ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q2W4D7 | MLIYLIAGEPSGDLLGGRLMAALKERLGEGVSFAGIGGESMRAEGLTSLFPMTELSVMGLVEVLPRIPKILRRVKQTISDIETKRPDALVTIDSWGFNGRIQAGLKARGVPVPRIHYVAPMVWAWKSGRTKTLARVLDLLLTLLPNEPEWFEKEGLKTLHVGHPVIEGAASRGDGAAFRVRHGFAPDRKLLCVLPGSRHSETAKLLAPFGETIALLARRFPDLAVVVPTVETVADEVSQAVKSWALPSMVVRGPEKYDAFAACDAALAASGTVALELAMARLPAVITYKVSPVSAFIATRFLGLSLKFVTLVNILVDEAV... | 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... |
Q1D393 | MTNPPRILVVAGEASGDTHAAELVAALRARRPDLTFFGMGGARLAAQGVELLFDAREVSVMGITEVLPRIPRILQILKGLAEAAAERKPDVAILVDIPDFNLRLAKKLKALGVPVAYYVSPMIWAWRRGRVRTIKRLVDRMLCILPFEEDFYREAGVSARYVGSPVVEQVPSPDTATAFRERLGLSKDAPTLALLPGSRMGEIRRLLPDMVEAAKRLSAERPGLQVVVPLAPTIDREEITSRFEGSGVTPILVEGRAPEVVGASDAAVVASGTAVLEAGLMQRPLVVVYRVSLITYWVGRLMLKVAFVSLINLLAGRRVV... | 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... |
Q9K1F5 | MADKKSPLIAVSVGEASGDLLGAHLIRAIRKRCPQARFTGIGGELMKAEGFESLYDQERLAVRGFVEVVRRLPEILRIRRGLVRDLLSLKPDVFVGIDAPDFNLGVAEKLKRSGIPTVHYVSPSVWAWRRERVGKIVHQVNRVLCLFPMEPQLYLDAGGRAEFVGHPMAQLMPLEDDRETARQTLGVDAGIPVFALLPGSRVSEIDYMAPVFFQTALLLLERYPAARFLLPAATEATKRRLAEVLQRPEFAGLPLTVIDRQSETVCRAADAVLVTSGTATLEVALCKRPMVISYKISPLTYAYVKRKIKVPHVGLPNILL... | 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... |
Q3JAC1 | MENSAPLVAIVAGEASGDQHAAHLIREVKKIAPGVRFGGIAGPQMRAAGVEPLFDSSRLAVVGLVEVLSHLNEIYGAMQKMRHFLEEKHPDLLILVDYPEFNLRLAKRAKTLGIKVLYYISPQVWAWRQYRVHQIGQVVDMMAVVLPFEVPFYEQAGVPVNFVGHPLQHEVKSKFNRNEAVVEFGFNPCCKTLGLLPGSRHSEIKRLLPVLLEAAERIYSEEPEIQYLLPLAATLKEIDLAPYLKGYRLPLRVIPDRSYDVMAACDAMVAASGTVTLEAALMGVPLVVIYKMNSLSYWMGRLLIKVDHIALCNIIAGEGV... | 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... |
C0QR27 | MKKAFISVGEISGDNYASQLVKALPDFMWVGITGPKMREAGVETVEKLENISVVGLMEALPKYFKIKETFKRSVEILDKGIDLLVVVDFPGFNLKLLKEAKKRGIKTVYFIAPQVWAWGKGRIPKIAQYTDLLIAIWPFEKEIYTDYISDSFRVEYVGHPILDIIKTEETEESFKEKIGIEKDKKIFGLLPGSRESEVKTLLPILLSSAEIIYRKREDLHFVIPSTPNMEENVKQIAGSKKVPLSVITVKDFRHPSYEVMKHSVFLNVASGTATLETAIFGNPFLLVYKVSPVTFFIGKMLVSIDYLGLPNIIAGREIIK... | 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... |
B2S6P7 | MNAYQKTIGRAVTLSGVGVHGGAPASARLLPADADTGILFQRSDIKDSAPVCAHVSQIGATDLCTSLGAREARIDTVEHLMAAISALGIDNLVVEIEGPEVPILDGTSARFIEAVDSVGVVTQDAKRRFIRILKTVRVEAGNSWGEFRPYDGTRFEVEIDFECPLIGRQKFAHDVDEETFRKELSTARTFGFMKDVERLWAAGLALGASLDNSLVIGDDNSIVNADGLRFKDEFVRHKTLDAVGDLALAGLPFIGCFSSYRGGHRLNSEAVKALLSDETAFEIIEA | 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... |
B8F3C2 | MIKQRTLKQAAKVTGIGLHSGKKVTLTLRPAPAHTGIIYARTDLDPVVYFPASAESIRDTQLCTCMINDEGVRISTVEHLNAAMSALGLDNLIVEVDAAEIPIMDGSSSPFIYLLLDAGIEEQDAPKKFIRIKESVRVEEGDKWAEFKPYSHGLKLDFTIDFTHPMITKEVRNYKMEFSAQHFIQQLSRARTFTFMKDVEYLQSIGLALGGSLDNAIVLDEYRILNEEGLRFKDELVRHKMLDAVGDLFMCGYNILGDFKAYKSGHSLNNKLLRAVLANENAWEFVTFDDKAEVPQGYQVTEQVFI | 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... |
O25692 | MKQTTINHSVELVGIGLHKGVPVKLVLEPLGENQGIVFYRSDLGVNLPLKPENIVDTKMATVLGKDNARISTIEHLLSAVHAYGIDNLKISVDNEEIPIMDGSALTYCMLLDEAGIKELDAPKKVMEIKQAVEIRESDKFVKIEPDSQLSLNFTIDFNHPVIAKQAHHFVFSKTAYKEQVAKARTFGFLQEVNYLRSIGLAKGGSLNNCIVLDENSILNKEGLRCEKEFVCHKILDAMGDLMVLGMPVMGKYTSFSGSHKLNSMLVKAILADAKNYEVLIAADPAKEFALQKAFA | 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... |
Q31I39 | MKQRTLANPIKAKGVGLHTGHKSIMTLRPAPVNTGIVFRRIDQTPIVEFPVSPELVKETMLCTTIVQEQDNQKIKIATIEHLMSALAGVGIDNLYIDITADEVPIMDGSASHFIFLLQSAGIQLQEASKKFIRIKKQVKVQNEKGGVAEFSPYEGFRLNFSIEFDHPAFDQTAEKMTLSFSSTAYFKEVSRARTFGFMKDMEKLRAQNLGLGAGLHNAIGLDENGVVNQEGLRDKDEFVRHKILDAVGDLYMAGHPIIGEFTAHKSGHALNNQLLRALVADPEAYEVVTYDDEEPPIQYGSSKILV | 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... |
Q9PEI3 | MPIFTAQELAERFNLQLFGDGNLRIHGVATLTQASPEQLSFLANPRYLTQLLNSRAGVIVLHADDVKTASGTVLIAKDPYVTFAKIAALFDIKPAREAGIHPLATVDPSAHVSPTAHVGAFVSIGARSSIGASCIIGTGSIIGDDCTIDDGSELIARVTLISKVRLGKRVRIHPGAVLGGEGFGLAMENGHWIKIPQLGGVVIGDDCEIGANSCIDRGALDDTVLEEDVHIDNLVQIAHNCRIGAHTAIAGCTGIAGSAKIGRYCLLGGHVGVVGHLQICDNVVITGKSVVRNSIHTPGEYSSGTPLTDNRTWRKNAVRF... | 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... |
P32203 | MPSIRLADLAQQLDAQVHGDGDLVITGIASMHSAEPSQITFLSNSRYQEQLATCNAGAVVLTEADLPFCKSAALVVKNPYLTYARMAQIMDTTPQPAQNIAPGAVISPQATLGENVSIGANAVIESGVVLGDNVVIGAGCFIGKNTHIGAGSRLWANVSVYHEVVIGQNCLIQSGTVIGADGFGYANDRGNWIKIPQLGSVHIGDRVEIGACTTIDRGALDNTIIGNGVIIDNQCQIAHNVVIGDNTAVAGGVIMAGSLKVGRYCMIGGASVINGHMEICDKVTITGMGMVMRPITEPGLYPSGIPLQPNKVWRKTAALV... | Function: Catalyzes the N-acylation of UDP-3-O-(hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-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]... |
Q9ZN40 | MKKFLFKQKFCESLPKSFSKTLLALSLGLILLGVFIPFPKVPKHQSVPLALHFTEHYARFIPTILSVAIPLIQRDAVGLFQVANASIATTFLTHATKRALNHVTINDQRLGERPYGGNFNMPSGHSSMVGLAVAFLMRRYSVKKYLWLLPLIPLTMLARIYLDMHTIGAVLAGLGTGMLCVGLFTSPKNLN | Function: Removes the 1-phosphate group from tetra- and probably hexaacylated lipid A species . Absence of the 1-phosphate group renders the bacteria partially resistant to host-derived cationic antimicrobial peptides (CAMP), allowing it to camouflage itself from the host innate immune response, and plays a role in the... |
B2RLI7 | MNRESFLLLLVLLFALPLHLQASSPCNNMADTTCISDSAKMFPPAIGVYHVKPMKNTLRHSLPLVAASLLTFNVDDNIRELRFTGAGSFHTKIDNVSQLVPLMAQLSMRGFGYKGRSKSWGKMLVSDALGMALMGGMVNAGKYSFGRLRPDGTAANSYPSGHTATAFACATLFHLEYGSRSPWYSVAGYTVASFTGISRIVNNRHWASDVLCGAAVGILVGELGYWISDLIFRDPTGYNYKLTKKQEGTLESMVISLSTGNRYINRQMDFEGKTVERTDAFGMNLKTTFNPSFARWVRIGLQFSVSTEKQKGLTRERPAK... | Function: Removes the 1-phosphate group from lipid A species. Absence of phosphate groups in lipid A renders the bacteria resistant to host-derived cationic antimicrobial peptides (CAMP) and allowing it to camouflage itself from the host innate immune response.
