRVVNGQPTPVSIRHRLTFELDS | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 201
Sequence Mass (Da): 21629
Location Topology: Single-pass membrane protein
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A0A662ESA5 | MKIEEDLKKLEEITTRLEKDDLPLDEAISLFEEGLSLAASVKKGLEEARLRIEKAVEETKGTFSLEPFDLS | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 71
Sequence Mass (Da): 8037
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A0A3B8K877 | MPEVAVSLGSNLDRESNICAAVETIKSLYPDAIFSAVFESEAVGFEGPAFYNLAAAFETDLEIAELVLQLREIEAQQGRVRIGESMDSREMDIDVLLYGDEILHSQGVNIPRDEILECGHVLKPLSLIWPDRHHPVEGATYRQLWEAMSRDQGESLSLVVLDC | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
EC: 2.7.6.3
Sequence Length: 163
Sequence Mass (Da): 18132
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A0A946L459 | MSDFHIRQMELSDLDAIQAIEQQVYPFPWASQIFIDSMEAGSLLVVMERQQRIIGYAVQSTAAGESQLLNIAIAPSEQGRGLGRVLLQWLIEQARNANSEMIFLEVRFSNQTAQSLYESMGFNEIGMRKAYYRVQGGKREDALVYALQLLSDDYFGSVSETIG | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 163
Sequence Mass (Da): 18367
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A0A946DFW8 | MFRLFVLSALILVLGGCVTTPDTSEPVTDESHELWSQRQQQLSTIHNWEIRGRVALFVDDDVYNLGLDWKLGKNHSTLKLEAPLGQGLIQLDKKDSQVTLVTSEGKNYSGLNAEQVLLQSTGWSIPVEGLESWIKGINHDNSGYLPDIDSSGKALTLLQDNWRINFLQYKESLLANYNNPTLPHKIYMKRQNLALKIVIDQWQAQQNTTTTDLFPSFKN | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Subcellular Location: Cell outer membrane
Sequence Length: 219
Sequence Mass (Da): 24812
Location Topology: Lipid-anchor
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A0A660UIR2 | MRYRGIITVLWLLCLLSLPVMAAEAEHADPEEASHFKLFGYGPGEYLWTLVWFGVLLVVLWKFAWKPMLAGLTNRTEHIEKQISDAEKTRAEAKKVLGEYGAKLADAERQGRDIIGARTKEAEKQAKEVHRKTQKELQEKKVRAEADLDRERLEAADELWDQTGDIIRKLGQEVFGKTLDGDDNQKLIDEAIARLKEQQG | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 200
Sequence Mass (Da): 22828
Location Topology: Single-pass membrane protein
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A0A0K8URE6 | MNPVPNREYIEVCAAAIHHHQQHPYPQHQHQHHQHHQQHQAVALNTLLSNAPPPPPPPVQLPHPHDLKAPPHEHQPHCKQQCFVFTEIADIELPPEITKLGGEKLKNGAITAAAYKMSACSDSGSEPSRSSRNRRLIVVLGIMLVCIAMAGGIPLALQLRSSSLLEARLAFIRRLLTESPLIEGSSWQPPMRGTVNRSSGGLLNEVRRNHVGAVFWPISVPCGAQYLDAVQLALEGIDEARRITANTDALHIVLSADEMEQTHIRGEVAVMLGLGGGHTLGASLAVLRSMYLLGARFVSITSLECTTPWAAACIRSHDYLFEENATHSINEFGKVGSRSMGSDSNFFVLHPCRQCFTK | Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
EC: 3.4.13.19
Subcellular Location: Membrane
Sequence Length: 358
Sequence Mass (Da): 39259
Location Topology: Lipid-anchor
