ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q9FY49 | MAPIDPHSFTDSSHPLTTHVALSLYLDFNTSIIHGSALLTLSSAFSGELSLDTRCISIAMVLDPLTLEPIPYSVSTTPDRIRGTEVVVVLSGQSSLLIVYSTSPSASALQWLSPLQTFSKLHPYVYTQCQAIHARSIFPCQDTPAARIRYDVVMNIPNSLSAVMSARHVRRRLAVPEEAKHLEAGSLGSSLWCGEDRVVEEFAMEQPIPPYLFAFAVGELGFREVGPRTRVYTESAAIEVLDAAALEFAGTEDMIKQGEKLFGDYEWERFDLLVLPPSFPYGGMENPRMVFLTPTVIKGDATGAQVVAHELAHSWTGNLI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
Q75B10 | MKLPAVLEERRAAATDRSTLSNYEDFAVRHTNLELEVAFDERQIRAEVCYDLEQTGKGVAEVHLDTSYVQLECILVDGKRVPWELRERQEPLGSQLVITPEGGLPARFQLTCRSVTTARSTAVQWLGGAQTAGKPYVYTQLESVHARSLVPCFDTPACKSPFTVRVRSPLRAVVAGQEQPGSGKDGVYVFEQPVPIPIYLLGLAAGDIACAPLGPRSNVYCEPALLEAAAGEFGGEIERFLDAAEELLPRYIWGNYNLLVCPSSYPYGGMEVAGTSFISPSVIAYDRSNNDLIVHEMAHSWSGNLITNANWGHFWLNEGW... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
Q59NB8 | MTRAIVESIKKRFHELDPCTNSNYSKFKVIHTDLTLTVSFESKTLDGTVVYDLKNLDNASEVILDTSALNIKSTKVNGKEVSFELKPVTPIYGAPLRIPINPNESEIQVEISFTTTDKCTAIQFIQGDTGPYVFSQCEAIHARSLFPCFDTPAVKSPYKFTGHSPAVVTMSGRAQPTDEPNTYHFDQPIPIPSYLVSITSGNLLKAPIGPRSDVYSEEPSLKKCQWEFEKDMENFIQIAEKIVFEYEWSRFDSLVLPSSFPYGGMEIPNMTQLTPTLISGDRTQTKVMAHELAHSWSGNLVTNSSWEHFWLNEGWTVYLE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
Q6FTM0 | MINRLIQRIVPFSRPLSTVKKTMLTPFLESKRPQQSPEYDYSTLSNYKSFQIKHTTLNFLLSFEKSTVSGDVVFDLTTLKEAVKHIDLDTSYLDVNEVLVDDKPVEFKIEERKQPLGSKLVIAAELEAERQFKLRVKFSTTKDCTALQWLTPQQTSGDKPYMFSQLEAIHARALFPCFDTPSYKSTFTANIESTLPVVFSGIATGSTPNGESTVYHFKQDIPIPAYLVGIASGDLVSASIGPRSKVYTEPHRLDDCVWEFSNDVEKFIKTAENLIFDYEWGTYDILVNVDSYPYGGMESPNMTFATPTLIAHDKTNIDVI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
Q2GY21 | MAPVRDPNTLSNYNEWRTKHTTADFKVDFTAKCLRGSVVLELESQTDKASKEIILDSSYVDVSAITLNSTPSQWEVRDRTGPSGSPVRVAVPNGAGKGEVVKLEIELATTDKCTALQWLTPAQTSNKKAPFMFSQCQAIHARSIFPCQDTPDVKSTYDFIIRSPHVVVASGVPVPGEPESVGEDKVYKFHQKVPIPSYLFAVASGDIASAKIGRCSSVATGPNELKASQWELEDDMDKFLDAAEKIVFPYQWGEYNVLVLPPSFPYGGMENPIFTFATPTIISGDRQNIDVIAHELAHSWSGNLVTSCSWEHFWLNEGWT... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotrien... |
Q96L50 | MKLHCEVEVISRHLPALGLRNRGKGVRAVLSLCQQTSRSQPPVRAFLLISTLKDKRGTRYELRENIEQFFTKFVDEGKATVRLKEPPVDICLSKAISSSLKGFLSAMRLAHRGCNVDTPVSTLTPVKTSEFENFKTKMVITSKKDYPLSKNFPYSLEHLQTSYCGLVRVDMRMLCLKSLRKLDLSHNHIKKLPATIGDLIHLQELNLNDNHLESFSVALCHSTLQKSLRSLDLSKNKIKALPVQFCQLQELKNLKLDDNELIQFPCKIGQLINLRFLSAARNKLPFLPSEFRNLSLEYLDLFGNTFEQPKVLPVIKLQAP... | Function: Substrate recognition subunit of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins . ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction dur... |
D3YY91 | MRLPCEVEVRSCHLPTLGLKSRGKGVRAVVSLCQAPGRNELQPEARAEPGGHACLLVSTMKDRQGTSYKLRENIEQLFTKFVDEGKATVRLKEPPVDICLSKANPGNLKTLLSAMRLAHRGCDVNTPLSTLKPVKTSEFEKYKTKMVITSKKDYPLSKNFPYFLEHLQASYCSLARVDMRMLCLKNLTKLDLSHNCIKKLPATIGDLTHLQELNLNDNQLETFSVPLCTSTLQKSLHSLDLSKNKIKALPVQFCQFRELTNLNLNDNELIHLPFKIGQLTNLRFLSAARNKLRNLPSEFKMLSLEYLDLFGNTFEKPEVI... | Function: Substrate recognition subunit of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins . ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction dur... |
Q5ZT84 | MQNNNPCGLDGFAFLEFSGPDRNKLHQQFSEMGFQAVAHHKNQDITLFKQGEIQFIVNAASHCQAEAHASTHGPGACAMGFKVKDAKAAFQHAIAHGGIAFQDAPHANHGLPAIQAIGGSVIYFVDEEHQPFSHEWNITSPEPVVGNGLTAIDHLTHNVYRGNMDKWASFYASIFNFQEIRFFNIKGKMTGLVSRALGSPCGKIKIPLNESKDDLSQIEEFLHEYHGEGIQHIALNTNDIYKTVNGLRKQGVKFLDVPDTYYEMINDRLPWHKEPLNQLHAEKILIDGEADPKDGLLLQIFTENIFGPVFFEIIQRKGNQ... | Cofactor: Binds 1 Fe cation per subunit.
Function: Catalyzes the transformation of p-hydroxyphenylpyruvate into HGA. Has hemolytic and brown pigment production activity.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 38923
Sequence Length: 348
EC: 1.13.11.27
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Q9H0V9 | MAATLGPLGSWQQWRRCLSARDGSRMLLLLLLLGSGQGPQQVGAGQTFEYLKREHSLSKPYQGVGTGSSSLWNLMGNAMVMTQYIRLTPDMQSKQGALWNRVPCFLRDWELQVHFKIHGQGKKNLHGDGLAIWYTKDRMQPGPVFGNMDKFVGLGVFVDTYPNEEKQQERVFPYISAMVNNGSLSYDHERDGRPTELGGCTAIVRNLHYDTFLVIRYVKRHLTIMMDIDGKHEWRDCIEVPGVRLPRGYYFGTSSITGDLSDNHDVISLKLFELTVERTPEEEKLHRDVFLPSVDNMKLPEMTAPLPPLSGLALFLIVFF... | Function: May be involved in the regulation of export from the endoplasmic reticulum of a subset of glycoproteins. May function as a regulator of ERGIC-53.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39711
Sequence Length: 348
Subcellular Location: Endoplasmic reticulum membrane
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P59481 | MAAASRPSWWQRWRRRAWARDGAKLLLFLLLLGSGPGPRHVRAGQAVEYLKREHSLSKPYQGVGTSSSSLWNLMGNAMVMTQYIRLTPDMQSKQGALWNRVPCFLKDWELQVHFKIHGQGKKNLHGDGLAIWYTKDRMQPGPVFGNMDKFVGLGVFVDTYPNEEKQHERVFPYISAMVNNGSLSYDHERDGRPTELGGCTAIVRNIRYDTFLVIRYVKRHLTIMMDIDGKHEWRDCIEMPGVRLPRGYYFGTSSITGDLSDNHDVISLKLFELTGVRTPEEEKLHRDVFLPSVDNLKLPEMTVPPTPLSGLALFLIVFFS... | Function: May be involved in the regulation of export from the endoplasmic reticulum of a subset of glycoproteins. May function as a regulator of ERGIC-53 (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39881
Sequence Length: 347
Subcellular Location: Endoplasmic reticulum me... |
P49257 | MAGSRQRGLRARVRPLFCALLLSLGRFVRGDGVGGDPAVALPHRRFEYKYSFKGPHLVQSDGTVPFWAHAGNAIPSSDQIRVAPSLKSQRGSVWTKTKAAFENWEVEVTFRVTGRGRIGADGLAIWYAENQGLEGPVFGSADLWNGVGIFFDSFDNDGKKNNPAIVIIGNNGQIHYDHQNDGASQALASCQRDFRNKPYPVRAKITYYQNTLTVMINNGFTPDKNDYEFCAKVENMIIPAQGHFGISAATGGLADDHDVLSFLTFQLTEPGKEPPTPDKEISEKEKEKYQEEFEHFQQELDKKKEEFQKGHPDLQGQPAE... | Function: Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins... |
P49256 | MAAEGWIWRWGWGRRCLGRPGLPGPGPGPATPLFLLLLLGPVVADITDGNSEHLKREHSLIKPYQGVGSSSMPLWDFQGSTILTSQYVRLTPDERSKEGSIWNHQPCFLKDWEMHVHFKVHGTGKKNLHGDGIALWYTRDRLVPGPVFGSKDNFHGLAIFLDTYPNDETTERVFPYISVMVNNGSLSYDHSKDGRWTELAGCTADFRNRDHDTFLAVRYSRGRLTVMTDLEDKNEWKNCIDITGVRLPTGYYFGASAGTGDLSDNHDIISMKLFQLMVEHTPDEENIDWTKIEPSVNFLKSPKDNVDDPTGNFRSGPLTG... | Cofactor: Binds 2 calcium ions per subunit.