Sequence Mass (Da): 49486
Sequence Length: 445
Pathway: Ba... |
Q2K2U9 | MPPLRWQACLFITINAVALSMLLFDAPVGASERPAAVKELGELLTGFGDSAWLICISILLFFQGKAGYKLLKTARSKAQALYVSWIGAYLFTTVVFSGLLANLLKRAIGRARPDHFHDYGMFSFTPFSGHAAFESFPSGHSTTVGAFFAAFALLFPRYRVAFIACAIWLGMTRVMVGAHYPSDVIAGLAFGGWFSLLTAIVYARCGLLFKLAPDGWPLAKRLFPDIEKPGAL | Function: Probably removes the 1-phosphate moiety from lipid A species. Does not seem to act on other membrane components, nor does it dephosphorylate the 4'-phosphate group of lipid A and/or lipid A precursors.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25297
Sequence Length: 232
Pathway: Bacte... |
Q8A6M3 | MIEFLSDIDTQLLLFFNGIHSPFWDYFMSAFTGKVIWVPMYASILYILLKNFHWKVALCYVVAIALTITFADQMCNSFLRPLVGRLRPSNPENPIADLVYIVNGRRGGGFGFPSCHAANSFGLAIFLICLFRKRWLSIFIVLWAFTNSYTRLYLGLHYPGDLVAGAIIGGFGGWLFYFIAHKLTARLQSDTPVPGKGAGMKQTEVMIYTGLLTLAGIIIYSIVQS | Function: Probably removes the 4'-phosphate group from lipid A. Removal of this phosphate group confers resistance to cationic antimicrobial peptides (CAMPs), inflammation-associated peptides produced by the human host. This LPS modification helps maintain the stability of this commensal bacterium in gut microbiota.
Lo... |
A0Q4N6 | MARFHIILGLVVCFFAWIFFLIFPNLDIQFAGHFYNSSAHQFIGGYDGFLGFLHWFARFFPIFFSIIVILFLLGSLFIDKFKIKYRKAIFFIAVCLWIGPGLVVNYVFKDHWGRPRPVMVEQFNGDKIFQPPFVISSQCDKNCSFVCGDASMGFWLFAFMPLLATRKKKLVAFIAAVVAGGGLGLMRMSQGGHFFSDVVFCGIFVYISTWVVYALMYRKKEY | Function: Removes the 4'-phosphate moiety from lipid IV(A) (a tetraacylated precursor of lipid A) and from pentaacylated lipid A, but not from hexaacylated lipid A (as is found in E.coli). Does not dephosphorylate phosphatidic acid, phosphatidylglycerophosphate, or the 1-phosphate group of lipid A and lipid A precursor... |
Q9ZJ31 | MKKLKGLFLSLLLWVYPLKSEPINEGAYILEEIGDVLRFLPIFVGTVSLAMRDYRGLGELAVGTLVTQGVIYGLKGAFSTAHKDGARVGFAKRPCCNSWRGMPSGHAGGAFSAAGFVYYRYGWKPALPVIALAILTDTSRVVAGQHTILQVTIGSLIAWGFAYLFTSRYKPKRWMLYPEISSDFKGSSRYGVGFSYQW | Function: Removes the 4'-phosphate group from tetra- and hexaacylated lipid A species, has no 1-phosphatase or Kdo hydrolase activity. Absence of the 4'-phosphate group renders the bacteria resistant to host-derived cationic antimicrobial peptides (CAMP), allowing it to camouflage itself from the host innate immune res... |
Q21TN9 | MTQPTQSSTWQQHLTRAWTHRGWLAWLLWPISLLYGVLVKLRRSLYQAGIFKSERVPVPVIVVGNVVAGGAGKTPVVMMVVRHLQARGLQVGVISRGYGRQTHDCREVCSDSAITDVGDEPALIQRSTAAPVFVASRRVDAARALLARYAQTQVIVCDDGLQHLGLQRDLEICVFDERGVGNGFLLPAGPLREPWPRAVDLVLHTGTPPAFAGFSAQRTLSRYALMADGSQQALGDLAGPTCLCNKPLLALAAIAKPENFFTMLRAQGLTLARTLALPDHYGFDSWSHNDYEGYTLICTEKDAVKLWPLEPDALAVPLVV... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 38721
Sequence Length: 355
P... |
Q0VQP4 | MGSLSEWVQQGWYKGSPWLVPLRPLSALVSFEARRRLQRFRKQRPRPPVPVLVVGNITVGGTGKTPLVIALVEAARSRGLKVAVVSRGFAGKTNHYPQHVTASSDALDMGDEPVLIARRTGVPVVLDPDRRNALDVAIREYAPDLVISDDGLQHYALPRSAEVVVVDAQRGLGNGRCLPEGPLREPATRLKEVDFVISTGGGWAGAYPMIMRPSGVTCLADNRTLTPDDFLRLHPQVHAVAGIGNPKRFFNLLSILGLSATPHVFPDHHAYQPADLAFTDGLPVLMTEKDAVKCAPFAEPHWWFVPVTASLPEGLLDQML... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35667
Sequence Length: 327
P... |
A8EU81 | MKQKIHLWIEEYLFFPKFFQKIISFLLLPLTLIYLIIIFTKRFKAKKIDFDIPIISIGNIIVGGSGKTPITIELASKYENACVILRGYGRSSKGLQIVSLNGDIKVDVTVSGDEAMLLAKSLKKATIIVSENRIEAILKAKELGSKIIFLDDGFSKYSISKFDILLKPKNEPTNNFCLPSGGYREPKSFYKKANIVLQEGKDFKRVITIKKDENIKELPSYTILLTAISKPKRLLEFLPKNIKMISFPDHHNFTKEEILDIQNEYKDYAILTTGKDMVKLKEFNLENLYLMDLSIKIDENVDFSSMNSYINSFK | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35989
Sequence Length: 314
P... |
Q0A8Q4 | MSELPAFWLRRPPDWRAHALRPLAALYGGVMRLRRYGYRKGWIRRGRLPVPVVVVGNIFVGGTGKTPLVAWIADTLAAMGRRPGIVSRGYGGRSREWPRRVAADSDPAEVGDEPLLLARGTGCPVAVGPDRVAAAQLLLAAGCDVVVSDDGLQHYRLPRALELVVCDGHRGLGNGLCLPAGPLREPADRLADVDMVISNGRAPALTPWWFELVPGPLRPLAADAAPEGGPEPGTTVHAVAGIGHPARFFATLEGLGYRVIPHPFPDHHPYRAGELRFGDDRPVIMTEKDAVKCAGLAPARSWFLPVEARPEPATRERLEA... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35790
Sequence Length: 331
P... |
Q2IL55 | MSGLEAIWWRERPGPLGALAGAPLLLAEAPFRAAAALRGALYDRGLLPAARAGAPVVSIGNLAVGGAGKTPAALAVAARLAGRGRRVAILSRGYGAARADARVASDGAGALLPAAEAGDEPALLARRLPGVAVLCGPRRAELARTAVESLGADALVLDDGFQHRALARDLDVVVLDASNPFGNGHLLPRGPNREPPSALRRAGLVWLSHADRAAPERLEALRALARDATGRAPVESRHAPTALLDGALREAGALEALRGRRVAALSGLARPAGFLRTLEALGAEVALARAFPDHHRFTAGELDAVLREAAASGCAWVVTT... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 38676
Sequence Length: 378
P... |
O67572 | MLRSSLLPFSYLYEKIINFRNTLYDKGFLKIKKLPVPVISVGNLSVGGSGKTSFVMYLADLLKDKRVCILSRGYKRKSKGTLIVSEYGNLKVSWEEAGDEPYLMAKLLPHVSVVASEDRYKGGLLALEKLSPEVFILDDGFQHRKLHRDLNILLLKKKDLKDRLLPAGNLREPLKEIRRADALVLTYQEVEPFEFFTGKPTFKMFREFCCLLNSDFEEVPFDILKEREVIAFSGLGDNGQFRKVLKNLGIKVKEFMSFPDHYDYSDFTPEEGEIYLTTPKDLIKLQGYENVFALNFKVKLEREEKLKKLIYRIFY | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36542
Sequence Length: 315
P... |
Q8LEA0 | MEKLRKVVNEIAYTRVHTNSPALHRSLVPFLTIASSLYGVALQIRRSLYRYSLLQKHRLPVPVISVGNLSWGGNGKTPMVEYISQFLVDSGLTPLILTRGYAGGDEVKMLERHLRGGPVKIGVGANRAATAALFLDKYGCVDSSSLRSFFDLHERAQVWTISEKIGCIILDDGMQHWSLSRDLEIVMLNGLNPWGNGHLMPHGPLREPLLALERADVAVVHHVDLITKQSLRDIENMIQGFKKSIPIFYSKMVPKYLFDVKNARSHVALEALRCASVLCVSAIGSADAFVKSIEMTGAHYVDRLDFSDHHLFEAEDVETM... | Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. 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'... |
Q5P108 | MARNAPAFWQTRSLAARLLLPLSGLFLLLAAVRRQLFRLGIRRAVRLPVPVVVVGNIAVGGSGKTPVVEWLVARLRDAGFTPGIVSRGYGGKAPGAVIVPPHGDVRLFGDEPVLLARLTACPVAVGADRPAAARALLQAYPGCDVIVADDGLQHYPLARDVEIAVVDERTLGNRWLLPAGPLREGPGRLRDVDIIIAHGALSPALSSLLDGRPVFAMHLEGSEFRRLDGAGCRNAEAFRGVRVHAVAGIGRPERFFAQLTRMGLEVVPHPFPDHHPFTAADLDFAPGEPKILTSKDAVKCASFASADTWEFPVKAHIAAG... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35877
Sequence Length: 336
P... |
A8I6A3 | MIGQAPAFWSRRNSLMGWVLSPIGALVGALTLKRMAGPSTGVPVPVICIGNPTVGGSGKTPTALMVLARLQEQGARPFALLRGHGGRLAGPVLVDPQTHTAADVGDEALLLAQATPTVVSRDRPAGAAHAVALGASHVVMDDGFQNPSLAKDVSLLVIDGEAGVGNGRVLPAGPLRAPLAPQLDRADALLVAGGGRCADALGRLAHSHGKVVLRGQVRPDPSVIATLEAGTVLAFAGIGRPQKLADTLAAAGVRIGRLQPFPDHHPYQPSDIAPLIAEAARERWQLVTTTKDHVRLADRRFADMAGAITALPVTMQLDAP... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 34919