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A0A496XIR7 | MSRSLYLALPILLILAGCAGQDTRDTSYPSWPEHRSALQQLEHWTARGKLALRSSERAETATLLWQQQGLSTELHLSGPMGVSATTITSDGQQMEIRQGDEFKTFDISTPDAIALNTGWDLPLHALLYWLKGIPVPESPVQLLELDPDRDLLRKLRQNGWEIHYEQYEQFKNLTLPTRLRIQRGSTSARMIIHDWQAQPS | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Subcellular Location: Cell outer membrane
Sequence Length: 200
Sequence Mass (Da): 22757
Location Topology: Lipid-anchor
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A0A455AF10 | MLMVCIVIGARKLGVNPDNIATPIAASLGDLITLSLLAFVSSFFHKHRDSRYLTPLVCIGFTALTAACILIAKQNPPVVKILKVGWFPIVLAMLVSSIGGLILNKTISKQQFQGMAVFAPIICGVGGNLVAIQTSRISTYLHLWSTPGILPLGMKERWPNPRSTFCSSAPEGMTGLVPVAGHAAHAAAPDQLHVGPRPALPGGSGPPHLLLHHLPGGRPVSPKRQNLRGALPAGGPGPGNDGPWVPSWERSLDTQDTVPTFEKSSQSIQPQGRDPDTLLRARVDFSQAVFQDSSWEGRGLCRVMVGSGGHSHEGGVSMSVTLKDRLGSLGNCPEQLQGSGCGAPGPDQGLRCLHEGPAGRSCPGWASGKSELHQPDPCPSLRAGGGAGRPPSCASHPRGAQGGPGVAVSTVVSALDMCWFLGDMGFLLGHHLVSAHLVTGDDPAVPGGSDGSADVEPGPGPG | Function: Acts as a magnesium transporter.
Subcellular Location: Membrane
Sequence Length: 462
Sequence Mass (Da): 47778
Location Topology: Multi-pass membrane protein
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A0A2E3E9Y5 | MATKKTPKKKAASKRKHPVSAWKRVEMARHPRRPMMLDYVASCFDDFIELHGDRHIGDDEAMPAGLVRIGGIKCMVIGHEKGRDTDEKLKRNFGSAGPEGYRKALRMMKFAEKFKLPVISIIDTPGAYPGVGAEERNIAESIAYNLREMMLLRTQIIAVVIGEGGSGGALGIGVADKVMMMENSYYSVISPEGCAAILWKDRKYAPDAANAMKLDAKSLKRLGIIDQIVREPSKGAHTNPSLASKNLKDSILDGIKELSSVPLDQLLELRYKKYREIGEFTG | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
EC: 2.1.3.15
Subcellular Location: Cytoplasm
Sequence Length: 282
Sequence Mass (Da): 31177
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A0A348RX18 | MNVVIIVAAGKGARMGVDKLWLEVDGTPILGHTWRALDTIAEIDRIIIVARDERHQAIDQLAGEIRVSKPYELVSGGAERQDSVWNGLEACPESCEIVAIHDAARPCAHPVLVRECLKEAHRYGAVVAGRKITDTIKRADDSQSIESTVDREGLWAVQTPQVFRLNLIREAVEKVRLAKKVFTDDTAACEHAGIPVKIVPSDYPNPKVTYPDDLPYVSWLLANQSRGV | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Length: 228
Sequence Mass (Da): 25164
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A0A967QZD7 | MPLSEFELIERYFARGPVARGDVRLGVGDDAAVLAISAGHEAVAGLATVVLAGQPPARRDPRRVGHHVLALALSRLAATGAEPAWATLSITLPAADEAWLAGFRDGFSALAERFGVQLVGGDTTRGAGVVTVVAHGLVPRARALRCDGARAGESIYVTGSLGGCALAERPGQTLRDSMPRVGAGVALRDLASAAADIPCGLARGLTTILRASGLGATLQAASVPLEPALGGDPRSLGGWPGVLTSGGDLELCFTVTPARAAQAEAACAVAGARATRVGYVESASGLRCVGAQGERIPLEDMR | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Length: 302
Sequence Mass (Da): 30581
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A0A968BKX0 | MTEEFKLPELYITPEHECSYLPDKHASTLFVNPQARKNNYLYSYLSSKGFRRSGEQLYMPYCTHCQACIPVRICVVEFKPDRNQRRILKKNSSLDISIEAVAFRDDEYELYCRYLGNRHSGSAMCNPSPEDYLSFLNSSWSNTRFHRYTLNDKLIAVAVVDYLNDALSAVYTFFDPEYSARSPGKFAILHSVNIAGELGLKWLYLGYWIEKCSKMNYKNRFQGIEYYYRQGWTSRAPGTKE | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) + N-terminal L-leucyl-L-aspartyl-[protein] + tRNA(Leu)