Function: Plays a role as an intracellular lectin in the early secretory pathway. Interacts with N-acetyl-D-galactosamine and high-mannose type glycans and may also bind to O-linked glycans. Involved in the transport and sorting of glycoproteins carrying high mannose-type gly... |
B8NWW2 | MTVTATERIVTVFGTGNQAGAVARALLADKTSQFKVRAISRHPDSASSRTLSALGVQVVKADGWNLEELTRAFADTWAAFVNTNSDDPLFLQKGDGPTEFDLGKNIIDSLVAAKVQHLVYSCFASSVEQTKGKLFIKPMEMKYQALKYARETGHFATTCGIYAAWYYEQFLDKATADVFGGFPTTPDEEGYITFRAPLWGDDEHPSFVSITHDFGDMVHGILLEPEQWDGKSVPAASDVMTFEQLAQTLQNATGRKSRYIPLPSWEDFGRGIPELDDHKLLFAFTQATGGRYFGDVPTETKTALRLKRRAAEAQGKSGNE... | Function: NmrA-like family domain-containing oxidoreductase; part of the lnb gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine .... |
B8NWW3 | MAARLLSSVSLTDVVLLLSSVWIAVHLVLAAYNVYLHPLRRYPGPKLAAASQLLNVYHVLKGDNCKWTAQLHEKYGTVVRIGPNELSYISPSANQTIFGGRPKEDKVFEKNPVAYLQGNGDISNIFFARFHDHNRLRKLMAPAFSETAVREQEATIQGYTNQLIAALRNRSGQAAYPDAKGVVNIIPWLHFILFDVLTRLSFGDPIGCLDRADYHPWVSVIFKAIIHSTYTQAAHRLAPYQWILKHFIPNDMTANYEAHLEFTRKQLDQRQQVKEEPVARADFSSFMLKGMSPDELFDNVNIVITAGGETTASTISSSLY... | Function: Cytochrome P450 monooxygenase; part of the lnb gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine . The lna and lnb bio... |
B8NWW6 | MMSKLFTPLQVGFCQLKHRVIMAPLTRFRADDNNVPLPIAKEYYSQRASVPGTLIIAEATYISLAAGGYPNVPGIWSPEQIARWKEITDAVHAQGSYIFLQLWALGRVGDADTLKQDGFDLISSSAVPVDAGEPVPRAMTEEEIKQYIALYAQAARNAVMAGFDGVELHGGNGYLVDQFTQDTCNRRTDSWGGSIPNRSRFAVEVTRAMVQAIGSERVAVKLTPWNDQQGMKMKDMEQQFLHLITSLKELKLAYLHLTNPRVSVDEDVPLQGPPDGHPLEDNAGFVKAWGETSPVFLGGGYTPQSAKHTLDVDYPLNEIG... | Function: NADP-dependent oxidoreductase; part of the lnb gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine . The lna and lnb bio... |
P30639 | MKKILPIIWLINLVSGSLSLEKKAPDLLGKVCAFGDFNADRNTDILVFANGTLTINYQETKLLDVLEASKFTPGTSFAISKPSLNADFVECSVGDFNGDSRLDVLVSIRDKDTEIYNHTLWTSEIEDEKEIFRPFHVAMLQQHAMAIDVSDDGWTDVLGFYPNGSMFCTGFNKEGKYNLLVNGCKHEFVAFPEKLNIYPGMPHLFVDLNSDLIADIVFMTKESDGSLFMSVWQKTKISWQFRDWVPKLTPAQYPFVGAPVVMDVDSDGELDILVPICREDECSHITQMASWSKTKLWGLVACDMQDYTVIKEPFSRVIFR... | Function: Probable cell adhesion protein involved in gonadal cell migration.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 67593
Sequence Length: 599
Subcellular Location: Apical cell membrane
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Q9ZI86 | MRWISRPGWPGHLLALAAGALTPLALAPFDYWPLAILSIALLYLGLRGLPGKSALWRGWWYGFGAFGAGTSWIYVSIHDYGAASVPLASLLMLGFTAGVAFFFALPAWLWARCLRRDNAPLGDALAFAALWLALELFRSWFLTGFPWLYAGYSQLQGPLAGLVPVGGVWLSSFVIALSAALLVNLPRLFPHGASLLLGLVLLLGPWAAGLYLKGHAWTHSAGEPLRVVAIQGNIAQELKWDPNQVRAQLDLYRDLSLPQQDVDLIVWPETAVPILQDMASGYLGAMGQVADEKNAALITGVPVRERLADGKSRYFNGITV... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
Q8Y210 | MRALFSSPAADTAGQQEALAVPLARLRFAAPLAALLGVMHTLAFAPNRWWWLQILSLAGLAALVRQAPRLRDVAWVGYAFGLGWFLSGIWWLYISMHVYGDMPAWMAAAAVLLFSAYLALHPALAAWLWQRLARGRQLSGAASALVFGAAWLVSEWLRGTEWTGFPWLNGGYAHTDGPLAGYAPLVGVYGVVAIAATLAGLLCAAAERRLHWLAGLAGVAVLAAGWPLHTIAWTQPVGKPITVRLLQGNVPQDVKFQQTGIDHSLALYTKMVTEQPAQLVVTPETAFPILLQDMPQEIALAIRTYVDTTGSSVLFGAANA... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
P58377 | MERLAGRIILLSGVSRTFVGFLAGLLAVLAQPPFGIFAAAFVSFPVLVWLIDGVAPDPGDGLLRRLMPPAAIGWSFGFGYFLGGLWWLGNALLVEADAFAWALPLTVVGLPAVLGLFYALAVVIARSLWSDGWGRIAALALGFGIAEWLRGFLFTGFPWNAIGYAAMPMPLMMQSASVVNLSTINMLAVFVFAAPALIWTGKGARAGLAIAAALFTAHVAFGFYRLAQPAPAPLQPEMTVRVVQPVIDQAKKLDDRERASIFEDHLSLTAAPVQDGAKRPDIVVWPETSIPFILTDNPDALARIADVLQDGQVLVAGAVR... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
Q7UGJ8 | MRWLSAASSAFAVVLWLSGPPFAIGPLVFIALVPLLAIAEVSPSSSWKRPLYAASLAYWLLSLQGLRYAHPLMFLPWIALSGYLAIYPVLFIALLRRLRLVDNCDVSQARRDRVPLCLVAAVVWVGLEWIRNYFFTGISVLMLGHALADMPMLIQIADLGGTYAVSFVIVCVNVAMFDALNRWVVQRTSSVSDSPMKSLVTAGGLLIATMVYGAMSMNAETEPTGKTIALLGDNELTVYEQDIVREQEIFATYGQMAIDAVAKSNTRIDAVVWPESMFSGGLPWMTTGADLVVPDFMQNPAAAPLQPEQLRFAVESKQND... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
Q9ZDG3 | MYKTKIICLLLGILSGLVFAPIFFIPALFTFSYLCYIVQKSQNWQVAAKFGYLFGFGHFLSGMYWISIGVSVYIADFWWAIPFALFGLPIILAFFISANCTLSFFAKNNKYYQLIFCLLWVLFEWIRSWILTGLPWNLIGYAFSFSEILIQPLSITGIYGLSFIVIYISTSAYPVFTKKFTQLKILLASSMLILTVMVIYGAVRVSTNPTNFTDIKVRLVQPSIPQTAKWDQEEFWHNLMLHINLSENLEPTDLIIWSEAALVVPDDIPQVKLKLLNMLNSTNAILITGGISDNKKHGDQFELYSAMYALDKNNNKLFEY... | Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn... |
A0Q491 | MSKLKIDTKRRFSLLIALVLIISLSSCATTQTNVTAITTKTVFNQETTYHNLLKLKKWQANGVIGIIYDNQAESANYTYLQDGDNFSIKLYGPLGIGSIEIKGDTNSVSLANSKGQKLTAKDAKTLMLEQLGWYVPVEGLKYWIKAIAIPNIRQTSELNTNNLLSKLSQNGWSISYSNYQLVDSKYPLPTKIRMSRDNLTLKIVIKSWQI | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23598
Sequence Length: 210
Subcellular Location: Cell outer membrane
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Q7VL53 | MKKSTLLFSLMAMALSGCNSVLNAPIEVKKLVYQIEHTDPAWQQHLKQLAEIKNYEVKGQFGYISPTERFSAHFDWQYKTPIDFTLALSSNLSTKLLKLQRSHQGLTVSDSEGYSRTEADIHALMQEIIGVSFPIDQFAYWVKGQPAQEGNYIVNEKRQLSQFSYPINQQIWQARYVEYHENRVPYLPKLIVLENGQQTLKIRLDHWNY | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24328
Sequence Length: 209
Subcellular Location: Cell outer membrane
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P45270 | MNNMKTFKFFTALFATAILTACTLDMERPTNVQYIDKTDAIWQQHLQKIQKIQSYQAKGQIGYISPTERFSSRFEWQYQNPKSYTLKLYSLISKSTLWIQMHQSGMTISDNNGNQQSAANSKLLLQEIIGMDVPLEHLAYWLKGQPAMNADYQVGTNHLLGAFTYHVDGSQWTADYLTYHSNNSMPENILLKNDSTKQTLKIRVDEWIY | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24193
Sequence Length: 209
Subcellular Location: Cell outer membrane
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A1WVQ5 | MTGRWSPRLLAGLLAALVLSGCALLVPEDEREAQYEAFLEERAELRDWSVAGRAALRAEGEAVSLSLRWEQRGEVYTINLSGPFGAGAVRIEGQPGRVTLRDGAGQSATAQSPEELLAAQTGHQLPVTALRDWIVGRPADGLEVDELSLDRVGRPDRLEQAGWRVDFQGWTDVDGVDLPSRVDLTRGSTQMRVALSGWSRSDD | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22106
Sequence Length: 203
Subcellular Location: Cell outer membrane
