entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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|---|---|---|---|---|
O27564
|
MTHK_METTH
|
Calcium-gated potassium channel MthK
|
MVLVIEIIRKHLPRVLKVPATRILLLVLAVIIYGTAGFHFIEGESWTVSLYWTFVTIATVGYGDYSPSTPLGMYFTVTLIVLGIGTFAVAVERLLEFLINREQMKLMGLIDVAKSRHVVICGWSESTLECLRELRGSEVFVLAEDENVRKKVLRSGANFVHGDPTRVSDLEKANVRGARAVIVDLESDSETIHCILGIRKIDESVRIIAEAERYENIEQLRMAGADQVISPFVISGRLMSRSIDDGYEAMFVQDVLAEESTRRMVEVPIPEGSKLEGVSVLDADIHDVTGVIIIGVGRGDELIIDPPRDYSFRAGDIILGIGKPEEIERLKNYISA
|
Calcium-gated potassium channel.
|
O28007
|
UDGA_ARCFU
|
Type-4 uracil-DNA glycosylase (EC 3.2.2.27) (AFUDG)
|
MESLDDIVREIMSCRKCDLHKTKTNYVPGVGNEKAEIVFVGEAPGRDEDLKGEPFVGAAGKLLTEMLASIGLRREDVYITNVLKCRPPNNRDPTPEEVEKCGDYLVRQLEAIRPNVIVCLGRFAAQFIFNLFDLEFTTISRVKGKVYEVERWGKKVKVIAIYHPAAVLYRPQLREEYESDFKKIGELCGKKQPTLFDYL
|
Removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP. Can remove uracil from double-stranded DNA containing either a U/G or U/A base pair as well as from single-stranded DNA.
|
O28025
|
TIAS_ARCFU
|
tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS (tRNA(Ile2)-agm2C synthetase) (EC 6.3.4.22) (tRNA(Ile2) agmatidine synthetase)
|
MRVWVGIDDTDSSRGMCTTYLAVLAMERVERELGKVIGFPRLIRLNPTIPYKTRGNGAVSFLVEVDDVGELVDVVNEVIIEHAMLDDEKTNPGAVFVDEELAVKLKPFADKAIKDVLQIDEALFVIGKYFIPHLRHKKGRGLIGALAAVGAELEDFTLELIAYRYPERFGTEREYDEESFFDMDYELYPQTFDNVDWCNDVVVCIPNTPCPVLYGIRGESVEALYKAMESVKTEPVDRRMIFVTNHATDMHLIGEEEVHRLENYRSYRLRGRVTLEPYDIEGGHVFFEIDTKFGSVKCAAFEPTKQFRNVIRLLRKGDVVEVYGSMKKDTINLEKIQIVELAEIWVEKNPICPSCGRRMESAGRGQGFRCKKCRTKADEKLREKVERELQPGFYEVPPSARRHLSKPLIRMNVEGRHIFR
|
ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA.
|
O28029
|
SYA_ARCFU
|
Alanine--tRNA ligase (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS)
|
MTLDEEYLDITFLTENGFVRKRCPKCGKHFWTADPEREICGDPPCESYSFIGNPVFKKPFELDEMREYYLNFFERRGHGRIERYPVVARWRTDIYLTIASIADFQPFVTSGVAPPPANPLTISQPCIRLDDLDSVGRTGRHLTLFEMMAHHAFNYPGKEIYWKNETVAYCTELLNELGVKKEDIVYKEEPWAGGGNAGPCLEAIVGGLEVATLVFMNLEEHPEGDIEIKGARYRKMDNYIVDTGYGLERFVWASKGTPTVYDAIFPEVVDTIIDNSNVSFNREDERVRRIVAESSKLAGIMGELRGERLNQLRKSVADTVGVSVEELEGIVVPLEKVYSLADHTRCILFMLGDGLVPSNAGAGYLARLMIRRSLRLAEELELGLDLYDLVEMHKKILGFEFDVPLSTVQEILELEKERYRTTVSKGTRLVERLVERKKKLEKDDLIELYDSHGIPVELAVGIAAEKGAEVEMPKDIYAELAKRHSKAEKVQEKKITLQNEYPATEKLYYDDPTLLEFEAEVIGVEGDFVILNRSAFYPESGGQDNDVGYLIANGGKFEVVDVLEADGVVLHVVKGAKPEVGTKVKGVIDSDVRWRHMRHHSATHVLLYSLQKVLGNHVWQAGARKEFSKARLDVTHFRRPSEEEIKEIEMLANREILANKPIKWEWMDRIEAERKFGFRLYQGGVPPGRKIRVVQVGDDVQACGGTHCRSTGEIGMLKILKVESIQDGVIRFEFAAGEAAIEAVEEMERLLREASSILRVEPAKLPKTVERFFEEWKDQRKEIERLKSVIADLWADILMERAEEFDSMKVVAEVVDADMQALQKLAERLAEKGAVGCLMAKGEGKVFVVTFSGQKYDARELLREIGRVAKGSGGGRKDVAQGAVQQLLDREEMLDVIFRFLSEHEG
|
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain.
|
O28126
|
CCA_ARCFU
|
CCA-adding enzyme (EC 2.7.7.72) (CCA tRNA nucleotidyltransferase) (tRNA CCA-pyrophosphorylase) (tRNA adenylyl-/cytidylyl- transferase) (tRNA nucleotidyltransferase) (tRNA-NT)
|
MKVEEILEKALELVIPDEEEVRKGREAEEELRRRLDELGVEYVFVGSYARNTWLKGSLEIDVFLLFPEEFSKEELRERGLEIGKAVLDSYEIRYAEHPYVHGVVKGVEVDVVPCYKLKEPKNIKSAVDRTPFHHKWLEGRIKGKENEVRLLKGFLKANGIYGAEYKVRGFSGYLCELLIVFYGSFLETVKNARRWTRRTVIDVAKGEVRKGEEFFVVDPVDEKRNVAANLSLDNLARFVHLCREFMEAPSLGFFKPKHPLEIEPERLRKIVEERGTAVFAVKFRKPDIVDDNLYPQLERASRKIFEFLERENFMPLRSAFKASEEFCYLLFECQIKEISRVFRRMGPQFEDERNVKKFLSRNRAFRPFIENGRWWAFEMRKFTTPEEGVRSYASTHWHTLGKNVGESIREYFEIISGEKLFKEPVTAELCEMMGVKD
|
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded. The structural flexibility of RNA controls the choice between CCA versus CCACCA addition: following the first CCA addition cycle, nucleotide-binding to the active site triggers a clockwise screw motion, producing torque on the RNA. This ejects stable RNAs, whereas unstable RNAs are refolded while bound to the enzyme and subjected to a second CCA catalytic cycle.
|
O28440
|
ASPD_ARCFU
|
L-aspartate dehydrogenase (L-aspDH) (EC 1.4.1.21)
|
MLVGLIGYGAIGKFLAEWLERNGFEIAAILDVRGEHEKMVRGIDEFLQREMDVAVEAASQQAVKDYAEKILKAGIDLIVLSTGAFADRDFLSRVREVCRKTGRRVYIASGAIGGLDAIFSASELIEEIVLTTRKNWRQFGRKGVIFEGSASEAAQKFPKNLNVAATLSIASGKDVKVRLVADEVEENIHEILVRGEFGEMEIRVRNRPMRENPKTSYLAALSVTRILRNLKEGLVV
|
Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. {ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000269|PubMed:16731057}.
|
O28597
|
NPD1_ARCFU
|
NAD-dependent protein deacylase 1 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 1) (SIR2-Af1)
|
MDEKLLKTIAESKYLVALTGAGVSAESGIPTFRGKDGLWNRYRPEELANPQAFAKDPEKVWKWYAWRMEKVFNAQPNKAHQAFAELERLGVLKCLITQNVDDLHERAGSRNVIHLHGSLRVVRCTSCNNSFEVESAPKIPPLPKCDKCGSLLRPGVVWFGEMLPPDVLDRAMREVERADVIIVAGTSAVVQPAASLPLIVKQRGGAIIEINPDETPLTPIADYSLRGKAGEVMDELVRHVRKALS
|
NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Deacetylates the N-terminal lysine residue of Alba, the major archaeal chromatin protein and that, in turn, increases Alba's DNA binding affinity, thereby repressing transcription. {ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:10841563}.
|
O28608
|
ALADH_ARCFU
|
Alanine dehydrogenase (AlaDH) (EC 1.4.1.1)
|
METLILTQEEVESLISMDEAMNAVEEAFRLYALGKAQMPPKVYLEFEKGDLRAMPAHLMGYAGLKWVNSHPGNPDKGLPTVMALMILNSPETGFPLAVMDATYTTSLRTGAAGGIAAKYLARKNSSVFGFIGCGTQAYFQLEALRRVFDIGEVKAYDVREKAAKKFVSYCEDRGISASVQPAEEASRCDVLVTTTPSRKPVVKAEWVEEGTHINAIGADGPGKQELDVEILKKAKIVVDDLEQAKHGGEINVAVSKGVIGVEDVHATIGEVIAGLKDGRESDEEITIFDSTGLAIQDVAVAKVVYENALSKNVGSKIKFFRI
|
Catalyzes the NAD(+)-dependent oxidative deamination of L-alanine to pyruvate, and the reverse reaction, the reductive amination of pyruvate. Its physiological role is not known. Cannot use NADP(+) instead of NAD(+) as a cosubstrate. In the deamination direction, can also efficiently use L-2-aminobutyrate as substrate. In the reductive amination direction, also exhibits high activity with 2-oxobutyrate and oxaloacetate as substrate. In contrast to bacterial homologs, does not exhibit any ornithine cyclodeaminase activity. {ECO:0000255|HAMAP-Rule:MF_00935, ECO:0000269|PubMed:15516582}.