EC: 2.3.2.29
Subcellular Location: Cytoplasm
Sequence Length: 241
Sequence Mass (Da): 28197
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A0A2E5RIQ9 | MNQLQEKECMKRAIKLAEFGMHTCKPNPRVGCVIVKEGKVIGEGWHKRAGGDHAEIMALKNCELNPEGSIVFVSLEPCTHQGRTPPCIEALIDANVSAVVFSSMDPNPEVSGRSIDMLNAAGIEVSHGLLEEESSELNIGFFHRMRFNRPFVRSKLGSSMDGKIALSNGESKWITSDASRKDVQNLRARSCATMTSNQTVLVDDPSMNVRIENFSTDDQPLRIVVDSSGKCSGNEKVFQLPGETMIHRDRANESLFEHLGSIEINNVLIESGPKMNGALLESGLIDELIIYMSPCILGSDAIDMFVFPAIEKLSDRFSFDIHDLHKIGTDMKITLRKKDV | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+)
Sequence Length: 340
Sequence Mass (Da): 37577
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A0A2E6M2N0 | MTQVTKNVFLLGATGSIGENTLNVIRRHPDRYNVFGLTGHSNLKLLAELTIEFNPQYVVLTSTDSLSTFKSLLKGHALRTEILEGQDELLSLIVKPEIDVVIAGIVGKAGLEPTLAAARAGQYILLANKESMVMAGPLFRKAILESQARIFPIDSEHNALFQTMPGELQSSSLVTQAACESHGIHQLVLTASGGPFLHTPKEELVNVTPAQACKHPNWAMGAKVSIDSASLMNKGLELIEACYLFGVSQSFVDVVVHPQSIVHSMVTYVDGSTLAHFSNPSMEVPIASGLAYPERHTTGVKPMRWDQMLELQFLPLPYEKFPCFSLARQAMAQAEKGQGATIVLNAANEIAVDAFINGKLGFTQIPNLVEQCLDRFGVTEAHDLADILALDQEVRDAAIDYL | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 402
Sequence Mass (Da): 43674
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A0A967H2R3 | GGSGREVVACITSMADELIRNLYHCAAAEFPTEGKVCSAVIALGGYGRAELNPLSDIDVMFYCSDKNKDFAEKIAERVLYLLWDLNLDVGYSVRTANDCMSLAQQDITIRTALLDTRFLAGDESLFREFEKHVFQPLLNRNTQSFLKYKHQEHVERQGKYGSSVYMLEPNIKEGEGGLRDLHTAVWMARVKFKAKSMRDLLRKGVLSESEFLDFEAAYDYLWRIRNQLHFESKRKTDQIQFDMQEQIASFLGYKGNKSALPVEQFMQDYYAHATSTEHLASTLIYKSYKEEKQESKSILRYLGKRSLGDDFFSYRGELKTARTNLFADKPAALMQAFLLTKQNDLDLSADVKHQIRDNLHLVNDSFRRNREISKMFREIMRGPTGAAKCLRDMHHVAFLNKYIPEFKRIYCKVQHDAYHVYTIDIHSIFAVEELEKLWSGFYKDKKPLYTSVANDXXAFIYQRRK | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Length: 465
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence Mass (Da): 53962
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A0A8T7D6B8 | MTLTVEVSISDELASDGSELSDDEVPESETLQSWAAAAYLGDAPALASLLVTTADEVRSLNRQYRDKDKPTNVLSFPMQSPDEIDVSLLGDIVLCAPVIKQEARQQGRSAASHWAHMVVHGMLHLQGYDHIDNRDAERMEQLEIDILDQLGFANPYEDITTGNLSDHSNR | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 170
Sequence Mass (Da): 18763
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A0A182DZF7 | MDCKEVSSCLLLPFMIVTMLPHTGLIAIERVIQRRCSLFLRHRFISIPTVTRRNVESVSNKEMKMSQSKSILEKVIMKESQTTVEKVKEKATNAYLYVAYVVSVVVMGGMAYLLYEEMLSPGAPQTVFSKALSLIKKDPECHKLLGDSIMGYVEGRGRMKQVPHHIYKKDGKDRTRIMFNVKGTRREGIATCEMEKNNGTWEWRFLIVSSADLIPEYVVLIDNR | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Location: Membrane