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C4K7Y9 | MLIFKICFYRLLPLSVLLLAACSALKAPESSSVLKNHIASDEWQEYQHQLKQIQQFQIQGSVAYFSDEKKAYARFFWQQYSPKNYHLLLLSPLGQTEFELKVTNGRVDMAKYKDQGEIKGDAEEILFKLTGIPIPLEHLSRWIVGASSDADEIILNRQSRLKTLIHHKKEQTWKVYYQAYNTKITPILPERLELYLISPNHQDQRMTLKINHWILK | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25333
Sequence Length: 216
Subcellular Location: Cell outer membrane
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O66646 | MAEILRAENIKKVIRGYEILKGISLSVKKGEFVSIIGASGSGKSTLLYILGLLDAPTEGKVFLEGKEVDYTNEKELSLLRNRKLGFVFQFHYLIPELTALENVIVPMLKMGKPKKEAKERGEYLLSELGLGDKLSRKPYELSGGEQQRVAIARALANEPILLFADEPTGNLDSANTKRVMDIFLKINEGGTSIVMVTHERELAELTHRTLEMKDGKVVGEITRV | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q5NZT6 | MSEATNEPVLACEGLSKTFREGADALQVLDGVTLAVARGERIAIVGASGSGKSTLLHLLGGLDVPSAGAVRLHGRDFSRMSDAERGRVRNEALGFVYQFHHLLPEFSALENVAMPLYIRRMEREAANERAVAMLKEVGLGHRLDHAPGELSGGERQRAAIARALVTQPACVLADEPTGNLDRRTAQSVFDLMLSLNERLATSFIIVTHDEQLAGRAQRTLRLDDGRLA | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q5LI72 | MIHLEGITKSFGSLQVLKGIDLEITQGEVVSIVGPSGAGKTTLLQIMGTLDSPDAGMINIDGTNVSRMKEKELSAFRNKHIGFVFQFHQLLPEFTALENVMIPAFIAGVPTKEASMRAMEILDFMGLKERASHKPNELSGGEKQRVAVARALINQPAVILADEPSGSLDSHNKEELHQLFFDLRNRFGQTFVIVTHDEALAKITDRTIHMVDGNII | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q8A1M1 | MIKLEGITKSFGSLQVLKGIDLEINKGEIVSIVGPSGAGKTTLLQIMGTLDEPDAGTVAIDGTVVSRMKEKELSAFRNKNIGFVFQFHQLLPEFTALENVMIPAFIAGVSSKEANERAMEILAFMGLTDRASHKPNELSGGEKQRVAVARALINHPAVILADEPSGSLDTHNKEDLHQLFFDLRDRLGQTFVIVTHDEGLAKITDRTVHMVDGTIKKD | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q6MMY0 | MRAVDIHKSYSQGVGELEILRGVSLDIREGEAFAILGASGAGKSTLLQIMGTLDRPNKGELYCEGRDLLAMSDDELSRFRNSEMGFVFQFHHLLSEFNALENVMIPCRVGGESIKVAKEKALHLLEFMGLADRRDHHPNQLSGGELQRVAIARALVRHPKILFADEPTGNLDSHTSGKIQELFFRLKEEMKLALVIVTHDLTFATRFPKVYRMKDGQWQS | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q492R2 | MANIPLLQCIQLTKYYQRANFLIKVLNCITLSIQSNEMIAVVGASGSGKSTLLHLLGGLDKPTEGEIFFEGHALHKLTDNERSVIRNKRLGFVYQFHHLLSDFDVLENVAMPLLIGGIAFNQAKSRAQCVLELVGLKNHINSFPHELSGGESQRVTVARAIVNNPSLILADEPTGNLDQKNSDSIFQLLKKLNTYYGTTFLIATHDLDFAKKCHKILMISNGKIKLSQNDSFR | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
Q89KN0 | MEQQQGAEDVPVIYLHEIKRQYLQGEVPLTILDGAKLALWAGQSVALVAPSGSGKSTLLHIAGLLEAPDSGEVYVNGAPTSQLPDIERTQLRRTDIGFVYQSHRLLPEFSALENVMLPQMIRGLKKSESVKRAKEILGYLGLGDRITHRPAELSGGEQQRVAIARAVANAPRVLFADEPTGNLDPHTADHVFQALMQLVKATRVSMLIATHNMELAGRMDRRVSLSDGQVVELE | Function: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Location Topology: Peripheral membrane ... |
P57383 | MNNIIIKCINLNKSYKDGDFTYTILKNISFQLNKGDIAGIIGKSGSGKTTFLHLLAGLENPTSGDILFNGRLFSSMSSNKMSKFRNIELGFIYQFHHLMLDFNILENVSMPLLISNKSKKDSEEIAYNMLKKFNLEDKIKKYPSELSGGERQRVAVARAFINKPSLIIADEPTGNLDEDNTNIIFNLITELNSDYNTSFIIATHDPTLIKKIPVLFKIENNQIFNYES | Function: Usually LolD forms an ABC transporter complex with LolC and LolE involved in the translocation of lipoprotein, in an ATP-dependent manner. However, LolE is certainly not functional as it is frameshifted.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25829
Sequence Length: 228
Subcellular ... |
Q72JM6 | MLPETMPVCPVRGSVIYPTMVMPIDAGRPISIRAIDEALARDRVLLIVSQRDKEVETPRPSDLFEVGTACNILKMRKNPDGSVQVLVQAFARVRVREWLDLGDHLEARGEVLADEPGEPILVKALVREVKDKFQALLKEGKYLAPEVAQFILNLEDPSQLADYVAFHMDFRLEDKQKVLETANVAERLRAVLVLLEAELALIETQRRIQQQVKEEIDRNQREYFLREQMKAIQRELHGEEGEQEVEEFRRKLEALDLPPVVRQEVERELNRFARMHPDSAEASVIRTYLDWIVNLPWNTRTEDNLDLERAKEILERDHYG... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
A9GIS9 | MFFKNDSDRGKNAPERGIVPLLPLRDIIVFPHMVSQLFVGRERSIAALDEAMNRGKEIFLAAQRNAKTNDPTPDDIFGVGSVGAIMQLLRLPDGTVKVLIEGKRRARIRRYVQSDAYFLIEYDEIVESSVASVEVEALMRSVQSTFEMYVKLNKKIQPEVLMAVQAIDEASRLADTIIANLPTIKLTDRQALLEMEEPQKRLERLIELMQAEIEILQVEKKIRSRVKKQMEKTQKEYYLNEQMQAIQKELGGGERDEFKNEIQEIEEALKTKRMSKEAAAKVKKELKKLKMMHPTSAEATVVRNYIDWILELPWYDKSEE... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
A9F8L0 | MSQLRSGASAPRSPFPLLPLRTGVLFPGTVLTLPVGRPRSVALLNAVHAGDVIGVIAQRDPKREDPRREDLHDIGTFARVVDISRVSNGYRLVIEGLDRFALSALVETEPTWRAEGTLAPEFLGDAEEARLLAASLRERAREVGPKTGTNLAEIAATSRAEPGVFADQVAGALGLPTEKEMEVLSELRVVPRLQRVAGLLAEASALADLKKKIDGDVRRELGKGQREVILREQLRAIQKELAGGEEGEDELSALRRRLDEAGLPEEARAVADRELRRLESVGPQSAEHNVIRTYLEWIADLPWSARAEVKDDLDAVKAKL... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield ... |
Q9HSC3 | MSNESTNDAPPDDDPDDPEPSVDHDDTDGLQDDPADSVDDAGEVDDLENLGSDVGVEGDVSIDEDNAEDDLLGGLRIDDTSDITVPDRLVDQVIGQEAAREIVKRAAKQHRHVMMIGSPGTGKSLLAKAMSRLLPKESLQDVLVYHNPDDSNEPKVRTVPAGKGEQIVDAHKEEARKRNQMRSFLMWIMILLAVGYALLIATPARPLLALLSAAGIYLLFRYTNRGSDAMVPKLLINNADRQVAPFEDATGAHAGAMLGDVRHDPFQSGGMATPSHERVEAGSIQKANKGVLFIDEINTLDVRSQQKLMTAIQEGEFSIT... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76017
Sequence Length: 702
Subcellula... |
Q58812 | MFSIKFKTTEELPEPSPRLIDQVIGQEEAVKIVLSAVKNKRNVILLGDPGVGKSMIVKAVGEILSDFGEFTPYYVIAKPNLKNMERPIVEVIDGEYKEDSKDMPKLDFKAPSSTTLLLIMIGAILLSEYLLKYLPQNYLLAAVTITALIVLIFGFVIILTSIMGASRASMPNNLNPMDLKPVLLYECKKRPLVRASAYNVTRLLGDIKHCPLGGRPPLGTPPHKRIILGAIHEAHRGILYVDEIKTMPLEVQDYILTALQDKQLPISGRNPNSSGATVETNPIPCDFILIMSGNMDDVYNLRAPLLDRIDYKIVLKNKMD... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71918
Sequence Length: 649
Subcellula... |
O26878 | MKTTIKNSRTQESVSYEGNETKKGTGETLSYETSKDIEVPERLIDQIIGQEEAVETIKKAAEQRRNVLLIGEPGVGKSMLAKAMAELLPREQLQDILVYPNIEDPNNPLIGAVPAGEGRKIVMNHKNKARSQDEKKNLFMMLIISFILVLGFMMNQFLAAIIAAGIIFLALQQFRPRTTVMVPKLLVNNEGRQVAPFVDATGAHAGALLGDVRHDPYQSGGLGTPAHERVEAGMIHKANKGVLYIDEIGTMKMKTQQELLTAMQEKRYSITGQSETSSGAMVRSQAVPCDFVLVASGNLQVLEGMHPALRSRIRGYGYEV... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70212
Sequence Length: 644
Subcellula... |
Q9UYC6 | MLKFYKMGIKRLSGEMTMGEERMDLGIEFETTEEIPVPERLIDQVIGQDHAVEVIKTAAKQRRHVLLIGEPGTGKSMLGQAMAELLPTEDLEDILVFPNPEDENMPRIKTVPAGQGRRIVEEYKRKAKEQENIRFYLLFFVFFIVAMAVFMSRGDPNTLLLGVFVILIALMVTANMRFRTQAMVPKLLVDNSGRKRAPFVDATGAHAGALLGDVRHDPFQCFSGEETVVIRENGEVKVLRLKDFVEKALEKPSGEGLDGDVKVVYHDFRNENVEVLTKDGFTKLLYANKRIGKQKLRRVVNLEKDYWFALTPDHKVYTTD... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