|
O29238
|
RGYR_ARCFU
|
Reverse gyrase [Includes: Helicase (EC 3.6.4.12); Topoisomerase (EC 5.6.2.2)]
|
MIPVVYSNLCPVCGGDLESKEIEKHVCFRKKRSLCLFPEDFLLKEFVEFFRKCVGEPRAIQKMWAKRILRKESFAATAPTGVGKTSFGLAMSLFLALKGKRCYVIFPTSLLVIQAAETIRKYAEKAGVGTENLIGYYHGRIPKREKENFMQNLRNFKIVITTTQFLSKHYRELGHFDFIFVDDVDAILKASKNVDKLLHLLGFHYDLKTKSWVGEARGCLMVSTATAKKGKKAELFRQLLNFDIGSSRITVRNVEDVAVNDESISTLSSILEKLGTGGIIYARTGEEAEEIYESLKNKFRIGIVTATKKGDYEKFVEGEIDHLIGTAHYYGTLVRGLDLPERIRFAVFVGCPSFRVTIEDIDSLSPQMVKLLAYLYRNVDEIERLLPAVERHIDEVREILKKVMGKERPQAKDVVVREGEVIFPDLRTYIQGSGRTSRLFAGGLTKGASFLLEDDSELLSAFIERAKLYDIEFKSIDEVDFEKLSRELDESRDRYRRRQEFDLIKPALFIVESPTKARQISRFFGKPSVKVLDGAVVYEIPMQKYVLMVTASIGHVVDLITNRGFHGVLVNGRFVPVYASIKRCRDCGYQFTEDRESCPKCGSENVDNSRSRIEALRKLAHDAEFVIVGTDPDTEGEKIAWDLKNLLSGCGAVKRAEFHEVTRRAILEALESLRDVDENLVKAQVVRRIEDRWIGFVLSQKLWERFNNRNLSAGRAQTPVLGWIIDRFQESRERRKIAIVRDFDLVLEHDEEEFDLTIKLVEEREELRTPLPPYTTETMLSDANRILKFSVKQTMQIAQELFENGLITYHRTDSTRVSDVGQRIAKEYLGDDFVGREWGESGAHECIRPTRPLTRDDVQRLIQEGVLVVEGLRWEHFALYDLIFRRFMASQCRPFKVVVKKYSIEFDGKTAEEERIVRAEGRAYELYRAVWVKNELPTGTFRVKAEVKSVPKVLPFTQSEIIQMMKERGIGRPSTYATIVDRLFMRNYVVEKYGRMIPTKLGIDVFRFLVRRYAKFVSEDRTRDLESRMDAIERGELDYLKALEDLYAEIKSID
|
Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.
|
O29428
|
FERCR_ARCFU
|
Ferric-chelate reductase (NAD(P)H) (EC 1.16.1.10)
|
MDVEAFYKISYGLYIVTSESNGRKCGQIANTVFQLTSKPVQIAVCLNKENDTHNAVKESGAFGVSVLELETPMEFIGRFGFRKSSEFEKFDGVEYKTGKTGVPLVTQHAVAVIEAKVVKECDVGTHTLFVGEAVDAEVLKDAEVLTYADYHLMKKGKTPRTATVYFESK
|
Catalyzes the reduction of bound ferric iron (Fe(3+)) in a variety of iron chelators (siderophores) using NAD(P)H as the electron donor, resulting in the release of Fe(2+). Not active with uncomplexed Fe(3+). Also reduces FMN and FAD, but not riboflavin.
|
O29777
|
COPA_ARCFU
|
Probable copper-exporting P-type ATPase (EC 7.2.2.8) (Copper-exporting P-type ATPase A) (Cu(+)-exporting ATPase)
|
MVKDTYISSASKTPPMERTVRVTGMTCAMCVKSIETAVGSLEGVEEVRVNLATETAFIRFDEKRIDFETIKRVIEDLGYGVVDEQAAVSAEVEHLSRMKRKLYVAAFAGVLLLFLAHFISLPYEDFVQLLIALPAIFYSGSSIFKAAFSALRRRTLNMDVMYSMGVGAAFLASVLSTAGVLPREYSFYETSVLLLAFLLLGRTLEARAKSRTGEAIKKLVGLQAKTAVVIRDGKEIAVPVEEVAVGDIVIVRPGEKIPVDGVVVEGESYVDESMISGEPVPVLKSKGDEVFGATINNTGVLKIRATRVGGETLLAQIVKLVEDAMGSKPPIQRLADKVVAYFIPTVLLVAISAFIYWYFIAHAPLLFAFTTLIAVLVVACPCAFGLATPTALTVGMGKGAELGILIKNADALEVAEKVTAVIFDKTGTLTKGKPEVTDLVPLNGDERELLRLAAIAERRSEHPIAEAIVKKALEHGIELGEPEKVEVIAGEGVVADGILVGNKRLMEDFGVAVSNEVELALEKLEREAKTAVIVARNGRVEGIIAVSDTLKESAKPAVQELKRMGIKVGMITGDNWRSAEAISRELNLDLVIAEVLPHQKSEEVKKLQAKEVVAFVGDGINDAPALAQADLGIAVGSGSDVAVESGDIVLIRDDLRDVVAAIQLSRKTMSKIKQNIFWALIYNVILIPAAAGLLYPIFGVVFRPEFAGLAMAMSSVSVVANSLLLRNYVPPIRRGGDSVEKIVLELSGLSCHHCVARVKKALEEAGAKVEKVDLNEAVVAGNKEDVDKYIKAVEAAGYQAKLRS
|
Probably involved in copper and silver export.
|
O29867
|
AGLB3_ARCFU
|
Dolichyl-phosphooligosaccharide-protein glycotransferase 3 (EC 2.4.99.21) (Archaeal glycosylation protein B) (AglB-L) (AglB-Long) (Oligosaccharyl transferase) (OST) (OTase)
|
MQNAESWFKKYWHLSVLVIAALISVKLRILNPWNSVFTWTVRLGGNDPWYYYRLIENTIHNFPHRIWFDPFTYYPYGSYTHFGPFLVYLGSIAGIIFSATSGESLRAVLAFIPAIGGVLAILPVYLLTREVFDKRAAVIAAFLIAIVPGQFLQRSILGFNDHHIWEAFWQVSALGTFLLAYNRWKGHDLSHNLTARQMAYPVIAGITIGLYVLSWGAGFIIAPIILAFMFFAFVLAGFVNADRKNLSLVAVVTFAVSALIYLPFAFNYPGFSTIFYSPFQLLVLLGSAVIAAAFYQIEKWNDVGFFERVGLGRKGMPLAVIVLTALIMGLFFVISPDFARNLLSVVRVVQPKGGALTIAEVYPFFFTHNGEFTLTNAVLHFGALFFFGMAGILYSAYRFLKRRSFPEMALLIWAIAMFIALWGQNRFAYYFAAVSAVYSALALSVVFDKLHLYRALENAIGARNKLSYFRVAFALLIALAAIYPTYILADAQSSYAGGPNKQWYDALTWMRENTPDGEKYDEYYLQLYPTPQSNKEPFSYPFETYGVISWWDYGHWIEAVAHRMPIANPFQAGIGNKYNNVPGASSFFTAENESYAEFVAEKLNVKYVVSDIEMETGKYYAMAVWAEGDLPLAEKYYGGYFYYSPTGTFGYANSQWDIPLNSIIIPLRIPSELYYSTMEAKLHLFDGSGLSHYRMIYESDYPAEWKSYSSQVNLNNESQVLQTALYEAVMRARYGVSPTMGTQEVLYKYAYTQLYEKKMGIPVKIAPSGYVKIFERVKGAVVTGKVSANVTEVSVNATIKTNQNRTFEYWQTVEVKNGTYTVVLPYSHNSDYPVKPITPYHIKAGNVVKEITIYESQVQNGEIIQLDL
|
Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a glucose-linked heptasaccharide composed of 3 Glc, 2 Man, 2 Gal and a sulfate for A.fulgidus AglB-L) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.
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O29976
|
DIPPS_ARCFU
|
Bifunctional IPC transferase and DIPP synthase [Includes: 1L-myo-inositol-1-phosphate cytidylyltransferase (IPCT) (EC 2.7.7.74); CDP-L-myo-inositol myo-inositolphosphotransferase (DIPP synthase) (EC 2.7.8.34) (Di-myo-inositol-1,3'-phosphate-1'-phosphate synthase)]
|
MILPCESFNGVPSGCLIIEMNWYSVLKASTAIFFPEKYSSSTSSLSKRSPISAPMINVDGEYLKIFAGRIKLMKAVILAAGLGTRLGGVPKPLVRVGGCEIILRTMKLLSPHVSEFIIVASRYADDIDAFLKDKGFNYKIVRHDRPEKGNGYSLLVAKNHVEDRFILTMGDHVYSQQFIEKAVRGEGVIADREPRFVDIGEATKIRVEDGRVAKIGKDLREFDCVDTGFFVLDDSIFEHAEKLRDREEIPLSEIVKLARLPVTYVDGELWMDVDTKEDVRRANRALVSAAVKGSGDGFISRKINRKISTRISAAIVNKVNPNQMTLISFLVGAFSALASFFSIPLAGLLYQFSSILDGCDGEIARASLKMSKKGGYVDSILDRFVDFLFLAIIALLYPKTATVAMFAIFGSVMVSYTSEKYKAEFGESIFGKFRVLNYIPGKRDERIFLIMIFCLLSAISLQWIFWMFLFVAAISLTRVVVTLLAVLVSK
|
Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate. The cytidylyltransferase is absolutely specific for CTP and L-myo-inositol-1-P. The DIPP synthase uses only L-myoinositol-1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-L-myo-inositol and CDP-D-myoinositol, are recognized as alcohol donors.
|
O30085
|
COPB_ARCFU
|
Copper-exporting P-type ATPase B (EC 7.2.2.9)
|
MHEHDSHGEAAHSNSEDMQMIHQHHEHHGHEEEHSAHHEKMKHSADHGDHHRMMMEDFKKRFYVSTLLTIPILILSPAIQTFLGFRVEFAGSLYILFLLSSAVYFYGGYPFLKGIFDELRRRQPGMMTLIAVAISVAYFYSSAVVFGLKGKFFFWELATLIDIMLLGHYIEMRSVLGASRALEELVKIMPSEAHLLKDGEIVEVKVENLKPGDKVLVKPGEKIPVDGIVVEGESFVNEAMLTGESKPVAKKPGDTVIGGAINGEGSLVVEVEKTGKDTYLNQVIELVRQAQESKSRTQDLANRAALLLTVIALTVGSVTLAIWLAYIADFAFAIERAVTVMVITCPHALGLAIPLVVAVSTSLAAKSGLLIRDRQAFERAKDLQAVIFDKTGTLTEGRFGVTDIVGFNHSEDELLQIAASLEARSEHPIAAAIVEEAEKRGFGLTEVEEFRAIPGKGVEGIVNGRRYMVVSPGYIRELGIKTDESVEKLKQQGKTVVFILKNGEVSGVIALADRIRPESREAISKLKAIGIKCMMLTGDNRFVAKWVAEELGLDDYFAEVLPHEKAEKVKEVQQKYVTAMVGDGVNDAPALAQADVGIAIGAGTDVAVETADIVLVRNDPRDVAAIVELSRKTYSKMKQNLLWATGYNAFAIPLAAGVLYSAGILLSPAVGAILMSLSTVIVAINARLLR
|
Involved in copper export.