Sequence Length: 224
Sequence Mass (Da): 25640
Location Topology: Single-pass membrane protein
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A0A0D8J376 | MPREVLSILVDNHSGVLTRVASLFGRRGFNIDSLTVSATDDPAISRITIVVHDDAKVLEQIIKQTARLEETREIFPLDTAHSLLRELLLVKVEAGEENRSAIREIANIYKAKIIDLSIGSMVMELTGEPEKIDGFLDVLSPYKILEMCRTGITALERGGVHRHA | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 164
Sequence Mass (Da): 18215
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A0A1N7BQ68 | MTDLLETARDVQSNAHVPYSEYPVGAALETADGEVFVGCNLENANYSNSLHAEEVAIAEAVKNGHREFTRVAVSSGQRDGVTPCGMCRQTLAEFCDDDLVVLCDRGDDEPPAEYTLGELLPDTITEEMLE | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Length: 130
Sequence Mass (Da): 14126
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A0A814P0G5 | MAESSRGAGGSRTRVAKTSRLHKCTKYVKRRLPSSIAWLILIVLSALYFVFICPYITQHLSLAIPIVQSILLLFVIINFLLATFMDPGRYERATQDENDQDEGIYYKTVEIHGTNSRMKWCQTCQFYRPPRCSHCSVCDYCIDQFDHHCPWLNNCVGRRNYRYFFQFLCYCMLHMFTVFSFTIYFFIVYGRFHFTSLSTIVSLVLFTFIILLTVPICGLTGFHIVLICRGRTTNEQVTGKFKNHLNPFDDDCCTNWLKTFISSNIPELRYIVKTKPRSSVVTQQTKKSRSAAYDSRSDHNKKVQPQKLYVPPTSNNNGNVVTKNKSITTFHHPHSLGLSNGHCHNHHHPQRQSTSTNRRSSTHHHHNRTRKPQRHNYYSTRLLDSSPVMSGLSTTGNFKTMQIPSSAIDIPTVMYYPLPLMKLLQNEEQVAQPHSKEQILSPTNYYSTKNGQHRIDSSRMMSGGEHTKTELKFKV | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 475
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 54918
Location Topology: Multi-pass membrane protein
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A0A6P7TKX3 | MNHSLTNLWAVLVACRIIWTLWPQQGYIHPDEFFQSTEIVVGDILNLDVERTWEFNSTQPLRSIFFLHLIYGLPVRLLAFLQKLGLFEISPYLLIIVPRLAITALMFTVDAVLWKSSKCLGIKPWFSLCLYASSYVTLTYLTRTLSNTIECLLFAIILYIVLPKFGAAYGSLSSSRRSRKRQKKNEEQQSPASVVDNSASAKGNKKAATSAKSANAVAAASSSAASAPGKSGKGKQKGKKTKTNPGSNTAPHGQQQQQKQKQQKQQQQKQQQHQKQQQQQKQQQQQKQQQKHSQKQQKQQHQQQQHHHQQQQQVLNSQKPHQTFSETDFVKTELFVLACCTVAGTFNRPTFPVFAVAPILAWFYCTSCTKPATLVKNIALFALFSLPVCVVFVCVDTFYYRISPTDFFNALDSCMHVGGPAGATLCAWRVLASHVTVTPFNFLLYNTQVTNLAEHGLHPSYLHVLINMPLLYHILYILFFYNIYQCFSQTAKLLIPSCVLSLFIVVPVTILSIFPHQEPRFLVPLLPLLVLIGAQVIEQCKWKFALHLSCTWVVANLVLALFYGFLHQGGVIPSLMSAKYNQISPPLDSTGISAPCGSSSSRQDHLVFYHTYMVPKHLLLNRHDNITLVTHDLKGGAMPLLTDLLHKLLSDNNNNDNENPLVPGACSVRVVLPATIADAFKRAQQCGVQYLCNEERWFAPHLSLEDPPLRLFGRTSSDGDLWTGWSLGSVFKDLHLKMFQIKKIML | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 746
Sequence Mass (Da): 83936
Location Topology: Multi-pass membrane protein
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A0A2G6KQL6 | MSSETGERVAITFDDKLGCRSMQTTDLPAVHAMEVENNPFPWTPGIFRDCLRHNYQCLCLLRECDFIGYAILQIVKDESHLLNICVDHSLQGQGYGQRFLEYLMRESVERGARTLFLEARSSNTKAMGLYAKVGFHEIGRRRHYYQNDGQREDAIVMACELIGVN | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 165