Sequence Length: 338
P... |
A1K5I2 | MAAARGAMPTAPSYWRSRGPRALLLYPLSLLFGLLAALRRRLYRAGLLSQVRLPVKVIVVGNIAVGGSGKTPVVAWLVEQLRAAGWHPGIISRGHGGSARGVLEVVASGDAGVCGDEPLLLARLTGVPVFVGRDRPAAAAALLQAHPECDVIVSDDGMQHYRLARDLELAVVDPATLGNRWLLPAGPLREPVGRLDRVDLVIRHGDEGELPPRLGARAVPMRLVGDGFRGVADPARRCEASAFRGRRVHAVAGIGRPQRFFDQLAAMGLDVVPHPFPDHHRFVAADLDFAPGEPKLMTSKDAVKCAPFAPADAWEFPVTA... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36421
Sequence Length: 341
P... |
Q30Y50 | MSSLPLQKSLYPLLRPLGAAYRVLMRARRRRYENGAACGTDVPCVSVGNIGWGGSGKTPVVQWLLQWAAVHGLHAVVLTRGYKASPPGLPYVVTPQSSAAHAGDEPLMLARSCPQATVVVDPVRSRSARWAQERLAPDFFVLDDGFQHVQVARDTDLVLLKKDDLHAEWGRVLPAGSWREGPEALSRAAAFCIKCGSGEFSGLVPDFENRLGSFGVPVFGFSLRPGALIPVCGAHEGAQLPAGAPYVLFSGVGDPAQVAVTVSSFLGYDPVRHHVFADHHGYTQADMDRMAGYGLPLVCTPKDAVKLTAPCGVPVWTLSL... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 38412
Sequence Length: 356
P... |
A6LIV7 | MLTDHTIKFNKLLTPFSFLYGIGVRFRNQLFDWKVLRTERYDLPIICVGNLTVGGTGKTPHTEYIIRLIKDRYRVAVLSRGYKRKTSGFLLADQRSTSKDIGDEPYQMKRKFPDILVAVDADRRRGIRNLLALPENKRPDVIVLDDAFQHRYVAPTLNILLTDCHRLYTQDRLLPAGRLREPMDGARRADVIIVTKCESCIQPIDFRIIEEDIHLSAYQELYFSRILYGELEPVFSGKAPRRTLKGLASTTEVLLVSGIASPAPLEKEIHKYTEHVTSLIFPDHHAFDRHDIQKIQTAFKRLTSTSKLIIITEKDAARLR... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 42738
Sequence Length: 369
P... |
A7HQR4 | MREPRFWYPAQRNSVPLAARLLAPLGYVYGLAGRIRRGRAEPQRAAVPVICVGNLTAGGAGKTPVALTLAEGLIAKGEKVHFLTRGYGGREQGPIRVDPLRHAAADVGDEPLLLAAAAPTWVAANRSEGAAAAVRGGAGLIIMDDGFQNPGLAKDFSILVVDAASGVGNGRLVPAGPLRERVDDALSRANALILTGRGHAGDGIAARARARGIPVFNSIVRPAVAPDFGAGPFLAFAGIGRPEKFYRTLRELGAELAETISFPDHHMFSESEALKLLVRARELGARLITTEKDAARLSHAPVSSARWRLDEAALRLPVRA... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36235
Sequence Length: 342
P... |
B4SDV3 | MHNPLSILLRPAALGYRVIVQLRNTLFDRQLLPAWKSPVPIVSIGNLSVGGTGKTPLVDWVVKYYLSIGCKPAIISRGYRRESKGVQLVSDGQKVLLSSSESGDETAMLAWNNPDAIVIVAKKRKEAVKYLVKHFAARMPSVIILDDAFQHRQIQRELNIAIINVSEPFLKARMLPEGRMREPLKNLSRADLIVLNKIDDPEKADAIVRKIKERGTPLIKARVAIAELVCFSGAFISSEEAPPLTSISALAFAGISSPQSFLDSLGKEGVTIAAHRFFYDHEPYSAKKLTEIFREAESKGLSLITTEKDYFRMLGHPELI... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 39655
Sequence Length: 355
P... |
Q4FPB7 | MKLKKPKFWDHKKPSFFSYLLLPFSIILGLITKIKSKPKFSNSKIKTICVGNIYIGGTGKTSLAIKIKEILDKNNIRACFIKKFYPNQTDEQKLLSKNGVLFSNLKRITALNEAISEGFEVAIFDDGLQDSTIKYDLEIVCFNNLNWIGNGLTLPSGPLRENINNLKSYENVFLNGNEESLIAIKEQIKRINPNININSGKYIPLNIDEFDKDQNYLVFSGIGNHKTFVEMLKNNKLKIVSDLEYPDHYQYSKKDFDEIIINAKKFNAHIITTEKDYLRLENLNKNEIFYVKSSLDISDEKNLTNKLIKLNEKN | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36175
Sequence Length: 314
P... |
Q7N6C5 | MIERIWSGRSWLYLLLLPFSALYGLISGLRWLSYKTGLRLPWKAPVPVVVVGNLTAGGNGKTPVVIWLVEQLQKKGYRVGVVSRGYGGKAESYPLLVTENVTTAQAGDEPVLIHRRTGAPVAVAPKRVAAVKALLANTSLDIIVTDDGLQHYALQRDFEIAVIDGVRRFGNGWWLPAGPMRELSGRLNRVNTIITNGGTPQPGELSMTLAGELAVNMVSGEKRAVNLIPHAVAMAGIGHPPRFFATLQQLGADLKKEYAFADHQLYTEDQLCHLADTNQNLLMTEKDAVKCFNFAQPNWWYLPVDARLPQEKGEIMLNKI... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36449
Sequence Length: 331
P... |
A6L0S5 | MEGNLIKINKWLYPVSWIYGTGVWLRNKLFDWGIYKERKFDIPVISVGNITVGGTGKTPHTEYLIRLLQKDYKVAVLSRGYKRKSKGFVLARPDTSVQMIGDEPFQMKQKFPDIHMAVDRDRCHGIEQLCNSHIAPGTEVIILDDAFQHRYVKPGINILLVDYHRLICEDTLLPAGRMREPENGKSRAHIVIVTKCPKDITPMDLRVLSKQMELYPYQQLYFTTLTYGKLHPLFTAGNAVSLKEIEKDKHILLVTGIASPAKLIQDLSPYNEHIESLAFSDHHDFTARDMELIKKRFMKLPEGKRMIITTEKDSVRLAAH... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 42282
Sequence Length: 366
P... |
A4SVJ1 | MSFSLFRKAPKFWERRGPTSLLLWPLSWLYGLILRARKLIHDLGIVRTKPTPVPIIIVGNIRVGGTGKTPIVIALAKRLSQLGWKPGIISRGYGSSSQTAPLLVRSDSSPSLVGDEPVLIAKRTDNQFPIWVYPKRQQSIQALLKHSPEVDVIISDDGLQHRGLTRWPAREGGRDIEFVVRDSRGEGNRFLLPAGPLREPATRDRDATLFTGNPSFNEKKTGILDEYFLGRRAFSLGTYLGRPYQLIDHANTQSLEQIAEQFLPKSMTAIAGLGNPQRFFDDLAKQGVTCKQIPLPDHAQYTPEFFAKVKAQCLLITEKD... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 40906
Sequence Length: 363
P... |
A1VNK5 | MKQVLLKAWRARGWLARLLWPVAQLHGLLVRLRRALYRRGMLSSERFKVPVIVVGNVVAGGAGKTPLVMALVKHFQAQGLRVGVVSRGYGRSGHESLEVRPGTPVDESGDEPALIQHATGAPVFVAQRRTQALRDLLAAYPATAVVVCDDGLQHYALQRDIEIAVFDDRGVGNGWLLPAGPLREPWPERLRQGVDLVLHTGQQPAFEGYTSRRQLADHAVAADGSSLALTALAHQPVVALAGIASPEAFFDMLRARGLTLQKTLALPDHHDFKTGDLNALAGRTVLCTEKDAVKLFALPDHSKIKLLAVPLEFSPEPAFF... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 37168
Sequence Length: 343
P... |
B2RIK3 | MDAPRINKWLKPLSALYGVGVRLRNYLFDKNVLISNSFDIPIVCVGNITIGGTGKTPHVEYLIRLLHPRYRIAVVSRGYKRKTKGMIVATEGSTAWDIGDEPRQIKRKYPDLTVIVDADRSRAIGYLCDLAEEQRPQLIVLDDGFQHRKVKADLNIVLTDYNRILTKDYLLPAGRLREPAGSIQRADMVILTKCPDDLAPIDLRAAKRDLALYPHQKLFFSKFMYGQGLKPLFSDQSPSAEVRSALAIAGIASPKLFFREIRTRFPSGTDRIYPDHHEFTDREVCLLIQDWHELHRKDANAIVVCTEKDAMRLALRQSSF... | 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).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 40997
Sequence Length: 357
P... |
Q86YD5 | MWLLGPLCLLLSSAAESQLLPGNNFTNECNIPGNFMCSNGRCIPGAWQCDGLPDCFDKSDEKECPKAKSKCGPTFFPCASGIHCIIGRFRCNGFEDCPDGSDEENCTANPLLCSTARYHCKNGLCIDKSFICDGQNNCQDNSDEESCESSQEPGSGQVFVTSENQLVYYPSITYAIIGSSVIFVLVVALLALVLHHQRKRNNLMTLPVHRLQHPVLLSRLVVLDHPHHCNVTYNVNNGIQYVASQAEQNASEVGSPPSYSEALLDQRPAWYDLPPPPYSSDTESLNQADLPPYRSRSGSANSASSQAASSLLSVEDTSHS... | Function: May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production. May regulate ITCH and NEDD4 E3 ligase activity and degradation .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37419
Sequence Length: 345
Subcellular L... |
A2AR95 | MWLLGPLCLLLSSTAESQLLPGNNFTNECNIPGNFMCSNGRCIPGAWQCDGLPDCFDKSDEKECPKAKSKCGPTFFPCASGIHCIIGRFRCNGFEDCPDGSDEENCTANPLLCSTARYHCRNGLCIDKSFICDGQNNCQDNSDEESCESSLEPGSGQVFVTSENQLVYYPSITYAIIGSSVIFVLVVALLALVLHHQRKRNNLMTLPVHRLQHPVLLSRLVVLDHPHHCNVTYNVNNGVQYVATQAEQNASEVGSPPSYSEALLDQRPAWYDLPPPPYSSDTESLNQADLPPYRSRSGSAYSASSQAASSLLSVEASSHN... | Function: May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production . May regulate ITCH and NEDD4 E3 ligase activity and degradation (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37467
Sequence Length: 3... |