PTM: This protein undergoes a protein self splicing that involves a post-translational excision of the i... |
Q9HJ89 | MEENIESVEEWVNKLDIETTKDIHVPKLLFDQVIGQDQAGEIVKKAALQRRHVILIGEPGTGKSMLAQSMVDFLPKSELEDILVFPNPEDPNKPKIKTVPAGKGKEIVRQYQIKAEREKRDRSRSIMFVIFSVVLLGIIAAIVLRSITLIFFAIMAAAFLYMAMAFNPVIRNERAMVPKLLVSHNPNDKPPFVDSTGAHSGALLGDVRHDPFQSGGLETPAHERVEAGNIHKAHKGVLFIDEINLLRPEDQQAILTALQEKKYPISGQSERSAGAMVQTEPVPCDFVLVAAGNYDAIRNMHPALRSRIRGYGYEVVVNDY... | Function: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71601
Sequence Length: 657
Subcellular Location: Cell... |
Q8NKS6 | MDEESTKERLIPREYGESLDLGIDFKTTEEIPVPEKLIDQVIGQEHAVEVIKTAANQRRHVLLIGEPGTGKSMLGQAMAELLPTENLEDILVFPNPEDENMPKIKTVPACQGRRIVENYRRKAKEQEGIKNYLLMFVIFTVILAIIMEPTATTLLMGMFVVLLSMMVLSNMRFRNTVLVPKLLVDNCGRKKAPFVDATGAHAGALLGDVRHDPFQSGGLGTPAHERVEPGMIHRAHKGVLFIDEIATLSLKMQQSLLTAMQEKKFPITGQSEMSSGAMVRTEPVPCDFILVAAGNLDTIDKMHPALRSRIRGYGYEVYMR... | Cofactor: Mg(2+). Exhibits no peptide cleavage activity without Mg(2+), regardless of the presence or the absence of ATP. Can also use other divalent cations such as Ni(2+), Ca(2+), Mn(2+) and Co(2+).
Function: Serine protease that displays ATP-independent proteolytic activity towards peptides and unfolded proteins and... |
Q9UN81 | MGKKQNRKTGNSKTQSASPPPKERSSSPATEQSWMENDFDELREEGFRRSNYSELREDIQTKGKEVENFEKNLEECITRITNTEKCLKELMELKTKARELREECRSLRSRCDQLEERVSAMEDEMNEMKREGKFREKRIKRNEQSLQEIWDYVKRPNLRLIGVPESDVENGTKLENTLQDIIQENFPNLARQANVQIQEIQRTPQRYSSRRATPRHIIVRFTKVEMKEKMLRAAREKGRVTLKGKPIRLTADLSAETLQARREWGPIFNILKEKNFQPRISYPAKLSFISEGEIKYFIDKQMLRDFVTTRPALKELLKEA... | Function: Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.
PTM: Polyubiquitinated, probably by UBR2, which induces ... |
P11260 | MAKGKRKNPTNRNQDHSPSSERSTPTPPSPGHPNTTENLDPDLKTFLMMMIEDIKKDFHKSLKDLQESTAKELQALKEKQENTAKQVMEMNKTILELKGEVDTIKKTQSEATLEIETLGKRSGTIDASISNRIQEMEERISGAEDSIENIDTTVKENTKCKRILTQNIQVIQDTMRRPNLRIIGIDENEDFQLKGPANIFNKIIEENFPNIKKEMPMIIQEAYRTPNRLDQKRNSSRHIIIRTTNALNKDRILKAVREKGQVTYKGRPIRITPDFSPETMKARRAWTDVIQTLREHKCQPRLLYPAKLSITIDGETKVFH... | Function: Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.
PTM: Polyubiquitinated, probably by UBR2, which induces ... |
P23490 | MSYQKKQPTPQPPVDCVKTSGGGGGGGGSGGGGCGFFGGGGSGGGSSGSGCGYSGGGGYSGGGCGGGSSGGGGGGGIGGCGGGSGGSVKYSGGGGSSGGGSGCFSSGGGGSGCFSSGGGGSSGGGSGCFSSGGGGSSGGGSGCFSSGGGGFSGQAVQCQSYGGVSSGGSSGGGSGCFSSGGGGGSVCGYSGGGSGCGGGSSGGSGSGYVSSQQVTQTSCAPQPSYGGGSSGGGGSGGSGCFSSGGGGGSSGCGGGSSGIGSGCIISGGGSVCGGGSSGGGGGGSSVGGSGSGKGVPICHQTQQKQAPTWPSK | Function: Major keratinocyte cell envelope protein.
PTM: Substrate of transglutaminases. Some glutamines and lysines are cross-linked to other loricrin molecules and to SPRRs proteins.
Sequence Mass (Da): 25761
Sequence Length: 312
Subcellular Location: Cytoplasm
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A0A142ZC57 | MKYTDFLAHPDEIIPTIRMMYADYRLKNMEIKDPSVRFCYNMLNRVSRSFAMVIQQLPVELRDATCVFYLILRALDTVEDDMAIPKEVKIPMLRTFHEHLSDRSWKIKCGYGPYVDLMDNYPLVTDVYLRFDEGTKAVIKDITRRMGNGMADFIDLDEVLTIPQYDLYCHYVAGLCGIGMCKLFVDSGLEKEDLVAEEDLANQMGLFLQKNNIVRDYLEDINELPAPRMFWPKEIWGNYAKQLDEFKDPKNLDKAMLCLNHMVTDALRHCEVGLRSLSLLHNPNILRAVLIPQVMGVRTLTLVYNNPEVFRGVVKMRRGE... | Function: Converts the C20 geranylgeranyl diphosphate (GGPP) to the C40 lycopaoctaene, the first committed intermediate in the production of lycopadiene . Converts farnesyl diphosphate (FPP) into squalene, a precursor for sterol biosynthesis in eukaryotes . Converts with low efficiency the C20 phytyl diphosphate (PPP) ... |
Q3ZC80 | MQANSSAKSLPTECPDYQPIHHLHLVVYSVVLAAGLPLNALALWVFLRALRVHSVVSVYMCNLAASDLLFTLSLPLRLSYYARHYWPFPDFLCQLAGAVFQMNMYGSCIFLTLINVDRYAAIVHPLRLRHLRRPRVARLLCLGVWALILVFAVPTILAHQPSSCARDGRNVSLCFESFSDKLWKGSLLPLLLLAEALGFLLPLAAVVYSSGRVFWTLARPDATRSQRRRKTVRLLLASLVIFLLCFVPYNATLAVYGLLRGEVVPASSEARKKVRGVLMVMVLLAGANCVLDPLVYYFSAEGFRNTLRGLRAPLRDRTLA... | Function: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40639
Sequence Length: 367
Subcellular Location: Cell membrane
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Q9H1C0 | MLANSSSTNSSVLPCPDYRPTHRLHLVVYSLVLAAGLPLNALALWVFLRALRVHSVVSVYMCNLAASDLLFTLSLPVRLSYYALHHWPFPDLLCQTTGAIFQMNMYGSCIFLMLINVDRYAAIVHPLRLRHLRRPRVARLLCLGVWALILVFAVPAARVHRPSRCRYRDLEVRLCFESFSDELWKGRLLPLVLLAEALGFLLPLAAVVYSSGRVFWTLARPDATQSQRRRKTVRLLLANLVIFLLCFVPYNSTLAVYGLLRSKLVAASVPARDRVRGVLMVMVLLAGANCVLDPLVYYFSAEGFRNTLRGLGTPHRARTS... | Function: Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41347
Sequence Length: 372
Subcellular Location: Cell membrane
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P32250 | MVSSNCSTEDSFKYTLYGCVFSMVFVLGLIANCVAIYIFTFTLKVRNETTTYMLNLAISDLLFVFTLPFRIYYFVVRNWPFGDVLCKISVTLFYTNMYGSILFLTCISVDRFLAIVHPFRSKTLRTKRNARIVCVAVWITVLAGSTPASFFQSTNRQNNTEQRTCFENFPESTWKTYLSRIVIFIEIVGFFIPLILNVTCSTMVLRTLNKPLTLSRNKLSKKKVLKMIFVHLVIFCFCFVPYNITLILYSLMRTQTWINCSVVTAVRTMYPVTLCIAVSNCCFDPIVYYFTSDTNSELDKKQQVHQNT | Function: Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35597
Sequence Length: 308
Subcellular Location: Cell membrane
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P43657 | MVSVNSSHCFYNDSFKYTLYGCMFSMVFVLGLISNCVAIYIFICVLKVRNETTTYMINLAMSDLLFVFTLPFRIFYFTTRNWPFGDLLCKISVMLFYTNMYGSILFLTCISVDRFLAIVYPFKSKTLRTKRNAKIVCTGVWLTVIGGSAPAVFVQSTHSQGNNASEACFENFPEATWKTYLSRIVIFIEIVGFFIPLILNVTCSSMVLKTLTKPVTLSRSKINKTKVLKMIFVHLIIFCFCFVPYNINLILYSLVRTQTFVNCSVVAAVRTMYPITLCIAVSNCCFDPIVYYFTSDTIQNSIKMKNWSVRRSDFRFSEVH... | Function: Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation. Important for the maintenance of hair growth and texture.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39392
Sequence Length: 344
Subcellular Location: Cell membrane