Sequence Mass (Da): 18913
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A0A6N8UL85 | MKLDPVAISPRIRNPILLALVAAVTFVLLAAYSPLDPEWNQASNNEAVRSFLGSVGSFLSGSLTLAIGYVSYVIPVLLVAKILSIVALPRETRWWIGLVSLGGFLLVVLSLCCLAAAWTGSPNAAIEVTSGKVGSLLASLLFPFVNVKILAVVGSVGVLLGIRFLIRFSWLPLIETLGRCLYVVATKGSRFLIDCIQWIFNLISKRGSNTLEERTVRSRTKATVRSRPVSVSRGTADSKRQEPQLKAKAVQRPRASTRTQTAKKHIRDVAKLPDLSLLAEFRAAPVTANSQQLINRIYEQLGTKLADFGVEAEVVSKFTGPVVTRFEIQPAAGVRVSKITALAKDLARALAVLSVRVVEVVPGKPFVGIEIPNDERSIVRLQEILKVVRRSGEMDSALKVVLGKDVAGNPILADIEKMPHLLVAGTTGSGKSVCINAILLSLLLHSTPENVRMILIDPKMLELASYEDIPHLLTPVVTDVQDASRALGWCIGEMERRYQLMAALNVRNLAGYNALVDAAEKRGEPILDPIGAELGSTDGTTLTKLPSIVVVVDEFADMIMVVGKKVEQLIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPCRISFQVSSTTDSRTILDQGGAEQLLGHGDMLYLPPGSGVPVRVHGAFVSDEEVLKVVEYWRTRCEPDYVEEVTSLDASQSAHSVFSLQQSEDEQDENFEEAVSFVLQSRKVSISSIQRKFRIGYNRAARIVEAMEGAGIVSAPNEMGNRQVLLSES | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif.
Subcellular Location: Membrane
Sequence Length: 762
Sequence Mass (Da): 82674
Location Topology: Multi-pass membrane protein
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A0A6B1EQQ0 | MSSARAPDLAGLIGPVTGLACEAGRRILELFRSDVLGVDYKLDRTPVTEADQAAHDHIVAGLERLTPGIPVLSEESGAEQHARERSGWDWHWLVDPLDGTREFIRGGEEFTVNIALIRGKAPVLGVVDAPAKGVVFFGHEGGGAHSRTADSDTPSPISVRQPPAQPLRVLASRSHAGSALELYIGALGLTHRRAISSSLKFCLIARGEADVYPRMWPISEWDTAAGQAVLECAGGAVFDLRGRRLRYGKDSISVPPFIACGDPAQDWLDYLP | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
EC: 3.1.3.7
Subcellular Location: Cell inner membrane
Sequence Length: 272
Sequence Mass (Da): 29232
Location Topology: Peripheral membrane protein
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A0A6B1GI74 | MVVALKAPRVFLASSSPQRYRLLQAMELDFSVISPDIDETPKNDESPSNYVLRLAVQKSAEAVQMAPQSTLERIFVGADTCVSIDEHKLGKPENMAEARQMLELLSGQIHQVYSAVSVTNCRITRCVVAVSEVEFNQLTETQIQSYLASGESENRAGAYAIQGRAVAFIKRVVGSLTSVIGMPVKETAELLELTGVSVPSYASVAGNVLAEFQFEHCWPDDYYI | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+)
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Sequence Length: 224
Sequence Mass (Da): 24581
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A0A353DXB4 | MSKKKRPKKQETLVTVETLTREHGEELMLQPMGEPCGLNRRIREPTVNRPGLALVGYKKYFASKRVQVFGSVETTYLRSLTPKEREDRYRWIFATRIPCVVFSRNLNPDTALLSAAREACIPVFKTPLITMRFINLATLALEMMFAPRRNEMGCMVDILGVGVLIRGESGIGKSEAVLALIERGYSLVADDITKVTLIDNQHVVGTSYETTRNLMEIRGIGIIDVAAMFGVRSVTREKQINLVVTLVHWDKAQTIDRLGLDEETTDILGVHIPHIVIPVRPGRDMGRLIEVAAFQTKLKMSGIHSAQALSERLMEKMTRDRDSHA | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).