O15165 | MPEAGFQATNAFTECKFTCTSGKCLYLGSLVCNQQNDCGDNSDEENCLLVTEHPPPGIFNSELEFAQIIIIVVVVTVMVVVIVCLLNHYKVSTRSFINRPNQSRRREDGLPQEGCLWPSDSAAPRLGASEIMHAPRSRDRFTAPSFIQRDRFSRFQPTYPYVQHEIDLPPTISLSDGEEPPPYQGPCTLQLRDPEQQMELNRESVRAPPNRTIFDSDLIDIAMYSGGPCPPSSNSGISASTCSSNGRMEGPPPTYSEVMGHHPGASFLHHQRSNAHRGSRLQFQQNNAESTIVPIKGKDRKPGNLV | Function: Functions as a negative regulator of TGF-beta signaling and thereby probably plays a role in cell proliferation, differentiation, apoptosis, motility, extracellular matrix production and immunosuppression. In the canonical TGF-beta pathway, ZFYVE9/SARA recruits the intracellular signal transducer and transcri... |
Q9BGL2 | MKNPMLEAVSLVLEKLLFISYFKFFSSGAPGQDKAGNTLYEISSFLRGDVLEVPRTHLTHYGIYLGDNRVAHMMPDILLALTDDKGRTQKVVSNKRLILGVIGRVASIRVDTVEDFAYGAEILVNHLDRSLKKKALLNEEVAQRAEKLLGITPYSLLWNNCEHFVTYCRYGTPISPQADKFCENVKIIIRDQRSVLASAVLGLASIFCLGLTSYTTLPAIFIPFLLWMAG | Function: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters . Retinyl esters are storage forms of vitamin A (Probable). LRAT plays a critical role in vision (Probable). It provides the all-trans retinyl ester substrates for the isomerohydrola... |
O95237 | MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTHYGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGANILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDKFCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG | Function: Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters . Retinyl esters are storage forms of vitamin A (Probable). LRAT plays a critical role in vision (Probable). It provides the all-trans retinyl ester substrates for the isomerohydrola... |
P94516 | MESTMSPYFGIVVSLAAFGIGTFLFKKTKGFFLFTPLFVAMVLGIAFLKIGGFSYADYNNGGEIIKFFLEPATIAFAIPLYKQRDKLKKYWWQIMASIIAGSICSVTIVYLLAKGIHLDSAVMKSMLPQAATTAIALPLSKGIGGISDITAFAVIFNAVIVYALGALFLKVFKVKNPISKGLALGTSGHALGVAVGIEMGEVEAAMASIAVVVVGVVTVLVIPVFVQLIGG | Function: Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to an... |
F4K4E3 | MLPLSLLKTAQGHPMLVELKNGETYNGHLVNCDTWMNIHLREVICTSKDGDRFWRMPECYIRGNTIKYLRVPDEVIDKVQEEKTRTDRKPPGVGRGRGRGVDDGGARGRGRGTSMGKMGGNRGAGRGRG | Function: Component of LSM protein complexes, which are involved in RNA processing. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. The cytoplasmic LSM1-LSM7 complex regulates developmental gene expression by the decap... |
P24094 | MAKKVTVTLVDDFDGAGAADETVEFGLDGVTYEIDLTNKNAAKLRGDLRQWVSAGRRVGGRRRGRSNSGRGRGAIDREQSAAIREWARRNGHNVSTRGRIPADVIDAFHAAT | Function: DNA-bridging protein that has both architectural and regulatory roles. Influences the organization of chromatin and gene expression by binding non-specifically to DNA, with a preference for AT-rich sequences, and bridging distant DNA segments. Represses expression of multiple genes involved in a broad range o... |
Q86X29 | MQQDGLGVGTRNGSGKGRSVHPSWPWCAPRPLRYFGRDARARRAQTAAMALLAGGLSRGLGSHPAAAGRDAVVFVWLLLSTWCTAPARAIQVTVSNPYHVVILFQPVTLPCTYQMTSTPTQPIVIWKYKSFCRDRIADAFSPASVDNQLNAQLAAGNPGYNPYVECQDSVRTVRVVATKQGNAVTLGDYYQGRRITITGNADLTFDQTAWGDSGVYYCSVVSAQDLQGNNEAYAELIVLGRTSGVAELLPGFQAGPIEDWLFVVVVCLAAFLIFLLLGICWCQCCPHTCCCYVRCPCCPDKCCCPEALYAAGKAATSGVP... | Function: Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells (By similarity). Maintains epithelial barrier function by recruiting MARVELD2/tricellulin to tricellular tight junctions ... |
Q99KG5 | MAPAASACAGAPGSHPATTIFVCLFLIIYCPDRASAIQVTVPDPYHVVILFQPVTLHCTYQMSNTLTAPIVIWKYKSFCRDRVADAFSPASVDNQLNAQLAAGNPGYNPYVECQDSVRTVRVVATKQGNAVTLGDYYQGRRITITGNADLTFEQTAWGDSGVYYCSVVSAQDLDGNNEAYAELIVLGRTSEAPELLPGFRAGPLEDWLFVVVVCLASLLFFLLLGICWCQCCPHTCCCYVRCPCCPDKCCCPEALYAAGKAATSGVPSIYAPSIYTHLSPAKTPPPPPAMIPMRPPYGYPGDFDRTSSVGGHSSQVPLLR... | Function: Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells . Maintains epithelial barrier function by recruiting MARVELD2/tricellulin to tricellular tight junctions .
PTM: Phosphor... |
Q15FB5 | MLMLHAVPVGICLLLWYVVYGTKRKECIPTIRRWPRLLPQFLDRLSYNDHAARLVKHGYEKHKNQPFRLLKMDMDLIVIPLQYALELRAVTSDKLDPLTASFDDNAGKVTRILLGSELHTRAIQQRLTPKLPQTLPVLLDELNHAFGQVLPAGNDGSNAWISVNPYELVLNLATRATARLFVGDLICRNEIFLETTASFSRNTFDTISTSRSFGNLFTHYFARWISTAKEAHGQLQYIQNLLGSEVQRRKLNSEEKHDDFLQWCTELAVTEDEARPEALAHRTLGILSMAVIHTTAMALTHILFDMISDDSLKESLRREQ... | Function: Cytochrome P450 monooxygenase; part of the gene clusters that mediates the biosynthesis of lolitrems, indole-diterpene mycotoxins that are potent tremorgens in mammals, and are synthesized by clavicipitaceous fungal endophytes in association with their grass hosts . The geranylgeranyl diphosphate (GGPP) synth... |
Q15FB4 | MKMLTEHFDFPKLNFATIVISGATIIGIIFLRYLNYPTKVNVPVVGIGVRYTKWLAAIINVRHARQSIREGYAKYGDFAFQIPTMTRMEVFICDRQMTREYQNVDDYHLSFRAVMTEEFQFKWLLPGQAHEARIIPNSVIAKALSWQRTRANKPSDPFFESFSAEFMQGFQEEMRRLIQYQNSSVMSNRSGAVLDPAHGWHAVPCFPLALKVIGRLTTYVLFGKPLCQDATFLNMCCQFGDVIPRDAIILRSWPALARPLIVKILSAPRVMGKLRNILIVEIKSRRESHETNPMSDILDFTMAWVDRHPNASFDDQHIAE... | Function: Cytochrome P450 monooxygenase; part of the gene clusters that mediates the biosynthesis of lolitrems, indole-diterpene mycotoxins that are potent tremorgens in mammals, and are synthesized by clavicipitaceous fungal endophytes in association with their grass hosts . The geranylgeranyl diphosphate (GGPP) synth... |
J7FJH0 | MSRSDWIFISLQGFFCLAGVIWKSREGYPIIDFPCPLQFIDSSDATLSYGTTSPWFGFRAVASMQSIWDNGPWFWLHLMLYIAQLVGLILIILHETVPHGAFLRKFESLAALGYLSYTVGLSTAFPVFSLWILNQYRAEKLVTAWPRRQEKAFLRTIFWCTGISHIGIFMVAIVATLLHRDATAPFHIGNSLLGVPDCSQFPCSEIAARHARLRQINEMTGTSSGFFLTVGLFSQALEAENKHLSLRVMVRMFFVSLIAGPAAGSADVLLLRDSITRSKKDCG | Function: Part of the gene cluster that mediates the biosynthesis of lolitrems, indole-diterpene mycotoxins that are potent tremorgens in mammals, and are synthesized by clavicipitaceous fungal endophytes in association with their grass hosts . The geranylgeranyl diphosphate (GGPP) synthase ltmG is proposed to catalyze... |
Q0KBC7 | MSRNIGVIGLGAMGFGVAQSLLRAGFNVHACDLRPEVLQRFADAGGVPCASPAELGSRCDVVLTLVVNAQQTEAVLFGANGAAAAMQPGKLVIASATVPPGFAEALGRRLAEQGLLMLDAPVSGGAARAASGEMTMMTSGPAEAYSLAEDVLAAIAGKVYRLGAAHGAGSKVKIINQLLAGVHIAAAAEAMALGLREGVDPDALYDVITHSAGNSWMFENRVPHILKGDYTPLSAVDIFVKDLGMVLDTARHSKFPLPLSAAAHQMFMMASTAGHGGEDDSAVIKIFPGIELPGKAE | Function: Catalyzes oxidation of L-threonate to 2-oxo-tetronate. Can use either NAD(+) or NADP(+) as cosubstrate, with a preference for NAD(+).