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O30298
|
BSUHB_ARCFU
|
Fructose-1,6-bisphosphatase/inositol-1-monophosphatase (FBPase/IMPase) (EC 3.1.3.11) (EC 3.1.3.25) (Inositol-1-phosphatase) (I-1-Pase)
|
MDERDALRISREIAGEVRKAIASMPLRERVKDVGMGKDGTPTKAADRVAEDAALEILRKERVTVVTEESGVLGEGDVFVALDPLDGTFNATRGIPVYSVSLCFSYSDKLKDAFFGYVYNLATGDEYYADSSGAYRNGERIEVSDAEELYCNAIIYYPDRKFPFKRMRIFGSAATELCFFADGSFDCFLDIRPGKMLRIYDAAAGVFIAEKAGGKVTELDGESLGNKKFDMQERLNIVAANEKLHPKLLELIK
|
Phosphatase with broad specificity it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate and fructose-6-phosphate. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.
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O30508
|
ARUC_PSEAE
|
Succinylornithine transaminase/acetylornithine aminotransferase (ACOAT) (SOAT) (Succinylornithine aminotransferase) (EC 2.6.1.11) (EC 2.6.1.81)
|
MSAPHAQVERADFDRYMVPNYAPAAFIPVRGEGSRVWDQSGRELIDFAGGIAVTSLGHAHPALVKALTEQAQRIWHVSNVFTNEPALRLARKLVDATFAERVFLANSGAEANEAAFKLARRYANDVYGPQKYEIIAASNSFHGRTLFTVNVGGQPKYSDGFGPKFEGITHVPYNDLEALKAAISDKTCAVVLEPIQGEGGVLPAQQAYLEGARKLCDEHNALLVFDEVQSGMGRVGELFAYMHYGVVPDILSSAKSLGGGFPIGAMLTTGEIAKHLSVGTHGTTYGGNPLASAVAEAALDVINTPEVLDGVKAKHERFKSRLQKIGQEYGIFDEIRGMGLLIGAALTDEWKGKARDVLNAAEKEAVMVLQASPDVVRFAPSLVIDDAEIDEGLERFERAVAKLVRG
|
Transaminates both N(2)-acetylornithine and N(2)-succinylornithine.
|
O30511
|
FUCT_HELPX
|
Alpha-(1,3)-fucosyltransferase FucT (EC 2.4.1.152) (4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase)
|
MFQPLLDAYVESASIEKMASKSPPPLKIAVANWWGDEEIKEFKNSVLYFILSQRYTITLHQNPNEFSDLVFGNPLGSARKILSYQNAKRVFYTGENESPNFNLFDYAIGFDELDFNDRYLRMPLYYDRLHHKAESVNDTTAPYKLKDNSLYALKKPSHCFKEKHPNLCAVVNDESDPLKRGFASFVASNPNAPIRNAFYDALNSIEPVTGGGSVRNTLGYNVKNKNEFLSQYKFNLCFENTQGYGYVTEKIIDAYFSHTIPIYWGSPSVAKDFNPKSFVNVHDFKNFDEAIDYIKYLHTHKNAYLDMLYENPLNTLDGKAYFYQNLSFKKILAFFKTILENDTIYHDNPFIFCRDLNEPLVTIDDLRVNYDDLRVNYDDLRINYDDLRVNYDDLRINYDDLRVNYDDLRVNYDDLRINYDDLRVNYDDLRVNYERLLSKATPLLELSQNTTSKIYRKAYQKSLPLLRAIRRWVKKLGL
|
Involved in the biosynthesis of the Lewis X (LeX) trisaccharide of the lipopolysaccharide (LPS) O-antigen. Catalyzes the addition of fucose in alpha 1-3 linkage to Gal-beta-1-4-GlcNAc-beta-O-R (LacNAc-R) type II acceptor.
|
O30640
|
MTBA_METBA
|
Methylcobamide:CoM methyltransferase MtbA (EC 2.1.1.247) (MT2-A) (Methylcobamide:CoM methyltransferase II isozyme A) ([Methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M)
|
MAEYTPKERLYRALRKQQVDRMPAVCFTQTATVEQMEACGAYWPEAHSDAEKMATLAEAAHTVVGFEAVRVPFDITAEAEFFGCGIKAGDLKQQPSVIKPSVKNLEDLEKLKNYNLKEGRIAVVLEAVKILSEKYGKELPIIGSMIGPFSLAQHINGDAWFGNLFTGEEVVPALLDFCSDFNVAYAKAMVENGADTIAIIDPTASYELIGGEFYEKYALPYQKKIVDAMKELDVATVLHICGNTTNGLGIMDKTGVNGISVDQKVDIKTATGSVKNAIIVGNLDPVAVLWNGTPEEIAEASKKALDAGVGLLTVGCGTVSMTPTVNLQKMIECAKSHTY
|
Methyltransferase involved in methanogenesis from methylamines methanol pathway. Catalyzes the transfer of the methyl group from the methylated corrinoid protein MtmC (MtmC1 or MtmC2) or MtbC to coenzyme M, forming the substrate for coenzyme-B sulfoethylthiotransferase.
|
O30916
|
SOPB_SALTY
|
Inositol phosphate phosphatase SopB (EC 3.1.3.-) (Effector protein SopB)
|
MQIQSFYHSASLKTQEAFKSLQKTLYNGMQILSGQGKAPAKAPDARPEIIVLREPGATWGNYLQHQKASNHSLHNLYNLQRDLLTVAATVLGKQDPVLTSMANQMELAKVKADRPATKQEEAAAKALKKNLIELIAARTQQQDGLPAKEAHRFAAVAFRDAQVKQLNNQPWQTIKNTLTHNGHHYTNTQLPAAEMKIGAKDIFPSAYEGKGVCSWDTKNIHHANNLWMSTVSVHEDGKDKTLFCGIRHGVLSPYHEKDPLLRHVGAENKAKEVLTAALFSKPELLNKALAGEAVSLKLVSVGLLTASNIFGKEGTMVEDQMRAWQSLTQPGKMIHLKIRNKDGDLQTVKIKPDVAAFNVGVNELALKLGFGLKASDSYNAEALHQLLGNDLRPEARPGGWVGEWLAQYPDNYEVVNTLARQIKDIWKNNQHHKDGGEPYKLAQRLAMLAHEIDAVPAWNCKSGKDRTGMMDSEIKREIISLHQTHMLSAPGSLPDSGGQKIFQKVLLNSGNLEIQKQNTGGAGNKVMKNLSPEVLNLSYQKRVGDENIWQSVKGISSLITS
|
Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicles, which are essential to create a favorable environment where Salmonella can replicate and avoid immune defenses of the host cell.
|
O31041
|
PDUD_SALTY
|
Propanediol dehydratase medium subunit (EC 4.2.1.28) (Diol dehydratase medium subunit) (DDH medium subunit) (Propanediol utilization protein PduD)
|
MEINEKLLRQIIEDVLRDMKGSDKPVSFNAPAASTAPQTAAPAGDGFLTEVGEARQGTQQDEVIIAVGPAFGLAQTVNIVGLPHKSILREVIAGIEEEGIKARVIRCFKSSDVAFVAVEGNRLSGSGISIGIQSKGTTVIHQQGLPPLSNLELFPQAPLLTLETYRQIGKNAARYAKRESPQPVPTLNDQMARPKYQAKSAILHIKETKYVVTGKNPQELRVAL
|
Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol (1,2-PD) to propionaldehyde. Required for S.typhimurium growth on 1,2-PD as the sole carbon and energy source (Probable). This subunit is directly targeted to the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation, and is also responsible for targeting the other 2 subunits (pduC and pduE). The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.
|
O31042
|
PDUE_SALTY
|
Propanediol dehydratase small subunit (EC 4.2.1.28) (Diol dehydratase small subunit) (DDH small subunit) (Propanediol utilization protein PduE)
|
MNTDAIESMVRDVLSRMNSLQGDAPAAAPAAGGTSRSAKVSDYPLANKHPEWVKTATNKTLDDFTLENVLSNKVTAQDMRITPETLRLQASIAKDAGRDRLAMNFERAAELTAVPDDRILEIYNALRPYRSTKEELLAIADDLENRYQAKICAAFVREAAGLYVERKKLKGDD
|
Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol (1,2-PD) to propionaldehyde. Required for S.typhimurium growth on 1,2-PD as the sole carbon and energy source. Localized in the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation. The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.