EC: 2.7.11.-
Catalytic Activity: [HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H(+)
Sequence Length: 325
Domain: The Walker A ATP-binding motif also binds Pi and PPi.
Sequence Mass (Da): 36584
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A0A2H0ZPR8 | MGTQIVVKKPLLIKLIKSKLEIADALDKSRKISKKDGNALLYSTASVSELSTLLREYEKEISMTEDDSRPIERKTHLRDEVADIIGEYHNELLATVPKKWSLYPPMVLFNNGTFDTPDWANYFLKNGTTLLFDHLSDSFFKGYTHYAVNKPIIEEDVMRRPFSLVPLHGDFGPEPTTQMFESPSGLDIERTFWCTVTQNGISQEWAPRYTMFSRGNITEKKRLLDSYRNLTGEDVVDLYAGIGYFTLSYLANGATVYCWEINPWSIEGLLRGLKKNGCKFCLIKDGDNFDATTHSEALGSGVNAFVFHESNEHAVERLSRLDLAIAHYNLGLLPTSRQGWEVVRRLESHKSKGPKVSPALVHAHENVHKNDFDQIVKEIETFFDGRVIQLNKVKTFAPDIWHIVLDVQLQI | Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
Function: S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86.
Subcellular Location: Cytoplasm
Sequence Length: 411
Sequence Mass (Da): 46831
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A0A945B0T4 | MRNKYLTQLIKAAVLISSVILLQACSSTRLQVQPDPMFAPVDLKQSRFQPVNNGSIFQQGRSVRLFEDSKAFRVGDLLSISLSESTNATKSAATNTAKDDDVTLGAGTFLGVSPTYKGNALMDNALTAERAFKGSGDTAQSNSLKGEITVMVSDILPNGNLVVRGEKIIGLNQGSEFIRITGIVRPQDVSSNNEVTSGKLANSRIYYGGGGVIAEANTKGWLSRFFSSPVFPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Location: Cell outer membrane
Sequence Length: 233
Sequence Mass (Da): 24960
Location Topology: Lipid-anchor
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A0A817Q0G8 | MAVISFGSTVDLEAGQRRKNGLSLPLHYIQLLGIIFMVFLILMNYLTLCVNIPTHPWQWLSIVISSVIILPFVTMFIIITYLDPAEDAVLNLHRGPKAKFDRRVHEHVITNLYCNICEVQVTSNAKHCSACNKCVYSFDHHCIWLNTCVGGKNYRIFFSMLIFIVIGTFFIFINSLLQFIGTFQNSSSAISLKPFYSTGKYKIYSTVFNTKEIGSSIHLLIKL | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 223
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 25398
Location Topology: Multi-pass membrane protein
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A0A6N9D276 | MKTPLIVANWKMNGNQLLCRQFSETLECPANGEVWIAPPSLYLETLAVDKKLRNFVRVGVQNVYGKSSGAYTGEVAATMVRESGGTFAIVGHSERRTQFNESDSFIAQKFYASIEADLIPILCVGESLEEREAGLTYAVVEQQLTEVIDTSGIKYFHKSVVAYEPVWAIGTGKAASPVNAEEVHVHIRQVIAKYDDQFIPILYGGSVNENNVGELWEQHNIDGFLIGGASLNPHTLNSIIGEITR | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 245
Sequence Mass (Da): 26963