Catalytic Activity: L-threonate + NAD(+) = 2-dehydro-L-erythronate + H(+) + NADH
Sequence Mass (Da): 30439
Sequence Length: 297
EC: 1.1.1.411
|
A0A0H2VA68 | MKTGSEFHVGIVGLGSMGMGAALSCVRAGLSTWGADLNSNACATLKEAGACGVSDNAATFAEKLDALLVLVVNATQVKQVLFGEKGVAQHLKPGTAVMVSSTIASADAQEIATALAGFGLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYRIGSEPGLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFENRMRHVVDGDYTPHSAVDIFVKDLGLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIKIFSGITLPGAKS | Function: Catalyzes oxidation of L-threonate to 2-oxo-tetronate. Can use either NAD(+) or NADP(+) as cosubstrate, with a preference for NAD(+).
Catalytic Activity: L-threonate + NAD(+) = 2-dehydro-L-erythronate + H(+) + NADH
Sequence Mass (Da): 30706
Sequence Length: 302
EC: 1.1.1.411
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O69690 | MGRKVAVLWHASFSIGAGVLYFYFVLPRWPELMGDTGHSLGTGLRIATGALVGLAALPVVFTLLRTRKPELGTPQLALSMRIWSIMAHVLAGALIVGTAISEVWLSLDAAGQWLFGIYGAAAAIAVLGFFGFYLSFVAELPPPPPKPLKPKKPKQRRLRRKKTAKGDEAEPEAAEEAENTELAAQEDEEAVEAPPESIESPGGEPESATREAPAAETATAEEPRGGLRNRRPTGKTSHRRRRTRSGVQVAKVDE | Function: Required for the import of both fatty acids and cholesterol during growth in macrophages and in axenic culture. Facilitates the uptake of these lipids by stabilizing protein subunits of the Mce1 and Mce4 multi-subunit transporters, which transport fatty acids and cholesterol, respectively. Required for full v... |
Q26304 | MEMEKEENVVYGPLPFYPIEEGSAGIQLHKYMHQYAKLGAIAFSNALTGVDISYQEYFDITCRLAEAMKNFGMKPEEHIALCSENCEEFFIPVLAGLYIGVAVAPTNEIYTLRELNHSLGIAQPTIVFSSRKGLPKVLEVQKTVTCIKKIVILDSKVNFGGHDCMETFIKKHVELGFQPSSFVPIDVKNRKQHVALLMNSSGSTGLPKGVRITHEGAVTRFSHAKDPIYGNQVSPGTAILTVVPFHHGFGMFTTLGYFACGYRVVMLTKFDEELFLRTLQDYKCTSVILVPTLFAILNKSELIDKFDLSNLTEIASGGAP... | Function: Produces green light with a wavelength of 570 nm.
Catalytic Activity: ATP + firefly D-luciferin + O2 = AMP + CO2 + diphosphate + firefly oxyluciferin + hnu
Sequence Mass (Da): 60495
Sequence Length: 548
Subcellular Location: Peroxisome
EC: 1.13.12.7
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Q9GV45 | MAYSTLFIIALTAVVTQASSTQKSNLTFTLADFVGDWQQTAGYNQDQVLEQGGLSSLFQALGVSVTPIQKVVLSGENGLKADIHVIIPYEGLSGFQMGLIEMIFKVVYPVDDHHFKIILHYGTLVIDGVTPNMIDYFGRPYPGIAVFDGKQITVTGTLWNGNKIYDERLINPDGSLLFRVTINGVTGWRLCENILA | Function: Catalytic subunit of oplophorus-luciferin 2-monooxygenase. Oxidoreductase that converts coelenterazine (the oplophorus luciferin) to coelenteramide under emission of blue light with a maximum at 454 nm. Is also active with bisdeoxycoelenterazine.
Catalytic Activity: coelenterazine + O2 = CO2 + coelenteramide ... |
P71067 | MQWTQAYTPIGGNLLLSALAALVPIIFFFWALAIKRMKGYTAGLATLGIALIIAVLVYRMPAEKALMSATQGAVYGLLPIGWIIVTSVFLYKITVKTGQFDIIRSSVLSITDDRRLQALLIAFSFGAFLEGAAGFGAPVAISAALLVGLGFNPLYAAGICLIANTAPVAFGAIGIPITAVEGPTGIPAMEISQMVGRQLPFLSVFIPLYLIIIMSGFRKALEIWPAILVSGVSFAVVQYLSSNFLGPELPDVLSALVSMAALAVFLKWWKPKTTFRFAGEQESAASIETARTNPAAPAYRGGQIFKAWSPFLLLTAMISV... | Function: Is the principal permease for the uptake of L-lactate in B.subtilis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59762
Sequence Length: 563
Subcellular Location: Cell membrane
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P23146 | MKFGNFLLTYQPPQFSQTEVMKWLVKLGRISEECGFDTVWLLEHHFTEFGLLGNPYVAAAYLLGATKKLNVGTAAIVLPTAHPVRQLEEVNLLDQMSKGRFRFGICRGLYNKDFRVFGTDMNNSRALMECWYKLIRNGMTEGYMEADNEHIKFHKVKVLPTAYSQGGAPIYVVAESASTTEWAAQHGLPMILSWIINTNDKKAQIELYNEVAQEYGHDIHNIDHCLSYITSVDHDSMKAKEICRNFLGHWYDSYVNATTIFDDSDKTKGYDFNKGQWRDFVLKGHKNTNRRVDYSYEINPVGTPQECIDIIQTDIDATGI... | Function: Light-emitting reaction in luminous bacteria.
Catalytic Activity: a long-chain fatty aldehyde + FMNH2 + O2 = a long-chain fatty acid + FMN + 2 H(+) + H2O + hnu
Sequence Mass (Da): 41401
Sequence Length: 362
EC: 1.14.14.3
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P84810 | MMKLVLFGIIVILFSLIGSIHGISGNYPLNPYGGYYYCTILGENEYCKKICRIHGVRYGYCYDSACWCETLKDEDVSVWNAVKKHCKNPYL | Function: The heterodimer non-edited LVP1 induces lipolysis in rat adipocytes. Induction of lipolysis by LVP1 appears to be mediated through the beta-2 adrenergic receptor pathway (ADRB2). Intracerebroventricular injection is not toxic to mice.
Sequence Mass (Da): 10457
Sequence Length: 91
Domain: Has the structural ar... |
P00719 | MHLMLVLLGLAALLGTSQSRTGCYGDVNRVDTTGASCKSAKPEKLNYCGVAASRKIAERDLQSMDRYKALIKKVGQKLCVDPAVIAGIISRESHAGKALRNGWGDNGNGFGLMQVDRRSHKPVGEWNGERHLMQGTEILISMIKAIQKKFPRWTKEQQLKGGISAYNAGPGNVRSYERMDIGTTHDDYANDVVARAQYYKQHGY | Function: Has bacteriolytic activity against M.luteus.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 22514
Sequence Length: 204
Subcellular Locat... |
Q9SGI7 | MAVSVSKQYMTSLVVILLFISLSSLSPTSTSHSCDPVEEEEEASSFGYVCHSNLQKCHTFAILRAKPPFYSLSDLSRHLGLDADDEYVPKGQLLLIPIECRCNGSIYEASLIKNCVKGDTFRSVSQSLQGLTTCLSIREKNPHISEDKLGDNIKLRLAIRCSCPQEGVSNASFLVTYPVGVRDSVSSLAVRFNTTEDAIVSANNKSGVVPLKPALIPLDHKPEKQGSRKRNPSKKKRSKMKLMIAVSSAIAGVCGLVTLMVFGYLHWKKETQIQTQTQKWISNKDPETRQLSLSIRTTSDKKISFEGSQDGSILDSHNTV... | Function: May recognize microbe-derived N-acetylglucosamine (NAG)-containing ligands.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73162
Sequence Length: 654
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cell membrane
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F4IB81 | MNLTFYIFFLSLLPSFSSSKPMNCSDTTRLCSSFLAFKPNQNQSFSVIQSMFDVLPQDITADISGGYFFIKKNCSCLTTTHQYTTNTTFTIRQNVGYVYNVTVSAYSGLAFPPNTTRAARAGAVVSVQLLCGCSSGLWNYLMSYVAMAGDSVQSLSSRFGVSMDRIEDVNGILNLDNITAGDLLYIPLDSVPGEPYETSKINPPAPSPAPASSLANGNISDDQVNHTAKSGSHVPYIWIVGGLGVVLALLVLCILVCICLRSSSCSSSEEDGNGHNFQILRKSGFFCGSGRYNCCRSGDFRQTNGETQVVAIPKALGDGM... | Function: Putative Lysin motif (LysM) receptor kinase that may recognize microbe-derived N-acetylglucosamine (NAG)-containing ligands.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 71445
Sequence Length: 651
Subcellular Location: Cell membrane
EC: 2.7.11.-
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Q6UD73 | MNLKNGLLLFILFLDCVFFKVESKCVKGCDVALASYYIIPSIQLRNISNFMQSKIVLTNSFDVIMSYNRDVVFDKSGLISYTRINVPFPCECIGGEFLGHVFEYTTKEGDDYDLIANTYYASLTTVELLKKFNSYDPNHIPVKAKINVTVICSCGNSQISKDYGLFVTYPLRSDDTLAKIATKAGLDEGLIQNFNQDANFSIGSGIVFIPGRDQNGHFFPLYSRTGIAKGSAVGIAMAGIFGLLLFVIYIYAKYFQKKEEEKTKLPQTSRAFSTQDASGSAEYETSGSSGHATGSAAGLTGIMVAKSTEFTYQELAKATN... | Function: Putative receptor for S.meliloti Nod factor signals essential for the establishment of the nitrogen-fixing, root nodule symbiosis with S.meliloti . Involved in the control of root hair curling after S.meliloti infection, probably by modulating the reorganization of the microtubular cytoskeleton in epidermal a... |