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Q8GXU8 | MDVASARSISSHPSYYGKPICSSQSSLIRISRDKVCCFGRISNGMTSFTTSLHAVPSEKFMGETRRTGIQWSNRSLRHDPYRFLDKKSPRSSQLARDITVRADLSGAATPDSSFPEPEIKLSSRLRGIFFCVVAGISATFLIVLMIIGHPFVLLFDPYRRKFHHFIAKLWASISIYPFYKINIEGLENLPSSDTPAVYVSNHQSFLDIYTLLSLGKSFKFISKTGIFVIPIIGWAMSMMGVVPLKRMDPRSQVDCLKRCMELLKKGASVFFFPEGTRSKDGRLGSFKKGAFTVAAKTGVAVVPITLMGTGKIMPTGSEGI... | Function: Plastidial enzyme of the prokaryotic glycerol-3-phosphate pathway that converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at position sn-2 . Utilizes palmitoyl-ACP (16:0-ACP) to produce phosphatidic acid containing a saturated group at position sn-2, which is character... |
Q8LG50 | MVIAAAVIVPLGLLFFISGLAVNLFQAVCYVLIRPLSKNTYRKINRVVAETLWLELVWIVDWWAGVKIQVFADNETFNRMGKEHALVVCNHRSDIDWLVGWILAQRSGCLGSALAVMKKSSKFLPVIGWSMWFSEYLFLERNWAKDESTLKSGLQRLSDFPRPFWLALFVEGTRFTEAKLKAAQEYAASSELPIPRNVLIPRTKGFVSAVSNMRSFVPAIYDMTVTIPKTSPPPTMLRLFKGQPSVVHVHIKCHSMKDLPESDDAIAQWCRDQFVAKDALLDKHIAADTFPGQQEQNIGRPIKSLAVVLSWACVLTLGAI... | Function: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. Has preference for C-18-CoA substrates compared to C-16-CoA substrates. Required for female but not male gametophyte development.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,... |
Q9SYC8 | MKIPAALVFIPVGVLFLISGLIVNIIQLVFFIIVRPFSRSLYRRINKNVAELLWLQLIWLFDWWACIKINLYVDAETLELIGKEHALVLSNHRSDIDWLIGWVMAQRVGCLGSSLAIMKKEAKYLPIIGWSMWFSDYIFLERSWAKDENTLKAGFKRLEDFPMTFWLALFVEGTRFTQEKLEAAQEYASIRSLPSPRNVLIPRTKGFVSAVSEIRSFVPAIYDCTLTVHNNQPTPTLLRMFSGQSSEINLQMRRHKMSELPETDDGIAQWCQDLFITKDAQLEKYFTKDVFSDLEVHQINRPIKPLIVVIIWLGFLVFGG... | Function: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. Has preference for C-18-CoA substrates compared to C-16-CoA substrates.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: M... |
Q8L4Y2 | MEVCGDLKSDNLKNRPLTPLRILRGLMILLVFLSTAFMFLLYFAPIAALGLRLLSVQQSRKVVSLIFGLWLALWPYLFETVNGTTVVFSGDIIPVEKRVLLIANHRTEVDWMYLWNIALRKGCLGYIKYVLKSSLMKLPIFGWGFHVLEFIPVERKREVDEPVLLQMLSSFKDPQEPLWLALFPEGTDFTEEKCKRSQKFAAEVGLPALSNVLLPKTRGFGVCLEVLHNSLDAVYDLTIAYKPRCPSFMDNVFGTDPSEVHIHVRRVLLKEIPANEAESSAWLMDSFKLKDKLLSDFNAQGKFPNQRPEEELSVLKCIAT... | Function: May convert lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position (By similarity). Has no activity when expressed in bacteria or yeast.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: M... |
A8J0J0 | MARKSSLAQAAIERKPVLLRPQLNVPRMSGITALPMERRPLPVAPSPSAKPELPARSALVCHAAAASVPLPNSDSAPQPNVLLAKIRAIMFFAWSFLLSLPLFVTMMVMAPLVLAFDKYRRLAQHFVNNLWACASTAPFYKVTIIGRENLPPPDKPVVYVANHQSFLDIYSLFHLQRPFKFISKTSNFLIPIIGWSMFLTGHVMINRVDRRSQLKCLQQCRDLLAEGAPVLFFPEGTRSLDCKMAGFKKGAFSVAAKAGVEVVPITLLGTGSLMPSGKESQLRPGQVTIVVHKALPPNKNADQLCDAARQAVASSLPPEL... | Function: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass ... |
Q41745 | MAIPLVLVVLPLGLLFLLSGLIVNAIQAVLFVTIRPFSKSFYRRINRFLAELLWLQLVWVVDWWAGVKVQLHADEETYRSMGKEHALIISNHRSDIDWLIGWILAQRSGCLGSTLAVMKKSSKFLPVIGWSMWFAEYLFLERSWAKDEKTLKWGLQRLKDFPRPFWLALFVEGTRFTPAKLLAAQEYAASQGLPAPRNVLIPRTKGFVSAVSIMRDFVPAIYDTTVIVPKDSPQPTMLRILKGQSSVIHVRMKRHAMSEMPKSDEDVSKWCKDIFVAKDALLDKHLATGTFDEEIRPIGRPVKSLLVTLFWSCLLLFGAI... | Function: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position.
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42571
Sequence Length: 37... |
Q8FA49 | MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTAEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAIREAFFAHYGERVEAEIISPDKTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDERFSWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFP... | Function: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] +... |
P47512 | MQTFIITSPVFNPYFNAALEEWLLTEFRKNELVKVIYFWQNANTIVVGRNQNTYAEVNLKELESDKVNLFRRFSGGGAVFHDLGNICFSIILPRTGKVMENAYEQTTRNVVKFLNSLNVPAVFHGRNDLEINNKKFSGLAEYIAKDRLLVHGTLLFDTDFSKLAKYLNVDKTKIASKGVDSVAKRVVNVKEYLPNWTTAKFLEEMINFFTVTEKAETIVLTKDALAKVEKRAKEHFQSWEWNFGKTYEYNFKNKRYFNNAGLFECNVQVEKGTVVDIKFYGDFLSVVDITPVTKKLIGQKYDYKTFEKLFNELDHFSDYF... | Function: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] +... |
C6DKP5 | MSSLRLLISDSYDPWFNLAVEECIFRQMPTTQRVLFLWRNAETVVIGRAQNPWKECNTRRMEEDGIKLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKSVSTQIVLDALSALGLKASASGRNDLVVETADGVRKVSGSAYRETKDRGFHHGTLLLNADLNRLADYLNPDIKKLQAKGITSVRSRVANLVELLPSVDHQVICQAVTQAFFDYFGEQCEPEIISPSAYPDLPGFSEQFARQSSWEWNFGQAPDFSHLLDNRFTWGGIELHFDVERGVIIRAQVYTDSLNPAPLEALACALQGTAYRPENMAATCQALITAFP... | Function: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] +... |
Q1QEC2 | MKLRILKSAVTNPWFNLATEDWIFNTLNPDSHTLFLWRNSETVVIGRSQNPWVECKIDKMEADDVFLARRQSGGGAVFHDLGNTNFTFLSPKDDYDQAANFTIIINALKKLGIDADLSGRNDMQVGDKKISGSAFKHTADRSFHHGTLLVNANMQKLGDYLNPHPLKLKAKGIKSVRARVANLVEFNEDINHETLSDAIIEAFREYYRDTDYGDTAPVEELDEASLAKQPNLNKYYQQMADWDWRFGKTPEFTHHIETRFNWGIIDLHLDVKQAAIREVVIFSDALNVELIDLLKESLADVKYDKHDIKAKFDELNRAHP... | Function: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] +... |
Q65T15 | MTILLQRAKFKKRLMPILFPLMLAGCTNLFGSNFQDVLRNDANASSEFYMNKIEQTREVEDQQTYKLLAARVLVTENKTAQAEALLAELTKLTPEQQLDKSILDALIAAVKRDNDSASALLKTIPLAQLSQSQTSRYYEVQARIAENKTDIIEAVKARIQMDMALTDVQRKQDNIDKIWALLRSGNKTLINTTQPEGNVALAGWLDLTKAYNDNLSQPSQLAQALQNWKTTYPNHSAAYLFPTELKSLSNFTQTQVNKIALLLPLSGNASILGSTIKSGFDDSRGADKSVQVDVIDTMAMPVTDAIALAKQNGDGMIVGP... | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a).
Location Topology: Lipid-anchor
Sequence Mass (Da): 63113
Sequence Length: 574
Subcellular Location: Cell outer membrane
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Q6LME4 | MNSMLNFTHKRKSVSRLLAPVALAVILAGCSSSNQQQASASNITAIATDTSANYLIKAESSDGIESIDWNILALKALIKEGQWTQADNQSKRLSRMSLSPIQMAEWQLARATLRYQQGQLQEALNTLNFQPWWPLPDNQYKRYFMLRAELLGQLGQHSKAARQRTMLDQYLPSNQKNANWQNLWQDLSSYNNSQLQSVSLKEDETVLRGWIQLSILKNTYSQRPVRLKSAVDEWLSMNPYHPAHQYLPTELEAIMSMEVAQLDNVALLLPLTGRFESQGKAVRDGFINAMLDDTSRDTDTELTVFDTEAESMTAIMAKLQ... | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a).