|
O31147
|
LON_MYCSM
|
Lon protease (EC 3.4.21.53) (ATP-dependent protease La)
|
MAEAKTVPVLFLNDSIVLPGMVVPIELDDAARAAVDAARASESGELLIAPRLEDRYPAYGVLASIVQIGRLPNGDAAAVVRGERRAHIGSGTSGPGAALWVQVEEVTDPEPTDETKKLAGEYKKLLLAMLQRRDAWQIVDMVNKITDPSALADTAGYASYLTGTQKRELLETTDVDRRLSLLIGWTGDHLAETEVNDKIAEDVRTGMEKQQKEFLLRQQLAAIRKELGELDDNGDGSSDDYRARIEQADLPEKVREAALREVGKLERASDQSPEGGWIRTWLDTVLDLPWNVRTEDSTDLARAREILDTDHHGLSDVKDRIVEYLAVRGAAPQRGMAVVGGRGSGAVMVLAGPPGVGKTSLGESVARALDRKFVRVALGGVRDEAEIRGHRRTYVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRDHYLDLDLDLSDVVFLVTANVIENIPSALLDRMELVEIDGYTADDKLAIAQGFLLPRQRERGGLTSDEVTVTEAALRKIAADYTREPGVRQFERLLAKAMRKAATKLADHPQAAPITIDEPDLVEYLGRPRFLPESAERTAVPGVATGLAVTGLGGDVLYIEANSTEGEPGLQLTGQLGDVMKESAQIAMSYVRAHAKQLGVDPEALNRRIHIHVPAGAVPKDGPSAGVTMVTALVSMATGRKVRGDVGMTGEVTLNGRVLPIGGVKQKLLAAQRAGLSTVFIPQRNQPDLDDVPADVLDALDVRPMTDVADIIAAALEPAHEASTAAAA
|
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 small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. {ECO:0000255|HAMAP-Rule:MF_01973, ECO:0000269|PubMed:9425059}.
|
O31156
|
PHNX_BACCE
|
Phosphonoacetaldehyde hydrolase (Phosphonatase) (EC 3.11.1.1) (Phosphonoacetaldehyde phosphonohydrolase)
|
MKIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVAITAEEARKPMGLLKIDHVRALTEMPRIASEWNRVFRQLPTEADIQEMYEEFEEILFAILPRYASPINGVKEVIASLRERGIKIGSTTGYTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYPWMCYKNAMELGVYPMNHMIKVGDTVSDMKEGRNAGMWTVGVILGSSELGLTEEEVENMDSVELREKIEVVRNRFVENGAHFTIETMQELESVMEHIEKQELIIS
|
Involved in phosphonate degradation.
|
O31266
|
HOD_PAENT
|
1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (EC 1.13.11.48)
|
MTDTYLHETLVFDNKLSYIDNQRDTDGPAILLLPGWCHDHRVYKYLIQELDADFRVIVPNWRGHGLSPCEVPDFGYQEQVKDALEILDQLGVETFLPVSHSHGGWVLVELLEQAGPERAPRGIIMDWLMWAPKPDFAKSLTLLKDPERWREGTHGLFDVWLDGHDEKRVRHHLLEEMADYGYDCWGRSGRVIEDAYGRNGSPMQMMANLTKTRPIRHIFSQPTEPEYEKINSDFAEQHPWFSYAKLGGPTHFPAIDVPDRAAVHIREFATAIRQGQ
|
Ring-cleaving dioxygenase involved in quinaldine degradation and utilization.
|
O31269
|
ISCS_AZOVI
|
Cysteine desulfurase IscS (EC 2.8.1.7)
|
MKLPIYLDYSATTPVDPRVAQKMCECLTMEGNFGNPASRSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDNLAIKGVAHFNASKGKHIITSKIEHKAVLDTTRQLEREGFEVTYLEPGEDGLITPAMVAAALREDTILVSVMHVNNEIGTVNDIAAIGELTRSRGVLYHVDAAQSTGKVAIDLERMKVDLMSFSAHKTYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGTLATHQIVGMGEAFRIAREEMAAESRRIAGLSHRFHEQVSTLEEVYLNGSATARVPHNLNLSFNYVEGESLIMSLRDLAVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEVDYAARKVCEAVGKLRELSPLWDMYKDGVDLSKIEWQAH
|
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine via an enzyme-bound persulfide intermediate. Functions as a sulfur delivery protein for Fe-S cluster synthesis. Cluster assembly on IscU homodimers proceeds sequentially from 1 2Fe-2S per dimer, to 2 2Fe-2S per dimer and finally 1 4Fe-4S per dimer.
|
O31422
|
SKFA_BACSU
|
Sporulation killing factor (SKF) (Sporulation-killing factor SkfA)
|
MKRNQKEWESVSKKGLMKPGGTSIVKAAGCMGCWASKSIAMTRVCALPHPAMRAI
|
Produces a 26-residue extracellular sporulation filling factor (SKF) that induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, providing a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation. Can also inhibit growth of other bacteria at high concentrations. Addition of SKF to solid cultures induces killing, but it is much less effective than SDP (AC O34344). Has a role in protecting the secreted lipase LipA against proteolysis, either by modulating its folding or by acting as a protease inhibitor.
|
O31461
|
ILVE1_BACSU
|
Branched-chain-amino-acid transaminase 1 (BCAT 1) (EC 2.6.1.42)
|
MNKLIEREKTVYYKEKPDPSSLGFGQYFTDYMFVMDYEEGIGWHHPRIAPYAPLTLDPSSSVFHYGQAVFEGLKAYRTDDGRVLLFRPDQNIKRLNRSCERMSMPPLDEELVLEALTQLVELEKDWVPKEKGTSLYIRPFVIATEPSLGVKASRSYTFMIVLSPVGSYYGDDQLKPVRIYVEDEYVRAVNGGVGFAKTAGNYAASLQAQRKANELGYDQVLWLDAIEKKYVEEVGSMNIFFVINGEAVTPALSGSILSGVTRASAIELIRSWGIPVREERISIDEVYAASARGELTEVFGTGTAAVVTPVGELNIHGKTVIVGDGQIGDLSKKLYETITDIQLGKVKGPFNWTVEV
|
Transaminates branched-chain amino acids and ketoglutarate. Involved in the final step of the methionine regeneration pathway, where ketomethiobutyrate (KMTB) is converted to methionine via a transamination. The amino donor preference is isoleucine, leucine, valine, phenylalanine, and tyrosine.
|
O31523
|
RHGT1_BACSU
|
Rhamnogalacturonan acetylesterase RhgT (RGAE) (EC 3.1.1.-)
|
MMKKPIQVFLAGDSTVSDCPPHEAPMAGWGQVFGQLFSEGVLVRNHAKGGASTNSFVEEGRLQAIAEHITQGDYLLIQFGHNDQKPRGTKPYSTFQQFLTLFADTAREKGAHPVFVTSVQRRRFDENGRIEHTLGEYPDAMKALAKELDVPVIDLLAKTKVLYEAYGPEESKRLFVWFQPNEHPNYPDGIEDNTHFSEKGAMEVAKLVAEGIEELGLPLKDHLVSREGKEHV
|
May play a role in the degradation of type I rhamnogalacturonan derived from plant cell walls. This enzyme has a broad substrate specificity, and shows strong preference for glucose pentaacetate, beta-naphthylacetate, and p-nitrophenyl acetate (pNPA). Also active toward acetylated xylan.
|
O31526
|
YESW_BACSU
|
Rhamnogalacturonan endolyase YesW (EC 4.2.2.23)
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MRRSCLMIRRRKRMFTAVTLLVLLVMGTSVCPVKAEGAARQMEALNRGLVAVKTDGGIFVSWRFLGTENASVLFNVYRDGQKLNAAPVKTTNYVDKNGSAGSTYTVRAVVNGTEQPASEKASVWAQPYHSVPLDKPAGGTTPKGESYTYSANDASVGDVDGDGQYELILKWDPSNSKDNSQDGYTGDVLIDAYKLDGTKLWRINLGKNIRAGAHYTQFMVYDLDGDGKAEVAMKTADGTKDGTGKVIGNANADYRNEQGRVLSGPEYLTVFQGSTGKELVTANFEPARGNVSDWGDSYGNRVDRFLAGIAYLDGQRPSLIMTRGYYAKTMLVAYNFRDGKLSKLWTLDSSKSGNEAFAGQGNHNLSIADVDGDGKDEIIFGSMAVDHDGKGMYSTGLGHGDALHTGDLDPGRPGLEVFQVHEDKNAKYGLSFRDAATGKILWGVYAGKDVGRGMAADIDPRYPGQEVWANGSLYSAKGVKIGSGVPSSTNFGIWWDGDLLREQLDSNRIDKWDYQNGVSKNMLTASGAAANNGTKATPTLQADLLGDWREEVVWRTEDSSALRIYTTTIPTEHRLYTLMHDPVYRLGIAWQNIAYNQPPHTSFFLGDGMAEQPKPNMYTP
|
Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases oligosaccharide products. Degrades rhamnogalacturonan, polygalacturonic acid, pectic acid and pectin.
|
O31527
|
YESX_BACSU
|
Rhamnogalacturonan exolyase YesX (EC 4.2.2.24)
|
MKPKKRQMEYLTRGLIAVQTEQGVFVSWRFLGTDHETTAFHLYRDGKRITRDPIAESTNFLDQNGTADSVYQVAAVNKGREEKLSKKARVWQENVLEVPLAKPEGGVTPDGKPYTYSANDASVGDIDGDGEYEMILKWDPSNSKDNAHDGYTGEVLIDAYKLDGTFLWRINLGRNIRAGAHYTQFMVYDLDGDGKAEIAMKTADGTTDGKGHIIGDEQADFRNEQGRILSGPEYLTVFKGETGEALTTVEYEPPRGKLEDWGDGYGNRMDRFLAGTAYLDGERPSLVMARGYYTRTVLVAYDFRNGRLKKRWVFDSNQPGHEAYAGQGNHSLSVADVDGDGKDEIIYGAMAVDHDGTGLYSTGLGHGDAMHVGDLDPSRKGLEVFQVHEDATKPYGLSLRDAGTGEILWGVHAGTDVGRGMAAHIDPSYKGSLVWGIDPPGNDGMSYGLFTSKGEKISDKAPSSANFAIWWDGDLVRELLDHDWDGTIGRPKIEKWDAENGCLKTIFQPAGVLSNNGTKGNPVLQANLFGDWREEVIWRTEDSSALRIYTTTHLTRHCFYTLMHDPVYRLGIAWQNTAYNQPPHTSFYLGTGMKKPPKPALYIAGSKAEAPL
|
Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases disaccharide products. Degrades rhamnogalacturonan, polygalacturonic acid and pectic acid. Has very low activity on pectin.