O64825 | MISFSFHLLVFILLSLSSFATAQQPYVGISTTDCSVSDNTTSVFGYSCNGLNKTCQAYVIFRSTPSFSTVTSISSLFSVDPSLVSSLNDASPSTSFPSGQQVIIPLTCSCTGDDSQSNITYTIQPNDSYFAIANDTLQGLSTCQALAKQNNVSSQSLFPGMRIVVPIRCACPTAKQINEDGVKYLMSYTVVFEDTIAIISDRFGVETSKTLKANEMSFENSEVFPFTTILIPLVNPPANTNSLIPPPPPPPPQSVSPPPLSPDGRKSKKKTWVYALAGVLGGALVLSVIGAAIFCLSKKKTKTQTQEETGNLDSFMGKKP... | Function: Lysin motif (LysM) receptor kinase that functions as a cell surface receptor in chitin elicitor (chitooligosaccharides) signaling leading to innate immunity. Recognizes microbe-derived N-acetylglucosamine (NAG)-containing ligands. Involved in the resistance to the pathogenic fungus Alternaria brassicicola and... |
O22808 | MAACTLHALSVTLFLLLFFAVSPAKAQQPYVNNHQLACEVRVYDNITNGFTCNGPPSCRSYLTFWSQPPYNTADSIAKLLNVSAAEIQSINNLPTATTRIPTRELVVIPANCSCSSSSGGFYQHNATYNLSGNRGDETYFSVANDTYQALSTCQAMMSQNRYGERQLTPGLNLLVPLRCACPTAKQTTAGFKYLLTYLVAMGDSISGIAEMFNSTSAAITEGNELTSDNIFFFTPVLVPLTTEPTKIVISPSPPPPPVVATPPQTPVDPPGSSSSHKWIYIGIGIGAGLLLLLSILALCFYKRRSKKKSLPSSLPEENKL... | Function: May recognize microbe-derived N-acetylglucosamine (NAG)-containing ligands.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 72569
Sequence Length: 664
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cell membrane
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Q93ZH0 | MKIPEKPIFLIFVSLILASSLTFTATAKSTIEPCSSNDTCNALLGYTLYTDLKVSEVASLFQVDPISILLANAIDISYPDVENHILPSKLFLKIPITCSCVDGIRKSVSTHYKTRPSDNLGSIADSVYGGLVSAEQIQEANSVNDPSLLDVGTSLVIPLPCACFNGTDNSLPAVYLSYVVKEIDTLVGIARRYSTTITDLMNVNAMGAPDVSSGDILAVPLSACASKFPRYASDFGLIVPNGSYALAAGHCVQCSCALGSRNLYCEPASLAVSCSSMQCRNSNLMLGNITVQQTSAGCNVTTCDYNGIANGTILTMLTRS... | Function: Required as a cell surface receptor for peptidoglycan (PGN) elicitor signaling leading to innate immunity. Plays an essential role in detecting PGNs and restricting bacterial growth (of Pseudomonas syringae pv. tomato DC3000 for example).
Location Topology: Lipid-anchor
Sequence Mass (Da): 43490
Sequence Leng... |
O23006 | METSCFTLLGLLVSLSFFLTLSAQMTGNFNCSGSTSTCQSLVGYSSKNATTLRNIQTLFAVKNLRSILGANNLPLNTSRDQRVNPNQVVRVPIHCSCSNGTGVSNRDIEYTIKKDDILSFVATEIFGGLVTYEKISEVNKIPDPNKIEIGQKFWIPLPCSCDKLNGEDVVHYAHVVKLGSSLGEIAAQFGTDNTTLAQLNGIIGDSQLLADKPLDVPLKACSSSVRKDSLDAPLLLSNNSYVFTANNCVKCTCDALKNWTLSCQSSSEIKPSNWQTCPPFSQCDGALLNASCRQPRDCVYAGYSNQTIFTTASPACPDSA... | Function: Chitin elicitor-binding protein involved in the perception of chitin oligosaccharide elicitor.
Location Topology: Lipid-anchor
Sequence Mass (Da): 37739
Sequence Length: 350
Subcellular Location: Cell membrane
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P0DP58 | MTPLLTLILVVLMGLPLAQALDCHVCAYNGDNCFNPMRCPAMVAYCMTTRTYYTPTRMKVSKSCVPRCFETVYDGYSKHASTTSCCQYDLCNGTGLATPATLALAPILLATLWGLL | Function: Acts in different tissues through interaction to nicotinic acetylcholine receptors (nAChRs) . The proposed role as modulator of nAChR activity seems to be dependent on the nAChR subtype and stoichiometry, and to involve an effect on nAChR trafficking and its cell surface expression, and on single channel prop... |
M4GGR9 | MSLGIRYLALLPLFVITACQQPVNYNPPATQVAQVQPAIVNNSWIEISRSALDFNVKKVQSLLGKQSSLCAVLKGDAYGHDLSLVAPIMIENNVKCIGVTNNQELKEVRDLGFKGRLMRVRNATEQEMAQATNYNVEELIGDLDMAKRLDAIAKQQNKVIPIHLALNSGGMSRNGLEVDNKSGLEKAKQISQLANLKVVGIMSHYPEEDANKVREDLARFKQQSQQVLEVMGLERNNVTLHMANTFATITVPESWLDMVRVGGIFYGDTIASTDYKRVMTFKSNIASINYYPKGNTVGYDRTYTLKRDSVLANIPVGYAD... | Function: Amino-acid racemase that catalyzes the interconversion of L-lysine and D-lysine. To a lesser extent, is also able to interconvert arginine enantiomers . Cannot use methionine, asparagine, alanine, leucine, glutamine, phenylalanine and histidine as substrates (Ref.1).
Catalytic Activity: L-lysine = D-lysine
Lo... |
P02987 | MKKAKAIFLFILIVSGFLLVACQANYIRDVQGGTVAPSSSSELTGIAVQ | Function: Lysis proteins are required for both colicin release and partial cell lysis.
Location Topology: Lipid-anchor
Sequence Mass (Da): 5157
Sequence Length: 49
Subcellular Location: Cell outer membrane
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P40495 | MFRSVATRLSACRGLASNAARKSLTIGLIPGDGIGKEVIPAGKQVLENLNSKHGLSFNFIDLYAGFQTFQETGKALPDETVKVLKEQCQGALFGAVQSPTTKVEGYSSPIVALRREMGLFANVRPVKSVEGEKGKPIDMVIVRENTEDLYIKIEKTYIDKATGTRVADATKRISEIATRRIATIALDIALKRLQTRGQATLTVTHKSNVLSQSDGLFREICKEVYESNKDKYGQIKYNEQIVDSMVYRLFREPQCFDVIVAPNLYGDILSDGAAALVGSLGVVPSANVGPEIVIGEPCHGSAPDIAGKGIANPIATIRST... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the NAD(+)-dependent conversion of homoisocitrate to alpha-ketoadipate.
Catalytic Activity: (2R,3S)-homoisocitrate + NAD(+) = 2-oxoadipate + CO2 + NADH
Sequence Mass (Da): 40069
Sequence Length: 371
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via... |
P61944 | MKIPVFLLLLALANAKVFQRCEWARVLKARGMDGYRGISLADWVCLSKWESQYNTNAINHNTDGSTDYGIFQINSRWWCNDDRIPTRNACNIKCSALQTDDVTVAINCAKRVVSDPQGIRAWVAWNRHCQNRDLSAYIAGCGL | Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidog... |
P0C8X2 | SIYERCELARELINR | Function: Lysozymes have primarily a bacteriolytic function.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 1865
Sequence Length: 15
Subcellular L... |
Q9AJC6 | MKVLVLGAGLMGKEAARDLVQSQDVEAVTLADVDLAKAEQTVRQLHSKKLAAVRVDAGDPQQLAAAMKGHDVVVNALFYQFNETVAKTAIETGVHSVDLGGHIGHITDRVLELHERAQAAGVTIIPDLGVAPGMINILSGYGASQLDEVESILLYVGGIPVRPEPPLEYNHVFSLEGLLDHYTDPALIIRNGQKQEVPSLSEVEPIYFDRFGPLEAFHTSGGTSTLSRSFPNLKRLEYKTIRYRGHAEKCKLLVDLTLTRHDVEVEINGCRVKPRDVLLSVLKPLLDLKGKDDVVLLRVIVGGRKDGKETVLEYETVTFN... | Function: Catalyzes the oxidative deamination of L-lysine in the presence of NAD. Can also use (S)-(2-aminoethyl)-L-cysteine as a substrate, but more slowly. Can use both NAD and NADP but the preferred substrate is NAD.
Catalytic Activity: L-lysine + NAD(+) = 2 H(+) + L-1-piperideine-6-carboxylate + NADH + NH4(+)
Seque... |
Q556Y7 | MRLLVTLILLIFVLTVSGQYSCSNPCYGNMCCSIPSNNEYYLTTFCDESTACGTPCSAQTYFTADSQRFGCGVTLTICSTSGGSTTTGGTGSAGTSTSSGSGSGSGSGSGSGSGSGSGTSGSSSSGSSSGSGSGSSSGSGGSSGSGSGSTMETGGFYGVCVKAITIDAGPNISVEEEAGMAIIDASSQICQDLFGSSSCGWSDKRSITAVQSSVEDGFPVNKPFNVTFEDYNKIISNSLILDQQCSNKNNCKYNKLELMK | Function: Has antibacterial activity.