Location Topology: Lipid-anchor
Sequence Mass (Da): 69215
Sequence Length: 613
Subcellular Location: Cell outer membrane
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Q2NWH5 | MLYSYVLVFKTGRLLPVVLASLILAACTAQGPESQTGHAAIPANANADYYLQQMQQSSNDTKTDYQLLAIRALIKEGRLPQAQQQLAALQQIDSASLDAPQRLRYTQAMINAGQSRPSLDLVRAYIAQAPLLTDPAARQQNIDKTWQTLVSLPSPQSNLVINADENILQGWLDLLRIYQDNRQDPTLLQAAIKDWQTRYPQNPAAKTLPTPLSQVQNYSSSSVGGIALLLPLNGQAQVFSNAIQQGFSAAKNGLTTQQSALEQDASAAGQSTDGVPQNDGTAGTEPAGGSANQNGPVTTPGTRPDPAASGVDGQASAADN... | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a).
Location Topology: Lipid-anchor
Sequence Mass (Da): 70665
Sequence Length: 670
Subcellular Location: Cell outer membrane
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A5F987 | MAMNHHQRRSVPRLLTPIALSIVLSACSTQPSSPDVVDITAQPLLTAQTYLMRADASQGNQQNDWLIMALKAAIEENNPDQAQLLIMRLAKQPLTPTQQAQWQLLRAQLLANTEQYQEALEQLSFQANWSLPQVQWQQYHQLRADIFTALDRSFDSTRELVALYGLSSNKDKEALADQIWANLNHYSASKIIKLSTEPDEAQLDGWLQLAIYMKTLGSDLPQLKNTLEKWLAENPQHPAAIYTPKAITDILALEIVKPTNTALLLPLTGKFAKQAQFIRDGFVFAMMNDADRQTNATLTIIDTNAETLESVDAILTSKQI... | Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a).
Location Topology: Lipid-anchor
Sequence Mass (Da): 67670
Sequence Length: 603
Subcellular Location: Cell outer membrane
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G7CES0 | MDGRQVVRARRWCATAAVALMTASTVAACGSDSGEIVISYYTPANEAATFTAVAQRCNAELGGRFRIEQRSLPREADAQRLQLARRLTGNDRSLDVMALDVVWTAEFAEAGWALPLSEDPAGLAEADATTNTLPGPLETAKWNGELYAAPITTNTQLLWYRADLMDEPPATWDEMLSEAARLHAQGGPSWIAVQGKQYEGLVVWFNTLLESAGGQVLSDDGQRVTLTDTPEHRAATVKALEIIKAVATAPGADPSITQTDENTARLALEQGRAALEVNWPYVLPSLLENAIKGGVGFLPLNENPALRGSINDVGTFAPTD... | Function: Part of the ABC transporter complex LpqY-SugA-SugB-SugC, which is highly specific for uptake of trehalose. Involved in the recycling of extracellular trehalose released from trehalose-containing molecules synthesized by M.thermoresistibile. Trehalose uptake is essential for virulence (By similarity). Binds de... |
F4I4K5 | MESLLCRRRIKRVMVLIIALTWLRSTCGELEDQLFEVGKLKMFVDDLPDMPRLYGFNSVHGIIKPASLQIGMFSTKWKFHRDLPATPVFAYGTSRSKATVPGPTIETVYGVDTYVTWRNHLPKSHILPWDPTISPATPKHGGIPTVVHLHGGIHEPTSDGNADAWFTAGFRETGPKWTKTTLHYENKQQPGNMWYHDHAMGLTRVNLLAGLVGAYILRHHAVESPFQLPTGDEFDRPLIIFDRSFRKDGSIYMNATGNNPSIHPQWQPEYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSNGLDFIVVGS... | Cofactor: Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
Function: Multicopper oxidase that may be involved in copper homeostasis and oxidative stress response, and that is necessary for root growth inhibition... |
Q949X9 | MEPSRRRMTRDMLLLIVTMAWLVTGDEGGIKQEERLFNLGKLEMFVDKLPHIPTLHGYHFVNGFLKPKSLHIGMFFKKWKFHRDLPATPVFAYGTSKRSATVPGPTIEAVYGVDTYVTWRNHLPLHHILPWDPTISPAIPKHGGIPTVVHLHGGIHEPTSDGNADSWFTAGFKETGSKWTKKTTHYVNKQQPGNMWYHDHAAGLTRVNLLAGLLGSYILRHSSVESPLRLPTGREFDRPLVIFDRSFRKDGSIYMNATGNNPTIHPQWQPEYFGDAIIVNGKAWPRLTVRRRKYRFRITNASNARFFRFFFSNGLDFIVV... | Cofactor: Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
Function: Multicopper oxidase that may be involved in copper homeostasis and oxidative stress response, and that is necessary for root growth inhibition... |
Q5ZE07 | MEKRRFLGVCLLVAVLVLRAAVLGRGDDGGGGGRLLDPGKLEMFVDELPDMPRMRGYGVAEGGKLVAGNLTIGMYETMWKFHRDLPATRVFAYGTSKETATVPGPTIEAMQGVPTYVTWTNHLPPRHFLPWDPTLTAAAPGSGVPAVVHLHGGVQHSGSDGHSLAWFTAGFAATGPRFSSPAAYEYPNQQPPGNLWYHDHAMGLTRVNILAGLLGAYRVASPAEEAALNLPSGEAFDRNLVLFDRDFLADGSLFMNRTGNNPSVHPQWQPEYFGAVVVANGKAWPYLRVRRRRYRLRILNASNARFFRLSLSGGLRFVHV... | Cofactor: Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
Function: Multicopper oxidase that may play a role in the maintenance of inorganic phosphate homeostasis.
Location Topology: Peripheral membrane protein... |
A2ZNT5 | MSPRIQQLAAVLLAAVVVVAAARDEPAAAKNYQTQWDTVMSILNCKSDSLIPSYICSVISKSRWGWASDDPNDDEYTPPDHPLPAPAAGRRRWPVMTSLNLTKYVDSLPRIAKIRGYGIRHGRPVPIKLTIGMYSKTWQFHRDMPPTPVFVYGQSLQTATFPGPTIVARQGVPLAVEWQNHLPDAHILPWDPKVPTAIPKKGGVPTVVHLHGGAHPPEFDGHAFAWFTRDFAENGSTWTRKTYTYPNVQAPGNLWYHDHALGLTRVSLLAGLLAAYVIEKPELEDPMNLPCGDHDLHLVIADREFYTNGSISIDREWKPE... | Cofactor: Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
Function: Multicopper oxidase that may play a role in the maintenance of inorganic phosphate homeostasis.
Location Topology: Peripheral membrane protein... |
P0AFA0 | MIIIRYLVRETLKSQLAILFILLLIFFCQKLVRILGAAVDGDIPANLVLSLLGLGVPEMAQLILPLSLFLGLLMTLGKLYTESEITVMHACGLSKAVLVKAAMILAVFTAIVAAVNVMWAGPWSSRHQDEVLAEAKANPGMAALAQGQFQQATNGSSVLFIESVDGSDFKDVFLAQIRPKGNARPSVVVADSGHLTQLRDGSQVVTLNQGTRFEGTALLRDFRITDFQDYQAIIGHQAVALDPNDTDQMDMRTLWNTDTDRARAELNWRITLVFTVFMMALMVVPLSVVNPRQGRVLSMLPAMLLYLLFFLIQTSLKSNG... | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40358
Sequence Length: 366
Subcellular Location: Cell inner membrane
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P45333 | MILIRYLIKEVFKSQIAILLILLLIFFSQQFVRVLGAAANGNVPADLVFSLLGLGMPTMAQLMLPLCLFIAILLTFGRLYAESEITVMRACGVGQRILVKVALIMSLLTAGIAAYNALWLSPWAIQKQVNMVEDAKANPTVGVLSSGQFISTNNNNVVLFIDKIKDNQIRNVYLFQMTPQKQTKPSVITAEKGELIALPNGDQVLNLKNTKRVEGTSALPDFRITHFDEYHAYLGYQSAENTNDEVAELTLSQLIDLDSSSAKAELHWRITLILAVPLMALIAVPLSRVNPRQGRFAKILPALLLYLIYFLLQSSFKSAG... | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41337
Sequence Length: 372
Subcellular Location: Cell inner membrane