|
O31602
|
SPX_BACSU
|
Global transcriptional regulator Spx (Redox-responsive transcription factor Spx) (Suppressor of clpP and clpX) (Spx)
|
MVTLYTSPSCTSCRKARAWLEEHEIPFVERNIFSEPLSIDEIKQILRMTEDGTDEIISTRSKVFQKLNVNVESMPLQDLYRLINEHPGLLRRPIIIDEKRLQVGYNEDEIRRFLPRKVRSFQLREAQRLAN
|
Global transcriptional regulator that plays a key role in stress response and exerts either positive or negative regulation of genes. Acts by interacting with the C-terminal domain of the alpha subunit of the RNA polymerase (RNAP). This interaction can enhance binding of RNAP to the promoter region of target genes and stimulate their transcription, or block interaction of RNAP with activator proteins and repress transcription. Exhibits no DNA-binding activity. Induces the expression of a large number of genes in response to a variety of stress conditions, such as disulfide, heat and cell wall stress, while concurrently repressing transcription of genes involved in various developmental and growth-related pathways during periods of extreme stress. Functions in the oxidative stress response via induction of the transcription of thioredoxin (trxA) and thioredoxin reductase (trxB) during thiol-specific oxidative (disulfide) stress. Mediates response to oxidative stress caused by paraquat (PQ) via induction of the methionine sulfoxide reductase genes, msrA and msrB. Also acts as a transcriptional activator of the bacillithiol (BSH) biosynthesis genes in response to oxidizing conditions and thio-reactive compounds. Involved in heat stress response and thermotolerance development, which results in diminished cellular protein aggregates. Plays an important adaptive role in the cell wall stress response. Participates in sulfate-dependent control of organosulfur metabolism. Negatively controls, via CymR, the expression of the organosulfur utilization operons ytmI, yxeI and ssu, and directly activates yrrT operon expression during growth in medium containing methionine as sole sulfur source. Negatively affects competence and sporulation. Inhibits biofilm formation in response to disulfide stress by repressing biofilm matrix genes.
|
O31611
|
YJBM_BACSU
|
GTP pyrophosphokinase YjbM (EC 2.7.6.5) ((p)ppGpp synthase YjbM) (Small alarmone synthase 1) (SAS 1)
|
MDDKQWERFLVPYRQAVEELKVKLKGIRTLYEYEDDHSPIEFVTGRVKPVASILEKARRKSIPLHEIETMQDIAGLRIMCQFVDDIQIVKEMLFARKDFTVVDQRDYIAEHKESGYRSYHLVVLYPLQTVSGEKHVLVEIQIRTLAMNFWATIEHSLNYKYSGNIPEKVKLRLQRASEAASRLDEEMSEIRGEVQEAQAAFSRKKKGSEQQ
|
Functions as a (p)ppGpp synthase GDP can be used instead of GTP, resulting in an increase of (p)ppGpp synthesis. The enzyme binds ATP, then GDP or GTP and catalysis is highly cooperative. In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. Probably has a minor role in the stringent response.
|
O31612
|
NADK1_BACSU
|
NAD kinase 1 (EC 2.7.1.23) (ATP-dependent NAD kinase) (Poly(P)-dependent NAD kinase) (PPNK)
|
MKFAVSSKGDQVSDTLKSKIQAYLLDFDMELDENEPEIVISVGGDGTLLYAFHRYSDRLDKTAFVGVHTGHLGFYADWVPHEIEKLVLAIAKTPYHTVEYPLLEVIVTYHENEREERYLALNECTIKSIEGSLVADVEIKGQLFETFRGDGLCLSTPSGSTAYNKALGGAIIHPSIRAIQLAEMASINNRVFRTVGSPLLLPSHHDCMIKPRNEVDFQVTIDHLTLLHKDVKSIRCQVASEKVRFARFRPFPFWKRVQDSFIGKGE
|
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (GTP, UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus. {ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:12897004}.
|
O31616
|
GLYOX_BACSU
|
Glycine oxidase (GO) (EC 1.4.3.19)
|
MKRHYEAVVIGGGIIGSAIAYYLAKENKNTALFESGTMGGRTTSAAAGMLGAHAECEERDAFFDFAMHSQRLYKGLGEELYALSGVDIRQHNGGMFKLAFSEEDVLQLRQMDDLDSVSWYSKEEVLEKEPYASGDIFGASFIQDDVHVEPYFVCKAYVKAAKMLGAEIFEHTPVLHVERDGEALFIKTPSGDVWANHVVVASGVWSGMFFKQLGLNNAFLPVKGECLSVWNDDIPLTKTLYHDHCYIVPRKSGRLVVGATMKPGDWSETPDLGGLESVMKKAKTMLPAIQNMKVDRFWAGLRPGTKDGKPYIGRHPEDSRILFAAGHFRNGILLAPATGALISDLIMNKEVNQDWLHAFRIDRKEAVQI
|
Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N-methylglycine), N-ethylglycine and glycine. Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine). Displays lower activities on D-alanine, D-valine, D-proline and D-methionine. Does not act on L-amino acids and other D-amino acids. Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine intermediate (dehydroglycine) required for the biosynthesis of the thiazole ring of thiamine pyrophosphate.
|
O31644
|
MANR_BACSU
|
Transcriptional regulator ManR (Mannose operon transcriptional activator) [Includes: Putative phosphotransferase enzyme IIB component (EC 2.7.1.191) (Putative PTS system EIIB component); Putative phosphotransferase enzyme IIA component (Putative PTS system EIIA component)]
|
MEYINTRQKEILYLLLSEPDDYLVVQDFADRVQCSEKTIRNDLKVIEDYLNEHSHAQLIRKPGLGVYLHIEEQERTWLSQQLHTEHFSSRQRSDKERMLHIAYDLLMNPKPVSAKDIAARHFVNRSSIKKDLYAVEEWLKRFDLTLVSRQRLGLKVEGNERNKRKALARISDLIHNTAFTSQFIKSKFLHYEVDFVTKEIKSLQKKHSLYFTDETFESLLLHTLLMVRRIKMKQPISLSPKEMAAVKKKKEYQWTFACLQRLEPVFAIRFPEEEAVYLTLHILGGKVRYPLQTEENLENAVLPKVVGHLINRVSELKMMDFHKDQDLINGLNIHLNTVLQRLSYDLSVANPMLNDIKKMYPYLFHLIIDVLEDINQTFDLHIPEEEAAYLTLHFQAAIERMQGSSETHKKAVIVCHMGIGMSQLLRTKIERKYHQIAVMACIAKADLKDYIKKHEDIDLVISTIALENITVPHIVVSPLLEPGEEKKLSAFIRQLGESHRQKQKTFQMLNNTTPFLVFLQQEAEHRYKLIEQLATALFEKGYVDKDYAVHAVMREKMSATNIGSGIAIPHANAKFIKQSAIAIATLKEPLEWGNEKVSLVFMLAVKHEDQTMTKQLFSELSYLSEQPAFVQKLTKETNVMTFLSHLDY
|
Positively regulates the expression of the mannose operon that consists of three genes, manP, manA, and yjdF, which are responsible for the transport and utilization of mannose. Also activates its own expression.
|
O31645
|
PTN3B_BACSU
|
PTS system mannose-specific EIIBCA component (EIIBCA-Man) (EII-Man) [Includes: Mannose-specific phosphotransferase enzyme IIB component (EC 2.7.1.191) (PTS system mannose-specific EIIB component); Mannose permease IIC component (PTS system mannose-specific EIIC component); Mannose-specific phosphotransferase enzyme IIA component (PTS system mannose-specific EIIA component)]
|
MKLLAITSCPNGIAHTYMAAENLQKAADRLGVSIKVETQGGIGVENKLTEEEIREADAIIIAADRSVNKDRFIGKKLLSVGVQDGIRKPEELIQKALNGDIPVYRSATKSESGNHQEKKQNPIYRHLMNGVSFMVPFIVVGGLLIAVALTLGGEKTPKGLVIPDDSFWKTIEQIGSASFSFMIPILAGYIAYSIADKPGLVPGMIGGYIAATGSFYDSASGAGFLGGIIAGFLAGYAALWIKKLKVPKAIQPIMPIIIIPVFASLIVGLAFVFLIGAPVAQIFASLTVWLAGMKGSSSILLALILGAMISFDMGGPVNKVAFLFGSAMIGEGNYEIMGPIAVAICIPPIGLGIATFLGKRKFEASQREMGKAAFTMGLFGITEGAIPFAAQDPLRVIPSIMAGSMTGSVIAMIGNVGDRVAHGGPIVAVLGAVDHVLMFFIAVIAGSLVTALFVNVLKKDITASPVLSETAPTSAPSEAAAANEIKQPIQSQKAEMSEFKKLTDIISPELIEPNLSGETSDDIIDELIQKLSRRGALLSESGFKQAILNREQQGTTAIGMNIAIPHGKSEAVREPSVAFGIKRSGVDWNSLDGSEAKLIFMIAVPKESGGNQHLKILQMLSRKLMDDNYRERLLSVQTTEEAYKLLEEIE
|
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in mannose transport.
|
O31662
|
MTNA_BACSU
|
Methylthioribose-1-phosphate isomerase (M1Pi) (MTR-1-P isomerase) (EC 5.3.1.23) (S-methyl-5-thioribose-1-phosphate isomerase)
|
MTHSFAVPRSVEWKETAITILNQQKLPDETEYLELTTKEDVFDAIVTLKVRGAPAIGITAAFGLALAAKDIETDNVTEFRRRLEDIKQYLNSSRPTAINLSWALERLSHSVENAISVNEAKTNLVHEAIQIQVEDEETCRLIGQNALQLFKKGDRIMTICNAGSIATSRYGTALAPFYLAKQKDLGLHIYACETRPVLQGSRLTAWELMQGGIDVTLITDSMAAHTMKEKQISAVIVGADRIAKNGDTANKIGTYGLAILANAFDIPFFVAAPLSTFDTKVKCGADIPIEERDPEEVRQISGVRTAPSNVPVFNPAFDITPHDLISGIITEKGIMTGNYEEEIEQLFKGEKVH
|
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). {ECO:0000255|HAMAP-Rule:MF_01678, ECO:0000269|PubMed:14551435}.