PTM: Contains disulfide bonds.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 26057
Sequence Length: 260
Sub... |
P83972 | MKAFIVLVALACAAPAFGRTMDRCSLAREMSNLGVPRDQLARWACIAEHESSYRTGVVGPENYNGSNDYGIFQINDYYWCAPPSGRFSYNECGLSCNALLTDDITHSVRCAQKVLSQQGWSAWSTWHYCSGWLPSIDDCF | Function: Unlikely to play an active role in the humoral immune defense. May have a function in the digestion of bacteria in the food.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in... |
P78285 | MPPSLRKAVAAAIGGGAIAIASVLITGPSGNDGLEGVSYIPYKDIVGVWTVCHGHTGKDIMLGKTYTKAECKALLNKDLATVARQINPYIKVDIPETTRGALYSFVYNVGAGNFRTSTLLRKINQGDIKGACDQLRRWTYAGGKQWKGLMTRREIEREVCLWGQQ | Function: Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity. Exhibits lytic activity against E.coli and S.typhi cell wall substrate.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between ... |
Q8N6I4 | MPKPPDYSELSDSLTLAVGTGRFSGPLHRAWRMMNFRQRMGWIGVGLYLLASAAAFYYVFEISETYNRLALEHIQQHPEEPLEGTTWTHSLKAQLLSLPFWVWTVIFLVPYLQMFLFLYSCTRADPKTVGYCIIPICLAVICNRHQAFVKASNQISRLQLIDT | Function: Required for mannose-6-phosphate-dependent trafficking of lysosomal enzymes . LYSET bridges GlcNAc-1-phosphate transferase (GNPTAB), to the membrane-bound transcription factor site-1 protease (MBTPS1), thus allowing proteolytic activation of the GNPTAB. GNPTAB is involved in the regulation of M6P-dependent Go... |
Q8BH26 | MPKAPDCSELSDSCSLAGGTGRFSGPLHRAWRMMNFRQRMGWIGVGLYLLASAAAFYYVFEINETYNRLALEHILQHPEEPREGTTWTHSLKARLLSLPFWLWTIIFLIPYLQMFLFLYSCTRADPKTVGYCIIPICLAVICNRHQAFVKASNQISRLQLIDT | Function: Required for mannose-6-phosphate-dependent trafficking of lysosomal enzymes. LYSET bridges GlcNAc-1-phosphate transferase (GNPTAB), to the membrane-bound transcription factor site-1 protease (MBTPS1), thus allowing proteolytic activation of the GNPTAB. GNPTAB is involved in the regulation of M6P-dependent Gol... |
A8M8Q9 | MRRACIIGASGVIGGELLRLLLGHNNVEVVCATSRRFAGEFIYRVHPNLRGFINLKFTQPSIDAVLKSESDVVFLALPHGESVKWVPKLVESGLLAIDLSADFRLKNPDDYVKWYHWPQPHPYPDLLKAAAYGLPELHRDEIKATKVIAVPGCMATASIVSLAPLVKGHLINNDFIVVDAKIASSGAGAEGTVLDYHWHRTHVVRPYQPVGHRHTAEIEQELSLLAGSQVNVAFTPHAVDMVRGIFVTGHARLSGSISEPDLWRAYRGMYGNERFIRIVKDKAGLAHYPSVKYVVGTNMVDVGFELDQRLNRVVVFSAID... | Function: Involved in both the arginine and lysine biosynthetic pathways.
Catalytic Activity: [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + H(+) + NADPH
Sequen... |
Q9RVQ9 | MSTEKKTVAIVGGSGYAGGEFLRLALGHPHLEVTQVTSERSAKLPVSMVHPNLRGATNLKFRKAAELEEADIIVLALPHNSAAKRITEFEAKGKVIVDLSADFRLKDPEVYERFYGEPHPAPEQLGQWVYGNPELHREDLRGATRIACAGCFATSVILALYPLLRLGALAPKDIIATGLVGSSAAGASASESSHHPERAGSLRVYKPVGHRHTAEAQQELPGKFPLHLTAISTPRVRGILTTIQAWVPDGWSDKDVWSAYREVYGQEPFIRIVKVAKGIHRYPDPMLLDGTNFCDIGFEMDVDTGRVVLMSAIDNLVKGT... | Function: Catalyzes the NADPH-dependent reduction of [LysW]-aminoadipate 6-phosphate to yield [LysW]-aminoadipate 6-semialdehyde.
Catalytic Activity: [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosph... |
Q5UZ50 | MTYTASVVGGSGFTGGELLRLLDGHPEFELAQATSRSKENKTIGHSHPNLRHSDLRFSSPEDLESVDVLFAATPHGVSMEQIDAFQEAAGTVVDLSADFRLESEAQYDEWYDGHTRPKLLEQSEYALPELNRDNLEGADLIASGGCNATATILGLLPLFEADILSGDEQIVVDVKVGSSEGGAGGGEASSHPERSGVVRPYAPTGHRHEAEIQQFLGIDVSFTVHAVDMIRGASATCHVFPEQRVSKGDLWGAYRGEYEDEPFVELVAGGGGVYRYPEPKSVAGTNRAEVGFELDPGNKRLVVFSAIDNMMKGSAGQAVH... | Function: Involved in both the arginine and lysine biosynthetic pathways.
Catalytic Activity: [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + H(+) + NADPH
Sequen... |
A8AAF8 | MTYEVAIVGASGYTGGELLRVLAVHPDVNVKVVTSREYANKPVYYAHPHLRGIYPASLKFKRLDDPDQLSDVVGDVDLVFLALPHKVSLHYVPKALEVGYKVVDLSADYRLKRVEDYKTWYGYEHPYPDLLEKAVYGLPELYGDKIRGAQLVANPGCNATSSILAVLPPAAERIIDLDRIVVDVKVGSSEAGAKPYRGGHHPEREGTARPYDAEGHRHVAELEQVIRDYTGRDVKVGFTPHAVSMIRGSLASAYSWLTKDLAPLDVQRIYAKYYAGKKFVKIVRGAPMPYPDVKNVYGSNYAEVGFALDKRVGRLAMFAA... | Function: Involved in both the arginine and lysine biosynthetic pathways.
Catalytic Activity: [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + H(+) + NADPH
Sequen... |
A9A1K6 | MKVGVVGASGYVGGETLRLLVNHPNVEITMVTSRQHVGEYLHRVQPSLKGFTDLTFSELDYDKLTDKCDLVFTAVPHGTATEIVKALYDRGIKIIDLSADYRLHDQDAYDKWYGWEHPHPDYLNKSVFGVPELHREEIKKAQLVSCPGCMAVTSMLALAPLIRNNIIDTDHIVVDSKIGSSGAGSGSGTAHAMRAGVIRPYKPAKHRHTGEIEQELSEIAGKKIHVSMSPHAVDVVRGILCTNHTFMQKDMEEKELWKLYRQTYGEEKFVRLIRDKKGLYKFPDPKFLVGSNFCDIGFDLDEDNNRLIALSASDNLMKGA... | Function: Involved in both the arginine and lysine biosynthetic pathways.
Catalytic Activity: [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + H(+) + NADPH
Sequen... |
Q6KYZ5 | MQVGIVGGSGYIAGQLLRMLAFHKDIEIKIVSSKSHAGEKLSRVHPDLLNILDLRFSDMDPVDLASRVDLVFLALPHGTSINYVPDIYEIGTKIIDMSADFRLKDPDLYREWYGFEHNYPDLLEKFVYGMPEFHRNEIKNSRYVSVPGCIASSTIYSVAPFSMLNLDNNIVTVDAKVGSSGSGSGTDSSKNYSERYNSVRAYKPVHHRHTPEIEQEIKYISGKNIKIAMSAHSVNMVRGILTTSNIFIDLDEPDALSQLREFYKNEKFIRLIFDRKSNFRYPDPKTVIGTNFADLGVISDGYIKRIVSLGAIDNMIKGAA... | Function: Involved in both the arginine and lysine biosynthetic pathways.
Catalytic Activity: [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + H(+) + NADPH
Sequen... |
O59397 | MIKVAIVGGSGYIGGELIRLLAMHPEVEIVAVTSREYAGKKVHKVHPNLRGLNLRFTSDYNFDADVIFLAVPHGVSMKLINEFLGSAKIIDLSADFRVRKELYEKYYGKHERPELIEDFVYGLPEIHRKEIKKAELVANPGCNATAVILALYPFKDLTKEVLVDLKVSSSAGGRRENLPSIHPERSNVVRVYKPYHHRHEAEVLQETGVRAMFTVHSVDIVRGLLATIYFTFEGNEKDLLKRMLIYKDEPFIRLVVDKGGLQRYPDPKYVLGSNFVDLGLAYDEENSRVIVFSALDNLIKGGAGQAVQNMNIMFGLDETL... | Function: Involved in both the arginine and lysine biosynthetic pathways.
Catalytic Activity: [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + H(+) + NADPH
Sequen... |
Q980X1 | MKDKVRVAVVGGSGYTGGELLRILVTHPKTEISVITSREYAGKPVSLIHPNLRGLISLNFTNFSIDKISDKADAIFLALPHGVSLNYAPKLLDLGLTVVDLSADFRLKNPELYKIWYNYEHPYPDLLDKAVYGLPELHYEELKNAKLIASPGCNATATILALAPIVATKITDEKKFISDVKVGSSEGGAKPSEGSHHPERQNAIRPYEAEGHRHAAEAEQELSRIAKANISVSIVPHAVSSIRGALASAHTWLTNELEEIEIWKKIAEFYRGKRFIRIIRGNIHPYPDPKFVIGSNFADIGFAVEKRISRLTTFSAIDNL... | Function: Involved in both the arginine and lysine biosynthetic pathways.