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P0ADC7 | MQPFGVLDRYIGKTIFTTIMMTLFMLVSLSGIIKFVDQLKKAGQGSYDALGAGMYTLLSVPKDVQIFFPMAALLGALLGLGMLAQRSELVVMQASGFTRMQVALSVMKTAIPLVLLTMAIGEWVAPQGEQMARNYRAQAMYGGSLLSTQQGLWAKDGNNFVYIERVKGDEELGGISIYAFNENRRLQSVRYAATAKFDPEHKVWRLSQVDESDLTNPKQITGSQTVSGTWKTNLTPDKLGVVALDPDALSISGLHNYVKYLKSSGQDAGRYQLNMWSKIFQPLSVAVMMLMALSFIFGPLRSVPMGVRVVTGISFGFVFY... | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39619
Sequence Length: 360
Subcellular Location: Cell inner membrane
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Q886N1 | MSLIDPRAIIDPTAILADSVEVGPWSIIGPGVEIGEGTVVGPHVVLRGPTKIGKHNRIYQFSSVGEDTPDLKYKGEETRLVIGDHNVIREGVTIHRGTVQDRAETTLGDHNLIMAYAHIGHDSVIGNHVILVNNTALAGHVHVDDWAILSGFTLVHQFCHIGAHSFSGMGTAIGKDVPAFVTVFGNPAEARSMNFEGMRRRGFSEEAIHALRRAYKTVYRQGLTIAQALSDLAEPAAQFPEVAVFLQSIQTSTRGIIR | Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-[ACP]
Sequence Mass (... |
Q4ZWR6 | MSLIDPRAIIDPTAVLADNVEVGPWSIIGPGVEIGEGTVVGPHVVLKGPTRIGKHNRIYQFSSVGEDTPDLKYKGEETRLVIGDHNVIREGVTIHRGTVQDRAETTLGDHNLIMAYAHIGHDSVIGNHVILVNNTALAGHVHVDDWAILSGFTLVHQFCHIGAHSFSGMGTAIGKDVPAFVTVFGNPAEARSMNFEGMRRRGFSEEAIHALRRAYKTVYRQGLTIGQALADLAEPAAQFPEVAVFLQSIQTSTRGIIR | Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-[ACP]
Sequence Mass (... |
Q4FRI4 | MSQIHPTALISPSATIDETATIGPYCIVGDEVTIGAHTVLHRHVVVTRLTRIGEHNQFYQFSSIGEDPQDLKYAGERTWLEIGDHNTIREACSLHRGTEQDGGLTKIGSHNLLMVNTHVAHDCLIGDHNVLANNVGVAGHVTIGNHIIVGGNSGIHQFCTIDDYSLVGGATLVLKDVAAFTMVSGNPAKAHGLNVEGMRRKGWSKDSIDVLRQAYRVVFRSGLTTVQALEVLKQDLLPKEQKIEFLIDSLQKSRRGVVR | Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-[ACP]
Sequence Mass (... |
A1SYV1 | MTKKIAMIHPTAIVHENAIIGKDVEIGPYTIIGDRVEIGDNCWIAPHVVIKGPTKMGKGNKIYQFASIGEDCQDLKYNGEETFLEIGDNNVFRESCTVHRGTAQDQGTTRIGNNNLLMAYVHVAHDCVLGNNIILSNNATLAGHTKLANNVIIGGLSALHQFTRVGEFAMIGGCSAVNKDIPPYFMATGNYVEAQGVNSVGLKRSGFNSKAIMEIKRAYKILCREGNSLEQAKIKIAEKLEGCPELQVLYDFICEESRGIVR | Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-[ACP]
Sequence Mass (... |
Q6ALW0 | MDKQKRETGSEIMVVTGEASGDIHGANLVRALKEKDSSLSFSGMGGPELASLGVEILYDAKKISVVGLVEVFSHLPSIFAAKKILQRRLKNKPPALLIIIDLPDFNLMLAKKAKALGIPVFYYITPQVWAWRSGRIKTIGERTDQLGVILPFEEEFFRQRGQAASYVGHPLLDNVSIKLSREEFLTKHRIGPAAKYVGLLPGSREKEISALLPDFLRAAKRLQDECSEKISFLLPIAATIDREQLLENGLAEYQDLLDIHVISEDRYELMACCDAVVAASGTVTLELAILEVPMLVVYRTSPISYWVGRKLVKIEFFSLV... | 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.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D... |
F4IAT8 | MRLPVTVKATKPSFLVIWIRYSSAASSPTVSLNPSGRLQQTLAGSVEVKGKSLHSGKFSTVKLNPEIAGAGRFFEFRSRFIPASIEFAQESPLCTTLLKDELKIRTVEHLLSALEAKGVDNCRIQIESESSDDREVEVPIFDGSAKEWVDAIQGVGINAAQNHDGESVEKMVAHVNKPVYVCKNDTFVAAFPALETRITCGIDFPQVPAIGCQWFSWRPIHESSFAKDIASSRTFCVYEEVERMREAGLIKGGSLDNAIVCSAEHGWMNPPLRFDDEACRHKILDLIGDLSLVSRGGNGGLPVAHIVAYKAGHALHTDLA... | Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal t... |
B7J3W7 | MIRQRTLKNMIWGTGIGLHSGKKVYIGLRPAPVNTGIVFHRSDIEGGAWIKADPLHVVDTRLSTNIGDGHIRVGTVEHLMSALAGLGIDNAYVDLDGPEVPIMDGSAAPFVFLIQCAGIEEQNAPKRFIRITKPLKAEDGDRWVQLEPFEGFKVSFAIDFDHPVMKNGGQEVTVDFARTSYLKEVARARTFGFMREVEALRRMGLALGGNLDNAIVVDDYRVLNEEGLRYTNEFVRHKVLDSIGDLYLLGHPLVGHFSGHKAGHALNNSLLRALLLRQDAWEFVDYAERRAPFSFADTLVTASA | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
S... |
Q029X9 | MRFETTVQRPVEASGVGLHSGVPVKIRILPAPVSTGVVFVRTDLDGFQIPASWRHVARVSYATSLMRQGVLISTTEHLLSVFYSMGIDNVYVEIDNLEVPILDGSGLPFVKLIAQAGIRQYRRKRRYLRIRRPISVEDKGKRISILPDEAFRLTCDTEYPAPVGRQSLELVVTPEHYASELAFARTFGWENDLDQMRNMGLIRGASLANAVCFTSEGPLNPDGLRAVDECCRHKALDLIGDLALLGRPLLGHVIAERAGHAMHAALVARIMGDPSIYEIITFDQLASRVTQALVS | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
S... |
Q30ST0 | MYQTTIKKSVELVGIGLHKGSAVKLRLEPLESNSGLIFYRSDVDVAIPLLPANVVDTKMATVIGKDGYVISTIEHMLSAIYAYGIDNLKIIVNADEVPVMDGSSASFCMLLDEAGVVQLDVPKKIMRIKKEIIVQEGEKYVKLSPSTDLKYGFTIKFPHPVIQQQEYVLNFTKQNYKDEIARARTFGFLHEVQYLRSKGLALGGSLENAIVLDDKKVLNPEGLRFDDEFVRHKILDAIGDMALIGMNFVGNYEALAGSHDLNHKLTLELLKDAENYEVIELVDEKTKELEKAYA | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
S... |
Q2LVE4 | MYFQRTLKSDLSCQSVGLHSGRKVNMRIRPASSDEGIILVRTDTRYRQMIRVCLENVTDTTLATTIGSSGAAISTVEHILSALSGMGVDNAIIEVDAPEIPIMDGSALPFVNMLKLVGIRTQEKLKKYLVVKKPVSVSEGESFAMLAPSSSFEITYKIEFDHPLIKEQSYHLKLSDETYEKEICSSRTFGFLKDVEYLQAKGLALGGSLKNAVILDEKRIINKEGLRSHNEFVKHKILDAIGDLSLIGMPIVGHFIAYKSGHKLNSMLVKALLEQQENWTTASFLNCQDAHGQNTREKFSIRDIPARKILGAIHA | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
S... |
Q3A225 | MIYQSTLNKPLTISGIGLHTGRQITMILRPAEPDNGIIFHCTDGERRVSIPAVSANVVDTRLATVIGKDGLSVSTIEHLMAALSACGIDNLHIDIDGPEVPVMDGSAAPFVALLQETGNRVQEKRRKYLAIRKPITLVDGEKRVSIIPSRFFRITFDIAFDHPCIGLQHRAIKVNTETFRKEIAPARTFGFLHEVEYLKANGLALGGSLDNAVVIGEEGVLNPDGVRFEDECVRHKILDAVGDFSLLGHRVLGHVKAYKAGHDINHQMVEKILANADCWQLVESGEAASHGSLSMTGCAAMAMAGVAEA | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
S... |
P72988 | MGHTIKAPLTVQGVGLHSGVETTVTLCPVAAGKGRYFQRVDLPKKPIIPADLTWVREAMLSTELGEPGATIRTVEHLLATLVALDIGDLRIEVNGPEVPLLDGSALSWLTAIAKVGTRPRSKKSQDQPIVITDPLTCQLEDAFVAAFPCATTRFSYGVDYPYLPIGKQWYTWEPDQENFATAIAPARTFGFADQIEKLRQAGLIKGGSLENALVCDKEKWLNPPLRFPDEPVRHKLLDLLGDLSLLGKIPQAHFVAYKASHKLHTQLAQKIADTYR | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
S... |
B5YKK1 | MPFQKTIKSEISLTGIGIHTGKKINLNLIPAQRDTGIVFYRKDRNFPIKAKLPFVVDTSFATTLGVDGIKIRTVEHLLATLHVFGITNVFIEIDSSEIPVMDGSAIDFTKAILKAGIAKQGKTVSLFKITKPVYYEESHSKIFAKPYRGFKITYKIFYEHPLIMEQSLSIEINEQNFLNDIAPARTFGFLKDINYLLKNGFAKGGSLDNALVLDEKGVVGGNLRFKDEFVRHKILDAIGDLSLIGYPIQGHFIIEKGGHTSHINFLRKLIETGCYELAEEPYFNFQLSAQAV | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
S... |