|
O31677
|
QUEE_BACSU
|
7-carboxy-7-deazaguanine synthase (CDG synthase) (EC 4.3.99.3) (Queuosine biosynthesis protein QueE)
|
MAKGIPVLEIFGPTIQGEGMVIGQKTMFVRTAGCDYSCSWCDSAFTWDGSAKKDIRWMTAEEIFAELKDIGGDAFSHVTISGGNPALLKQLDAFIELLKENNIRAALETQGTVYQDWFTLIDDLTISPKPPSSKMVTNFQKLDHILTSLQENDRQHAVSLKVVIFNDEDLEFAKTVHKRYPGIPFYLQVGNDDVHTTDDQSLIAHLLGKYEALVDKVAVDAELNLVRVLPQLHTLLWGNKRGV
|
Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:14660578, ECO:0000269|PubMed:19354300, ECO:0000269|PubMed:23194065}.
|
O31678
|
QUEF_BACSU
|
NADPH-dependent 7-cyano-7-deazaguanine reductase (EC 1.7.1.13) (7-cyano-7-carbaguanine reductase) (NADPH-dependent nitrile oxidoreductase) (PreQ(0) reductase)
|
MTTRKESELEGVTLLGNQGTNYLFEYAPDVLESFPNKHVNRDYFVKFNCPEFTSLCPKTGQPDFATIYISYIPDEKMVESKSLKLYLFSFRNHGDFHEDCMNIIMNDLIELMDPRYIEVWGKFTPRGGISIDPYTNYGKPGTKYEKMAEYRMMNHDLYPETIDNR
|
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1), a late step in the queuosine pathway.
|
O31691
|
GLCT_BACSU
|
PtsGHI operon antiterminator (RNA-binding antitermination protein GlcT)
|
MNGSFTVKKVLNNNVLIASHHKYSEVVLIGKGIGFGKKQDDVIEDKGYDKMFILKDEKEQKQFKKLLDYVDEKLVDISNDVIYHISNRTNHSLNEHIHIALTDHIAFAIKRQQQGFDMKNPFLMETQSLYPEEYQIAKEVIDMINEKAGLCLPEGEIGFIALHIHSALTNRPLSEVNQHSQLMAQLVEVIEDSFQMKVNKESVNYLRLIRHIRFTIERIKKEEPTKEPEKLMLLLKNEYPLCYNTAWKLIKILQQTLKKPVHEAEAVYLTLHLYRLTNKIS
|
Mediates the positive regulation of the glucose PTS operon (ptsGHI) by functioning as an antiterminator factor of transcription via its interaction with the RNA-antiterminator (RAT) sequence located upstream of the ptsG gene. The RNA-binding domain of GlcT directly binds to the RNA antiterminator (RAT) sequence and prevents transcriptional termination. GlcT binding requires two identical and nearly symmetrical triple base pairings in the RAT sequence.
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O31718
|
RPOY_BACSU
|
DNA-directed RNA polymerase subunit epsilon (RNAP epsilon subunit) (EC 2.7.7.6) (DNA-directed RNA polymerase subunit omega 1) (RNA polymerase epsilon subunit) (RNA polymerase omega 1 subunit) (Transcriptase subunit epsilon) (Transcriptase subunit omega 1)
|
MIYKVFYQEKADEVPVREKTDSLYIEGVSERDVRTKLKEKKFNIEFITPVDGAFLEYEQQSENFKVLEL
|
A non-essential component of RNA polymerase (RNAP). Has a similar structure to bacteriophage T7 protein Gp2 (AC P03704), which is known to bind to RNAP in the DNA binding-cleft. Unlike Gp2 however, this protein does not inhibit transcription initiation. In vitro reconstitution experiments show this subunit is dispensible.
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O31749
|
PYRH_BACSU
|
Uridylate kinase (UK) (EC 2.7.4.22) (Uridine monophosphate kinase) (UMP kinase) (UMPK)
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MEKPKYKRIVLKLSGEALAGEQGNGINPTVIQSIAKQVKEIAELEVEVAVVVGGGNLWRGKTGSDLGMDRATADYMGMLATVMNSLALQDSLETLGIQSRVQTSIEMRQVAEPYIRRKAIRHLEKKRVVIFAAGTGNPYFSTDTTAALRAAEIEADVILMAKNNVDGVYNADPRKDESAVKYESLSYLDVLKDGLEVMDSTASSLCMDNDIPLIVFSIMEEGNIKRAVIGESIGTIVRGK
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Catalyzes the reversible phosphorylation of UMP to UDP, with ATP or dATP as the most efficient phosphate donors. Is also able to phosphorylate 5-fluoro-UMP and 6-aza-UMP.
|
O31760
|
RNJ2_BACSU
|
Ribonuclease J2 (RNase J2) (EC 3.1.-.-)
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MKKKNTENVRIIALGGVGEIGKNLYVIEIDSDIFVVDAGLMHPENEMLGIDVVIPDISYLIERADRVKAIFLTHGHDENIGGVFYLLNKLSVPVYGTKLTLALLREKLKQYGHNRKTDLREIHSKSVITFESTKVSFFRTIHSIPDSVGVSFKTSLGSIVCTGDFKFDQTPALNQTCDIGEIAKIGNSGVLALLSDSANAERPGYTPSEAAVSGEISDALYNSQNRVIIAVFASNINRIQQVIHAAAQNGRKIAVAGKNLQSVLQLARKLGYIEADDELFISVQDVKKYPKREVAIITAGSQGEPLAALTRMANKAHKQLNIEEGDTVVIASTPIPGQELIYSKTVDLLARAGAQVIFAQKRVHVSGHGSQEELKLMINLLKPKYLIPVNGEYRMQKAHSKIAEETGMKRSDIFLIEKGDVVEFRGQNVKIGDKVPYGNILIDGLGVGDIGNIVLRDRRLLSQDGILIVVITLDKQKKHLVSGPEIITRGFVYVRESEGLIVQATELVRSIVTEATETSNVEWSTLKQAMRDALNQFLYEKTKRKPMIIPIIMEV
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Endonucleolytically cleaves the 5'-leader sequence of certain mRNAs. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Plays a role in mRNA maturation and stability. Appears to have a limited effect on 16S rRNA maturation, despite its similarity to RNase J1. This subunit alone has very poor 5'-3' exonuclease activity.
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O31774
|
RNY_BACSU
|
Ribonuclease Y (RNase Y) (EC 3.1.-.-)
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MTPIMMVLISILLILLGLVVGYFVRKTIAEAKIAGARGAAEQILEDAKRDAEALKKEALLEAKDEIHKLRIDAEQEVRERRNELQKQENRLLQKEENLDRKHEGIDKREAMLEKKDHSLNERQQHIEEMESKVDEMIRMQQSELERISSLTRDEAKQIILERVENELSHDIAIMTKETENRAKEEADKKAKNILSLALQRCAADHVAETTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRRETARIALDKLVQDGRIHPARIEEMVEKSRREVDDYIREMGEQTTFEVGVHGLHPDLIKILGRLKFRTSYGQNVLKHSMEVAFLAGLMASELGEDAKLAKRAGLLHDIGKAIDHEVEGSHVEIGVELATKYKEHPVVINSIASHHGDEEPTSIIAVLVAAADALSAARPGARSETLENYIRRLEKLEEISESYEGVEKSFAIQAGREVRIMVKPDSINDLEAHRLARDIRKRIEDELDYPGHIKVTVIRETRAVEYAK
|
Endoribonuclease that initiates mRNA decay. Initiates the decay of all SAM-dependent riboswitches, such as yitJ riboswitch. Involved in processing of the gapA operon mRNA, it cleaves between cggR and gapA. Is also the decay-initiating endonuclease for rpsO mRNA. Involved in degradation of type I toxin-antitoxin system bsrG/SR4 RNAs and a minor role in degradation of type I toxin-antitoxin system bsrE/SR5 degradation.
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O31775
|
YMDB_BACSU
|
2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) (Global regulator YmdB)
|
MRILFIGDVVGSPGRDMVKEYVPKLKTKYKPHFTIINGENAAHGKGLTEKIYHSLIQSGADAITMGNHTWDKKEIFDFIDDVPNLVRPANFPEGTPGKGITYVKANGKELAVINLQGRTFLPPLDDPFLKADELIAEAAKRTPYIFIDFHAEATSEKLALGWYTDGRASAVVGTHTHVQTADNRILPKGTAYITDVGMTGPYDGILGMDRETIIKRFKTNLPVRFTVAEGKTTLSGVVIDIDDQTKKAVKIERILINDDHMFFE
|
Plays a central, regulatory role in the late adaptive responses and affects the levels of many genes. May act via regulation of cAMP levels. Decreases the expression of motility genes and induces genes involved in biofilm formation, by controlling the expression of SlrR. Required for formation of intercellular nanotubes that bridge neighboring cells to allow molecular exchange. Plays a key role in directing the early stages of colony development. In vitro, has a metal-dependent phosphodiesterase activity against 2',3'-cAMP and 2',3'-cGMP. Has also 3',5'-cyclic-nucleotide phosphodiesterase activity, but cannot use cyclic di-AMP or cyclic di-GMP, and does not have phosphatase activity.
|
O31854
|
CDAS_BACSU
|
Cyclic di-AMP synthase CdaS (c-di-AMP synthase) (EC 2.7.7.85) (Diadenylate cyclase) (DAC)
|
MKAMRYEQISENAFKGKIQVYLEQILGDASLILKTLHEKDQCLLCELDDLGHVFQDMQGIASSFYLQSYIEEFTPAFIELAKAIKALSEHKHGALIVIERADPVERFIQKGTSLHAEISSSLIESIFFPGNPLHDGALLVRENKLVSAANVLPLTTKEVDIHLGTRHRAALGMSGYTDALVLVVSEETGKMSFAKDGVLYPLISPRT
|
One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di-AMP synthesis. Overexpression of the hyperactive mutant (L44F) in the absence of c-di-AMP phosphodiesterase GdpP leads to growth defects in log phase (long curly cell filaments) that disappear upon sporulation spore formation is normal, showing sporulation is insensitive to the excess c-di-AMP. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis it is toxic when present in excess.