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A0A946SIA9 | MMALIMINKNKIVLKIIICLTIILSTNLLSQTRELGGTGEFIDGIAAIVNDGVILRSEVEQQLTMIIANLEKQEGRMPPIDVIQEQVMERLIIQRVQLQRAERFGVRISDEALNAAITNVAQNNQVEFKDFPKILEAEGIKYKDYRKELREQLTIDQLRQRDVASRISVSESELESFMVLQKDQDALNYDYNLSHILIPVSSSSSNNEIKKAENLINTLYEKISNGENFESLAVEFSKGQQALNGGNLGWMQGEQLPNIFVQAVNLIETNQLSQPFKSGSGFHLLRLNAIKGNDPILEDQINVRHILIKTNEVLDDSAAEEKLKTIRNQIINEGDFGAVASAISEDSGSAQEGGDMGWTAQGFFVPEFELVANSLSENEISMPFKTGYGWHIIEFLGKRTFDNTEEIQKRKAISAIRNSKLSDEIEIWARELRDEAFVEILPYN | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Subcellular Location: Periplasm
Sequence Length: 444
Domain: The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Sequence Mass (Da): 50021
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A0A6B1EFU2 | MRYYRQPNKGVLHTRAVPSVAGVSTSIKTTALKINSGEPRIAARQLPSNVVRVLRGLHRAGYRACVVGGGVRDLLLNLQPKDFDIVTDARPEQVKKLFRRVLLIGRRFRLAHVMFGREFIEVATFRGSGNEASDPEGSVVRGTNGRILRDNRFGSLEEDVLRRDFTINALYWDYADKRIIDHVGGLKDIARRRLRLIGEPRLRFEEDPVRMLRAARFAAKLGCELDVRCAEPIPEMARLLRAEPPARLLEEVRKLFLGGHAVSSFEELRRFGLLDELFPFLGPWMDEEPRAEGFVRDALAATDKRLSEGSHASLMFLLCVFYWGPISRAVAPGGSRIPRYTQITDAFRRMVRDSQYGLRPTKKMMADMEHVLGRQALLQARPRRRVNQTLKHPLFRPAYRLLCLRRRLAEIDEQCVLYWRKRAGSAPSRSWSKRRRHGPGRAGGRSANGNEKKVR | Function: Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control.
EC: 2.7.7.19
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Length: 455
Sequence Mass (Da): 51993
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A0A945T4B9 | MSRFTRFKERFFWPDSTYATCGLAWSNHFILDHPLIQSITNGTPEAIGLRAETLRKESTADAIIILDIHGTILYHSFTPERLGASLMSWNIVRNSLLGESLDSSIVQDLDNFIIYSPSLVSDNLGEIIGLVLVGYAINDHLLQNISQESQIEITLVRRRAVMASTFSRPESRMSTIPLSYISYQSMLQNPKSIKSFEYGGIEYLAIARRLSRMAKNQEGSILLTFPRQGLNEVKQRLLWEYGILFFVEFFLIALISARFSGNLLRPIYQLIEQIEQSDKTQELQFTSIDSGGEIGIIANRFNQLVGTIHKQNSKLRNYSASLEQKVEERSLALKNAYETLARKERSLTHAQHIAKIGSWEWEIHSDHLHCSEEMLKICDIPTDQFGGTLEEFTNTLAPNQRESFTIELRHSARAASTFHGEYTVYHKNGDEYALLIETEITEDSEGNPTAVSGTIQDITERKLAEVERQQYQERLEDLVAVRTSQLREEKERAEAANEAKDNFLAAMSHELRTPLTTIIGNSEFLAEQETNKDKQELISAIETAGRGQLALVNDILDISKIESGKFTIDEAPYEFSVLLQDIQHMLTTRAHDAGLTLEVKQTNQEKHLLIGDAQRISQILINLIGNAIKFTESGSITLTTRANNHHLIFQVKDSGIGMSPDTVDHLFQRFEQADGSISRRFGGSGLGLFISESLADMMGGVIDASSREGEGSIFELILPYQPSTLLARKGQNHSETRPVLNKQLEGHVLIAEDTPELQLLERRILEGMGMTVSCANNGEEAVELATQQSFDLILMDMQMPIMDGIEATQALRQRGYKHPIVALTANVMQKHQDAFNSAGCNAFLAKPIDKQKLYEILEQCISDRHHTPDPAVDEEVGEEVDDELMTIFKASAANNKKILTDALHEKEWNNIRQVAHNIKGSGASFGLPNLSLLGKVVCDAIDEGESEQLSQQVTDLIIELEKIEGTSKNTSFSQ | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 974
Sequence Mass (Da): 109172
Location Topology: Multi-pass membrane protein
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