A5CWY8 | MIKQRTIKKEVKARGIGIHSGSVVNMTLIPAKEDHGVVFRRMDVGDKLVRAHSAFVNEVVLSTGLENKGVKVSTVEHLMSAFSALGIDNVLVELDSFEVPIMDGSSAPFIFLVQSAGIEEQSTHKKFFVIKDTIRVENGDSWAQVSKYEGFKVSLEIDFDHKKVKESGEKLSINFSKQSYLKEISRARTFGYMKDVEMMQRQNLALGASMDNAIALSDDDVLNEDGMRYQNEFVKHKILDIVGDLYLLGSNLIGHYEGYKTGHLLNDQLLSTILAKPDTWSIETFEEDNSPIQFYSEDWQNSL | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
S... |
A0M2A1 | MKFTATQIAEILDGKVEGNPEAEVSELAKIEEGSEGSLTFLSNPKYTSFLYTTNASVTIVNDDFEVEQPVNTTLIKVKDAYKAFSTLLEYYNQIKLNKSGIEQPSHISESAKYGEGLYLGAFAYIGENVSIGENVKIYPNVYIGDNVKIGNNVTLFPGVKVYSESLIGSEVTIHSGVVIGADGFGFSPGDTGEYSKVPQIGNVIIEDYVDIGAGTTIDRATLGSTIIRKGAKLDNHIQIAHNVEIGENTAIAAQTGIAGSTKIGKNCLIGGQVGIAGHLTIGNRVKIQAQSGIGRDIKDDEMLQGSPAIGYSDYNKSYIH... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q1R023 | MKTLTPCAFTLGELAERLKARLVGDSDRRVTGLATLLDAGPNDITFLANKTYLKYLPDTRAAAVLVHPAHGTDAPCARLELENPYLGYAELSRLFDPLAGQAPEGVHPSAVVAESARIGEHVSVGPQCVIEAGAVIGDGCVIGAGSIVGADSEIGADSRLHANVTVYHGVSVGRRAILHSGCVIGADGFGFAHDGQGWHKIAQLGGVIVGDDVEIGSCSSIDRGALGDTVIGNDVKIDSQVQIAHNVQIGDHSALAGCVGIAGSTRVGSHCMLGGGVGLSGHLTLCDGVQVTGMSLVTNSIHEPGVYSSGTGAMPNGLWR... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q7NVY4 | MSYTLEHIVKQLGGALRGPNREVSRLAPLELAGAGEIAFVASAKFRRQMLESAADALIVTEALAAELPDRSLIVAADPYLYFARLATLFHPPKAPRAGIHPRAVVGVGCRIGESSEIAANATIGDNVVIGERCRLMPGVVVGDGCEIGDDVTLYPNVTIYHDCVIGNRVGVHSGSVIGGDGFGLAWDKDHWFKIPQTGRVVLEDDVEIGANTTVDRGALVDTVIRKGAKIDNLVQIAHNVEIGEHTAIAGCVGIAGSTKIGARCTVGGAAMFVGHIEVADRTHIGGGTLVSKSIKEAGNYASSYPLQSMKDWLSNAVHVR... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q485G0 | MTYTLAEIAIKLDAKLIVPAALDEQNEALTQISGLATLAKAGTGQVAFLANSKYQQQLSSTNASAVIVSPDAVEACQVSALVMDNPYMGYAMLASLLDSTPKVSCGIHPNAVIADDVLIGENVSVGANTVIESGVQLADNVSIGAGCFIGHGAKIGESTILWANITIYHRVEIGHHCLIQASTVIGSDGFGYAPVKGQYKWHKIPQLGSVIIGDHVEIGASTTIDRGALDNTEIRDGVILDNQIQIAHNVIVGENTAIAGCTVIAGSTVIGKNCTIAGLVGVNGHITIADNCVFTGMSMVTKNISQAGVYSSGMPVVQNK... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q1LNE8 | MKTPTLGQLATENGAQVVGDPDLAVVGLAPLDQAGPGDLSFLSNPLYLPQALASAAGAVIVSPADLERIRADGQAEGRNWLVARNPYVCFARVAQRFDRAANADSRTGIDPRASVAPDAVVPASCFIGPNVVIESGARLGERVRILANAFIGASAEIGEDTLIYANVSVYHRCVIGARNILHSGAVIGADGFGFAPDIGPTGVEYVKIPQVGRAVLGNDVEIGANTAVDRGAMADTVIEDGCKIDNQVQIAHNVHVGAHTVIAGTAAVSGSTKIGRFCVIGGAANFSGHLNIADRTTVSGGTSITKSITKPGGHYTSVFP... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q11WA1 | MEFTLEEIAHLLGGEVKGDGKAKVSSIAKIEEASSGSISFLSNPKYESFIYSTNASAVIVKKDFQPRESLKTSLILVDDPYTSFTTILEAYQQALNASKMGKEEPSFIGKNAVIGSNHYIGAFAYIGSNCKIGNNVKIYPQAYIGDNVTIGDNTTIYAGVKIYANCELGNQVTIHSGCVIGSDGFGFAPQADGTYKTIPQIGNVVIGNHVDIGANTVIDCATMGSTIIYDGVKIDNLIQIAHNVKIGKNTVIAAQAGISGSTTIGENCIIAGQVGIIGHIKIANKTTIAAQAGIGRTISEEGLTLLGSPAIEKLDFLKSF... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
A8ZYC0 | MKRSLEQIARLVSGRVVGDAAKKVSGAAPFEQAGPEEITLAGSAGFLKRIDQTGAGALVVPTDFTDSRRNLVAVENPAAAFARIRQMFDTGCRQPVGIDPRAVIGGGFACGEDVSIGPGVVIGDHVTLGDRVLLYPGVFLGNHVRIGNDGIIHANTSILRECVLGNRVIIHAGSVIGSDGFGFAPDGEMYVKIPHSGMVQIDDDVEIGAGNAIDRATFGRTWIRQGVKTDNLVHIAHNVTVGENTIIVAQVGIAGSTTVGRHVILAGQAGISGHLDIGDNAVVGPQAGIVKSIKPGETVSGTPGMPHKLWLRAQSIVAGL... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q6AJ06 | MKENITVAMLAELVDGEVIGDGEVLVGNFVSLETAGEGDITFLVKAGDQDLLTSTKAGAVIVHRKVEVESPATLIKVDDAYLAAAKIHTFLLEDEFSPEGIHRSAFVGEGCQISSEVTIKALVSIGNRVVIGPRTRIESGVAIGDDVTIGEDCLLKANVTIADGSQLGNGVTIHSGTVIGSDGYGYATDKMGFHYKRPQVGTVRVDDNVEIGANSCVDRATYGLTWIKSGAKIDNLVQIAHNVVVGENSLIVSQVGISGSTSLGRNVVMGGKAAAVGHLQIGDGVMIAGGSGVLSNLSAGAVVGGIPARPIKQWRKSVVL... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q2LVL5 | MKKSINEIADFLGGKVVGDGGILIKAVRGIDEAGPGDITFVANPQYEKKLNETGASAVLVTRDTERPGENVTLIQVDDPYVSLGKLLTIFYPEEREKPGISAQAIVEEGAEISPSATVYPGVYISSGAGIGAGVVLYPGVFVGRDAVIGENSILYPNVCVYRRCLIGKRVILHAGAVVGSDGFGFANPGRDNIKIPQIGIVQIDDDVEIGANTTIDRATLGRTWIQRGVKIDNLVQIAHNVVIGEKSIIVSQVGISGSTRLGRSVILGGQAGLVGHLQIGDFAMVGAQSGVHEDVPANSVVSGSPCQPHRNWLRSMSCLP... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q3A555 | MATLNELAELIGGEVVGDGSVVLNRMAPIESAGPGDITFVANPKYLAKLKDTTASAVIVKAGIECPGVNLLICANPYLAFAKVLTALHAQRPAPQGVMDGAWVDPSAELGADVTVHPGCVVGKNVRVGRGTILYPGVVLYDDVQVGEDCLVHAGVLVREQCRLGNRVVVQPGAVIGSDGFGFAPDGKSYYKIPQVGIVAIEDDVEVGANVCIDRAAMGVTLIKRGTKIDNLVQIAHNVSIGEDTILVAQVGIAGSSKVGDHCTLGGQVGVSGHLKIGDNTMVGAQSGIISDLPAGQVFSGTPTMPHREWLKASASMRSLP... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q31N90 | MRWSEFLQHLEAKTGPCTAKAIAGDPELHGVAAINEAQSGQVSFLDQESGLQDWIEQTAASALILPPDPALQARAEARNLPWMTTAQPRLAFAAAIAVFYQPFRPVAGIHPSAVIDPSAQLGDRVSVGAHVVIGANCVIGNDVILHANVVLYPGVSLGDRCQIHANSTIHERSQIGQDCVIHSGAVIGAEGFGFVPTASGWFKMEQSGIVVLEDGVEVGCNSAIDRPAVGETRIGAQTKLDNLVHIGHGCQIGKACAMAAQVGLAGGVEVGDRVILAGQVGVANRVKIGDRAIASSKSGIHGEIEAGAIVSGYPAIPNRQ... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
A0LPR5 | MESCFQGDSRKSYSLSELAEILGAAVRGDPAIRIRGVNSLEDALPDELSFITDVRYKPLLSKCRAAAIIVSPALAELEFPLLVAERPYVVFARAAQLFAEPPFLAPGVHPGAYIGPNVHLGEGVSVGPQAHIGEDCVVGPGTRIYGSAYLGPGVRVGENCMLYPGAVILDRCLLGNRVTVHSGTVVGSDGFGYAQDEKGRHVKIPQTGIVQIDDDVEIGANCTVDRATFGRTWVRRGAKIDNQVQIAHNVVIGEHAILVAQVGISGSTTLGSHVVLAGQVGVAGHIEIGDRARVGAKSGVHHSVGAGEDILGIPGVPARE... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q2JLY8 | MQLQEIAQKLGCAYEGDPTLEIHSVASLAEARPGELSFLSEARYLPLLEQTQASAVIVEEGLALPCSIACLRGRDPRLLFAQAIELFYQPYRLPVGIHPTAVIDPSVELGEGVAIGPHAVVMEGVKIGDHTQIHPNVTIYPHVRIGSRCQLFANCVIHERTEIGDDCLIHSGAVIGDDGFGHIPLADGSWRRMLQAGRVVLEDNVEVGSNTTIDRAAVGETRIGRGTKIDNLVQIGHGVRTGSHCLIVAQVGIAGSTQLGHHVILAGQCGLAGHLHIGDGVRVAAQTGVTSDVPAGQTVAGYPHQPIAEWRKSMAVQRHL... | 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.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
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