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O32001
|
YOKF_BACSU
|
SPbeta prophage-derived endonuclease YokF (EC 3.1.-.-)
|
MKKVLLGFAAFTLSLSLAACSSNDSEKVSTEKETPQASTDVEKKTEQKESTKEKTADKSKEKDKKELVDVTLDRAVDGDTIKVTYNGNVDTVRYLLIDTPETKKPNSCVQPYGEDASKRNKELVNSGKLQLEFDKGDRRDKYGRLLAYVYVDGKSVQETLLKEGLARVAYVYEPNTKYIDQFKKDEQEAKSEKLSIWSKNGYVTDRGFNGCVKEKTTAVKKATTSKPAATQPTTPKASSETSTTTEKEASSETTGGTETFKNCTELRKKYPNGVPSSHPAYQSKMDRDHDNYACER
|
Catalyzes the hydrolysis of supercoiled double and single strand DNA and RNA. Involved in chromosomal DNA degradation and cell death caused by thermal stress.
|
O32076
|
FLOT_BACSU
|
Flotillin-like protein FloT (Bacterial flotillin homolog YuaG)
|
MTMPIIMIIGVVFFLLIALIAVFITKYRTAGPDEALIVTGSYLGNKNVHVDEGGNRIKIVRGGGTFVLPVFQQAEPLSLLSSKLDVSTPEVYTEQGVPVMADGTAIIKIGGSIGEIATAAEQFLGKSKDDREQEAREVLEGHLRSILGSMTVEEIYKNREKFSQEVQRVASQDLAKMGLVIVSFTIKDVRDKNGYLESLGKPRIAQVKRDADIATAEADKETRIKRAEADKDAKKSELERATEIAEAEKINQLKMAEFRREQDTAKANADQAYDLETARARQQVTEQEMQVKIIERQKQIELEEKEILRRERQYDSEVKKKADADRYSVEQSAAAEKAKQLAEADAKKYSIEAMAKAEAEKVRIDGLAKAEAEKAKGETEAEVIRLKGLAEAEAKEKIAAAFEQYGQAAIFDMIVKMLPEYAKQAAAPLSNIDKITVVDTGGSGESSGANKVTSYATNLMSSLQESLKASSGIDVKEMLENFSGKGNVKQSINELTNEIKEAKTIQKSE
|
Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. FloA and FloT function is partially redundant double deletions have marked synthetic phenotypes. Flotillins are thought to be important factors in membrane fluidity, especially during periods of rapid growth in rich media (Probable). Whether specific proteins are associated with FMMs is controversial in one study FloT rafts have been shown to include proteins involved in adaptation to stationary phase, while FloA-FloT rafts include proteins involved in differentation including sporulation, biofilm formation and DNA uptake competence. Another (more finely resolved) study only showed association of NfeD2 with FloT rafts of all the proteins examined. Aids homooligomerization of KinC and KinD but not KinB, may prevent incorrect hetero-association of the above kinases. Simultaneous overexpression of both FloA and FloT leads to defects in cell division and differentiation, in part caused by stabilization of FtsH and its subsequent increased ability to degrade proteins. Cells make more biofilm, are about half as long, have less EzrA and more frequent Z-rings. Involved in spatial organization of membranes, perhaps recruiting proteins (e.g. NfeD2) to specific membrane regions (Probable). Plays a role in phosphorylation of master regulator Spo0A, an early sporulation event. Plays a non-redundant role with dynamin-like protein A (dynA) in membrane dynamics and cell shape.
|
O32129
|
LIPA_BACSU
|
Lipoyl synthase (EC 2.8.1.8) (Lip-syn) (LS) (Lipoate synthase) (Lipoic acid synthase) (Sulfur insertion protein LipA)
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MAKKDEHLRKPEWLKIKLNTNENYTGLKKLMRENNLHTVCEEAKCPNIHECWAVRRTATFMILGSVCTRACRFCAVKTGLPTELDLQEPERVADSVALMNLKHAVITAVARDDQKDGGAGIFAETVRAIRRKSPFTTIEVLPSDMGGNYDNLKTLMDTRPDILNHNIETVRRLTPRVRARATYDRSLEFLRRAKEMQPDIPTKSSIMIGLGETKEEIIEVMDDLLANNVDIMAIGQYLQPTKKHLKVQKYYHPDEFAELKEIAMQKGFSHCEAGPLVRSSYHADEQVNEASKKRQAQA
|
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. {ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:19820084}.
|
O32141
|
PUCL_BACSU
|
Uric acid degradation bifunctional protein PucL [Includes: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (OHCU decarboxylase) (EC 4.1.1.97); Uricase (EC 1.7.3.3) (Urate oxidase)]
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MFTMDDLNQMDTQTLTDTLGSIFEHSSWIAERSAALRPFSSLSDLHRKMTGIVKAADRETQLDLIKKHPRLGTKKTMSDDSVREQQNAGLGKLEQQEYEEFLMLNEHYYDRFGFPFILAVKGKTKQDIHQALLARLESERETEFQQALIEIYRIARFRLADIITEKGETQMKRTMSYGKGNVFAYRTYLKPLTGVKQIPESSFAGRDNTVVGVDVTCEIGGEAFLPSFTDGDNTLVVATDSMKNFIQRHLASYEGTTTEGFLHYVAHRFLDTYSHMDTITLTGEDIPFEAMPAYEEKELSTSRLVFRRSRNERSRSVLKAERSGNTITITEQYSEIMDLQLVKVSGNSFVGFIRDEYTTLPEDGNRPLFVYLNISWQYENTNDSYASDPARYVAAEQVRDLASTVFHELETPSIQNLIYHIGCRILARFPQLTDVSFQSQNHTWDTVVEEIPGSKGKVYTEPRPPYGFQHFTVTREDAEKEKQKAAEKCRSLKA
|
Catalyzes two steps in the degradation of uric acid, i.e. the oxidation of uric acid to 5-hydroxyisourate (HIU) and the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
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O32142
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HIUH_BACSU
|
5-hydroxyisourate hydrolase (HIU hydrolase) (HIUHase) (EC 3.5.2.17) (Transthyretin-related protein) (TRP)
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MGKLTTHILDLTCGKPAANVKIGLKRLGESIMKEVYTNNDGRVDVPLLAGEELMSGEYVMEFHAGDYFASKNMNAADQPFLTIVTVRFQLADPDAHYHIPLLLSPFGYQVYRGS
|
Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
|
O32148
|
PUCG_BACSU
|
(S)-ureidoglycine--glyoxylate transaminase (UGXT) (EC 2.6.1.112) ((S)-ureidoglycine--glyoxylate aminotransferase) (Purine catabolism protein PucG)
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MSGRRELCTPLRTIMTPGPVEVDPRVLRVMSTPVVGQFDPAFTGIMNETMEMLRELFQTKNRWAYPIDGTSRAGIEAVLASVIEPEDDVLIPIYGRFGYLLTEIAERYGANVHMLECEWGTVFDPEDIIREIKKVKPKIVAMVHGETSTGRIHPLKAIGEACRTEDALFIVDAVATIGGCEVKVDEWKIDAAIGGTQKCLSVPSGMAPITYNERVADVIAARKKVERGIATQADRAALSGNRPITSNYFDLSQLEDYWSERRLNHHTEATTMLYALREGVRLVLEEGLETRFERHRHHEAALAAGIKAMGLRLFGDDSCKMPVVTCVEIPGGIDGESVRDMLLAQFGIEIASSFGPLAGKIWRIGTMGYSCRKENVLFVLAGLEAVLLRHNAGIEAGKALQAALDVYENAGRQAAV
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Catalyzes the transamination between an unstable intermediate ((S)-ureidoglycine) and the end product of purine catabolism (glyoxylate) to yield oxalurate and glycine. Glyoxylate is the preferred substrate, but other amino-group acceptors can be used.
|
O32163
|
SUFU_BACSU
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Zinc-dependent sulfurtransferase SufU (EC 2.-.-.-) (Putative iron-sulfur cluster assembly scaffold protein SufU) (Sulfur acceptor protein SufU)
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MSFNANLDTLYRQVIMDHYKNPRNKGVLNDSIVVDMNNPTCGDRIRLTMKLDGDIVEDAKFEGEGCSISMASASMMTQAIKGKDIETALSMSKIFSDMMQGKEYDDSIDLGDIEALQGVSKFPARIKCATLSWKALEKGVAKEEGGN
|
Part of the SUF-like system that mediates the biosynthesis of iron-sulfur (Fe-S) clusters. Acts as a sulfurtransferase and thus transfers sulfur from SufS to SufB. Mechanistically, the transfer from SufS to SufU is triggered by zinc-ligand swapping that provides a free thiol from SufU to accept sulfur from SufS.
|
O32164
|
SUFS_BACSU
|
Cysteine desulfurase SufS (EC 2.8.1.7)
|
MNITDIREQFPILHQQVNGHDLVYLDSAATSQKPRAVIETLDKYYNQYNSNVHRGVHTLGTRATDGYEGAREKVRKFINAKSMAEIIFTKGTTTSLNMVALSYARANLKPGDEVVITYMEHHANIIPWQQAVKATGATLKYIPLQEDGTISLEDVRETVTSNTKIVAVSHVSNVLGTVNPIKEMAKIAHDNGAVIVVDGAQSTPHMKIDVQDLDCDFFALSSHKMCGPTGVGVLYGKKALLENMEPAEFGGEMIDFVGLYESTWKELPWKFEAGTPIIAGAIGLGAAIDFLEEIGLDEISRHEHKLAAYALERFRQLDGVTVYGPEERAGLVTFNLDDVHPHDVATVLDAEGIAVRAGHHCAQPLMKWLDVTATARASFYLYNTEEEIDKLVEALQKTKEYFTNVF
|
Type II cysteine desulfurase that acts as the initial step in the SUF-like Fe-S cluster assembly pathway. Catalyzes the removal of elemental sulfur atoms from L-cysteine by using the cofactor pyridoxal 5'-phosphate (PLP), resulting in the production of L-alanine and persulfide. Activity is stimulated by SufU, which acts as a sulfurtransferase that receives sulfur from SufS via a zinc-ligand swapping mechanism and transfers it to SufB.