Catalytic Activity: [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + H(+) + NADPH
Sequen... |
Q8DVB6 | MLMILLFQRLGIIMILAFLLVNNSYFRQLIEERSKREKLVLIIIFGIFVIISNMTGIEITSDKSLVERPILTTISHSDSLANTRTLVITTASLVGGPLVGTVVGFIGGVHRFFQGNFSGAFYIVSSALVGYISGRLGDQLKTNNLYPSTSQVIVISIIAESIQMLFVGFFTGWDLVKLIFIPMMLLNSLGSTLFLAILKTYLSNERQLRAVQTRDVLDLTQQTLPYLRQGLSQQSATKVCNIIKQHTNFDAVGLTDRTNVLAHIGVGQDHHIAGQAVKTDLSKSVILNGQPQIALDKTAIACPDQSCLLNSAIVVPLKIN... | Function: Member of the two-component regulatory system LytR/LytS that probably regulates genes involved in cell wall metabolism.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64274
Sequence Length: 580
Subcellular... |
P94514 | MLRVLIVDDEMLARDELAYLLKRTNDEMEINEAENIESAFDQMMDQKPDLLFLDVDLSGENGFDIAKRLKKMKHPPAIVFATAYDQYALKAFEVDALDYLTKPFDEERIQQTLKKYKKVNRDIVETEQNSHAGQHKLALSVGESIVIVDTKDIIYAGTEDGHVNVKTFDHSYTVSDTLVVIEKKLPDSDFIRVHRSFVVNTEYIKEIQPWFNSTYNLIMKDGSKIPVSRTYAKELKKLLHI | Function: Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism.
PTM: Phosphorylated by LytS.
Sequence Mass (Da): 27834
Sequence Length: 241
Subcellular Location: Cytoplasm
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Q82Z76 | MHVLIVDDEPLAREELSYLVSQHPQVTSVAEADSVAEAMEEMMDQKPDLLFLDIHLTDESGFDLAEKLTHLKKAPYLVFATAYDQYALKAFQVNAKDYILKPFEEEKITQVIEKASKEMGQAVPENTAEKGPKSEAIPIQGEDRIYLVAPEDIYLVSVEERQLSIFVDQQVYKMTGTLNSIEQKLPATLFIKTHRSFILNRTKIQEIQPWFNNTLQVILTNGSKVPVSRSYVKEFKEKLGLS | Function: Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism.
PTM: Phosphorylated by LytS.
Sequence Mass (Da): 27551
Sequence Length: 242
Subcellular Location: Cytoplasm
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Q8EQQ3 | MKIHIMIAEDERLAREELMYLLQQENDIILCPSAENGDQLLNLYQEYNPNVIFLDIHMPGINGIEVAKKIRNEFEDKDIIIIFTTAYESYGVQAFEIQATDYLLKPFSEERFKIAMNRIRKTLSTKKVRKPKVDKLVVNLDEKMMVIDPNQIGFAAREGRTVKIHFISNEVIETKMNLKELEEKLSGFPFYRPHRSYLVNMDCIKEITPWFNGAYNLVIKDLAESTIPVSRTAAKGLFDALQGVHH | Function: Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism.
PTM: Phosphorylated by LytS.
Sequence Mass (Da): 28511
Sequence Length: 246
Subcellular Location: Cytoplasm
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C5FP82 | MARPAAGPGGISKFGNDFGLQRWRNTPRYDQTQPLEGSVCGYGLSNPFHESLFSCPAASWPQAKLGRPNTPQEPSKDLKRILSQISPKRIEATIRKLVSFGTRHTLSTQTNATHGIGAARDWIASEFQRYADASDGRLTVKVIGYEQQPDGSRVLFPVRISDVVATLKGSEDPERVYVVSGHYDSRASDPLDYKTDAPGANDDASGVAVSLEIARVMSQRNLPRPKATIVFAAVAGEEQGLLGSNFLAQTYRNSSTNVEGMFTNDIIGSSTADDGTKEPHVIRLFAQGVPPLNVENQAMREKRLMIGGENDTPARQLARF... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Sequence Mass (Da): 55828
Sequence Length: 508
Subcellular Location: Secreted
EC: 3.4.-.-
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A4R017 | MRSPPGAVAALASVAAQLATAALVPRDAAAPTTAAMPLPFPAQVGIDDSNLATCANANWPPPSSPVGEVISAQLPDADLQAALGEVDPARIRAIVDKLVGFGTRHTLSTQTDPTRGIGAARDWIAEEMRGYAATAGGRMEVTVPGYVQGVASRISFPVKISNVVATLKGDKDPDRVYVVSGHYDSRVTDVMNYEADAPGANDDASGVALAMELARIFATRRPAATIVFTAVAGEEQGLYGSAFMAQTYRNASVNVEGVLNNDIIGSSTGSRGEKDPHTVRVFCQGGSPAGESKERAETRASIGGENDSPARELGRFIAEV... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Sequence Mass (Da): 52930
Sequence Length: 502
Subcellular Location: Secreted
EC: 3.4.-.-
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B2W3C7 | MLFRSALLSNVLLLPACAHDVLFSRDLPLPIAANAESYTDCANAAWPPSNVGVELVPQPPDDELRAMVDEMSAENIEATITKLVSFGTRHTLSTFNSSTRGINAARDWIASEMRKYAAESNGTMTVEVQSYVQGVASRIPFPVTISNVLAKATGSEDPSRVYVMTGHYDSRVTDVLNYESDAPGANDDASGTAIAMELARVLAKHQPKSTIILGAVSGEEQGLYGSTYLAQTLKNTSTNVEGMLNCDIVGSSTGDRGQKDPFTIRAFAQGPPPLSAESSAKAAQRLQIGGENDSPARELARFSAEVAANNATGMKVAIIY... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Sequence Mass (Da): 52235
Sequence Length: 483
Subcellular Location: Secreted
EC: 3.4.-.-
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Q92918 | MDVVDPDIFNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQKEILILKTCRHANIVAYHGSYLWLQKLWICMEFCGAGSLQDIYQVTGSLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFGISAQIGATLARRLSFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQPPLFDVHPLRVLFLMTKSGYQPPRLKEKGKWSAAFHNFIKVTLTKSPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLKNPGKGPSIGDIEDEEPELPPAIPRRIRS... | Function: Serine/threonine-protein kinase, which may play a role in the response to environmental stress . Appears to act upstream of the JUN N-terminal pathway . May play a role in hematopoietic lineage decisions and growth regulation . Able to autophosphorylate . Together with CLNK, it enhances CD3-triggered activati... |
Q12851 | MALLRDVSLQDPRDRFELLQRVGAGTYGDVYKARDTVTSELAAVKIVKLDPGDDISSLQQEITILRECRHPNVVAYIGSYLRNDRLWICMEFCGGGSLQEIYHATGPLEERQIAYVCREALKGLHHLHSQGKIHRDIKGANLLLTLQGDVKLADFGVSGELTASVAKRRSFIGTPYWMAPEVAAVERKGGYNELCDVWALGITAIELGELQPPLFHLHPMRALMLMSKSSFQPPKLRDKTRWTQNFHHFLKLALTKNPKKRPTAEKLLQHPFTTQQLPRALLTQLLDKASDPHLGTPSPEDCELETYDMFPDTIHSRGQH... | Function: Serine/threonine-protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Acts as a MAPK kinase kinase kinase (MAP4K) and is an upstream activator of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway and to a lesser extent of the ... |
Q8IVH8 | MNPGFDLSRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHPNIVAYFGSYLRRDKLWICMEFCGGGSLQDIYHVTGPLSELQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSFIGTPYWMAPEVAAVERKGGYNQLCDLWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFVTQHLTRSLAIELLDKVNNPDHSTYHDFDDDDPEPLVAVPHRIHSTSR... | Function: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 101316
Sequence Length: 894
EC: 2.7.11.1
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Q9Y4K4 | MEAPLRPAADILRRNPQQDYELVQRVGSGTYGDVYKARNVHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHTKGKMHRDIKGANILLTDHGDVKLADFGVAAKITATIAKRKSFIGTPYWMAPEVAAVEKNGGYNQLCDIWAVGITAIELGELQPPMFDLHPMRALFLMSKSNFQPPKLKDKTKWSSTFHNFVKIALTKNPKKRPTAERLLTHTFVAQPGLSRALAVELLDKVNNPDNHAHYTEADDDDFEPHAIIRHT... | Function: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 95024
Sequence Length: 846
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q8BPM2 | MEAPLRPAADILRRNPQHDYELVQRVGSGTYGDVYKARNVHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQDIYHVTGPLSEMQIAYVCRETLQGLAYLHTKGKMHRDIKGANILLTDHGDVKLADFGVAAKITATIAKRKSFIGTPYWMAPEVAAVEKNGGYNQLCDIWAVGITAIELGELQPPMFDLHPMRALFLMSKSNFQPPKLKDKTKWSSTFHNFVKIALTKNPKKRPTAERLLTHTFVGQPGLSRALAVELLDKVSNPDNHAPYSEGDEDDLEPHAIIRHT... | Function: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 95045
Sequence Length: 847
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P75831 | MTPLLELKDIRRSYPAGDEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKATSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAEQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRTEYYPAQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAIEKVNVTGGTEPVVNTVSGWRQFVSGFNEALTMAWRALAANKMRTLLTMLGIIIGIASVVSIVVVGDAAKQMVLADIRSIGTNTIDVYPGKDF... | Function: Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. When overexpressed, the system confers resistance against ma... |
Q7VMF9 | MKQPLIELKNIERYHTNGDTLTTVLKSINLKIYSGEMVAIVGASGSGKSTLMNIIGALDVPNSGEYFIYGRNIADLSGDELAELRCRHFGFVFQRYHLLSHLTAVKNVEVPAIYAMADKILRNQRANALLCQLGLEKQLENKPAQLSGGQQQRVSIARALMNGGDIILADEPTGALDSQSSQDVLKILKDLNRKGHTVILITHDLAIAEHADRVICIQDGKIVSDTANALESMIKPQNKRTFIDDAVIEVCQQHNTEKLNRPNEKNNIDNDNKENNNGYNRNDNSFLNNPKKKLNSSILRSFNSYAESFFMAFNMMMAHK... | Function: Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Mu... |
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