|
O32219
|
CADA_BACSU
|
Cadmium, zinc and cobalt-transporting ATPase (EC 7.2.2.12) (EC 7.2.2.21)
|
MRLVKQEYVLDGLDCSNCARKIENGVKGIKGINGCAVNFAASTLTVSADGKEEQWVTNKVEKKVKSIDPHVTVRQKHIKKSADDGYRNRMVNMLIRMAAAVILGAAAYLVQSGTIEFFLFLGAYLIIGGDIIIRAVKNIIRGQVFDEHFLMALATIGAFLIQQYPEGVAVMLFYQIGELFQGAAVSRSRKSISALMDIRPDYANLKTKNGIEQVSSEDVQTGDIIVVNPGESIPLDGKVVQGSAMVDTSALTGESVPRKAAEGQDVMSGFINQNGVLHIEVTKGYQESAVSKILDLVQNASSRKARTENFITKFAKYYTPAVVIIAVLLAFVPPLVLSGAALSDWVYRALIFLVISCPCALVVSIPLGFFGGIGAASKAGVLVKGSNYLEALNQVKYAVFDKTGTLTKGSFEVTEIKPAEGFTKDRLLEAAAYAELHSQHPIAESVRKAYGKMLSSDEIESYEEISGHGIFAKVNGTEILAGNKKLMEREQIEDVPDENAGTIVHVAVDQRYAGAIIIADEIKEDAAQAVADLKSLGIKQTAMLTGDSKQTGEAVGKQLGIGEVYAELLPQDKVAQVEALEAKLLPSEKLIFVGDGINDTPVLARADIGVAMGGLGSDAAVEAADIVLMTDQPSKIAEAIRIAKRTRRIVWQNIGFALGVKAIFLILGAFGIATMWEAVFSDVGVTLLAVANAMRVMRLKNK
|
Couples the hydrolysis of ATP with the transport of cadmium, zinc and cobalt out of the cell. Does not seem to transport copper.
|
O32220
|
COPA_BACSU
|
Copper-exporting P-type ATPase (Protein CopA) (EC 7.2.2.8) (Copper-exporting P-type ATPase A) (Cu(+)-exporting ATPase)
|
MSEQKEIAMQVSGMTCAACAARIEKGLKRMPGVTDANVNLATETSNVIYDPAETGTAAIQEKIEKLGYHVVTEKAEFDIEGMTCAACANRIEKRLNKIEGVANAPVNFALETVTVEYNPKEASVSDLKEAVDKLGYKLKLKGEQDSEAAAKKKEERKQTARLIFSAVLSFPLLWAMVSHFTFTSFIWVPDIFLNPWMQFALATPVQFLIGWPFYVGAYKALRNKSANMDVLVALGTTAAYAYSLYLTFQSIGSHGHTDGLYYETSAILLTLILLGKLFETKAKGRSSDAIKKLMKLQAKTATVVRDGQEQIIPIDEVLVNDIVYVKPGERIPVDGEVVEGRSAVDESMITGESLPVDKNPGDSVTGSTVNANGFLKIKAVNVGKDTALSHIIKIVEEAQGSKAPIQRLADQISGIFVPIVLGIAVLTFLIWYLWAAPGDFAEAISKFIAVLVIACPCALGLATPTSIMAGSGRAAEFGILFKGGEHLEKTHRLDTIVLDKTGTVTNGKPRLTDAIPFGRFEEKDLLQFAAAAETGSEHPLGEAIIAGVKDKGLEIPKLTRFEAKVGAGILAEAGGKSILVGTRKLMESEQVEHGALLAQMEELEAEGKTVMLVSIDGEAAGLVAVADTIKDTSRKAVARLKELGLDVIMMTGDNRRTAEAIAKEAGIANIIAEVLPEQKAAEIARLQKEGRQTAMVGDGINDAPALATADIGMAIGTGTDIAMETADITLIRGDLNSIADAIRMSRLTMKNIKQNLFWALGYNSLGIPIAALGFLAPWIAGAAMAFSSVSVVLNALRLQKVK
|
Involved in copper export.
|
O32224
|
AZOR2_BACSU
|
FMN-dependent NADH:quinone oxidoreductase 2 (EC 1.6.5.-) (Azo-dye reductase 2) (FMN-dependent NADH-azo compound oxidoreductase 2) (FMN-dependent NADH-azoreductase 2) (EC 1.7.1.17)
|
MAKVLYITAHPHDEATSYSMATGKAFIESYKEANPNDEVVHIDLYKENIPHIDADVFSGWGKLQSGTGFEELSESEKAKVGRLGELSDQFASADKYVFVTPLWNFSFPPVMKAYLDSVAVAGKSFKYTEQGPVGLLTDKKAIHIQARGGYYSEGPAAEMEMGHRYIGIMMNFFGVPSFDGIFVEGHNAEPDKAQQIKEDAIARAKEAGKTF
|
Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones (Probable). Contributes to resistance to 2-methylhydroquinone (2-MHQ) and catechol. Exhibits NADH-dependent 2,6-dichloroindophenol (DCIP) oxidoreductase activity.
|
O32472
|
PHAJ_AERCA
|
(R)-specific enoyl-CoA hydratase (EC 4.2.1.119)
|
MSAQSLEVGQKARLSKRFGAAEVAAFAALSEDFNPLHLDPAFAATTAFERPIVHGMLLASLFSGLLGQQLPGKGSIYLGQSLSFKLPVFVGDEVTAEVEVTALREDKPIATLTTRIFTQGGALAVTGEAVVKLP
|
Catalyzes the hydration of trans-2-enoyl-CoA with a chain-length of 4-6 carbon atoms, forming the corresponding (3R)-3-hydroxyacyl-CoA.
|
O32504
|
PPRA_DEIRA
|
DNA repair protein PprA (Pleiotropic protein promoting DNA repair)
|
MLPLAFLICSGHNKGSMARAKAKDQTDGIYAAFDTLMSTAGVDSQIAALAASEADAGTLDAALTQSLQEAQGRWGLGLHHLRHEARLTDDGDIEILTDGRPSARVSEGFGALAQAYAPMQALDERGLSQWAALGEGYRAPGDLPLAQLKVLIEHARDFETDWSAGRGETFQRVWRKGDTLFVEVARPASAEAALSDAAWDVIASIKDRAFQRELMRRSEKDGMLGALLGARHAGAKANLAQLPEAHFTVQAFVQTLSGAAARNAEEYRAALKTAAAALEEYQGVTTRQLSEVLRHGLRES
|
dsDNA-binding protein that contributes to the ionizing radiation resistance of D.radiodurans. Plays a role in DNA repair and genome reconstitution, and is necessary for recovery from severe genomic fragmentation as a result of exposure to severe levels of ionizing radiation. In vitro, binds to double-stranded DNA carrying strand breaks and stimulates the DNA end-joining reaction catalyzed by DNA ligases. Thus, PprA plays a critical role in a non-homologous end-joining (NHEJ) pathway for the repair of radiation-induced DNA double-strands breaks. Cannot bind to dsDNA without strand breaks or single-stranded DNA.
|
O32583
|
THIS_ECOLI
|
Sulfur carrier protein ThiS (Thiamine biosynthesis protein ThiS)
|
MQILFNDQAMQCAAGQTVHELLEQLDQRQAGAALAINQQIVPREQWAQHIVQDGDQILLFQVIAGG
|
Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.
|
O32765
|
LDH_LACHE
|
L-lactate dehydrogenase (L-LDH) (EC 1.1.1.27)
|
MAREEKPRKVILVGDGAVGSTFAFSMVQQGIAEELGIIDIAKEHVEGDAIDLADATPWTSPKNIYAADYPDCKDADLVVITAGAPQKPGETRLDLVNKNLKILSSIVEPVVESGFEGIFLVVANPVDILTHATWRMSGFPKDRVIGSGTSLDTGRLQKVIGKMENVDPSSVNAYMLGEHGDTEFPAWSYNNVAGVKVADWVKAHNMPESKLEDIHQEVKDMAYDIINKKGATFYGIGTASAMIAKAILNDEHRVLPLSVPMDGEYGLHDLHIGTPAVVGRKGLEQVIEMPLSDKEQELMTASADQLKKVMDKAFKETGVKVRQ
|
Catalyzes the conversion of lactate to pyruvate. {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:9212432}.
|
O33125
|
DBH_MYCLE
|
DNA-binding protein HupB (HupB) (EC 1.16.3.1) (21 kDa laminin-2-binding protein) (ML-LBP21) (DNA-binding protein HU homolog) (Histone-like protein) (Hlp)
|
MNKAELIDVLTQKLGSDRRQATAAVENVVDTIVRAVHKGDSVTITGFGVFEQRRRAARVARNPRTGETVKVKPTSVPAFRPGAQFKAVVAGAQRLPLEGPAVKRGVATSAAKKAAIKKAPVKKALAKKAATKAPAKKAVKAPAKKITTAVKVPAKKATKVVKKVAAKAPVRKATTRALAKKAAVKKAPAKKVTAAKRGRK
|
A nucleoid-associated protein (NAP) that plays a role in local chromosome architecture and chromosome compactation. Required for biofilm formation, stress survival and possibly in cell wall assembly, probably influences transcription (By similarity). RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment and in the host (By similarity). Binds Fe(3+) but not Fe(2+). Has ferroxidase activity, converts Fe(2+) into Fe(3+) and in the presence of H(2)O(2) prevents the generation of hydroxyl radicals (the Fenton reaction). Protects DNA from damage in the presence of FeSO(4) and H(2)O(2). May function in iron storage.
|
O33194
|
G3PP_MYCTU
|
D-glycerol 3-phosphate phosphatase (D,L-glycerol 3-phosphate phosphatase) (G3P phosphatase)
|
MKSIAQEHDCLLIDLDGTVFCGRQPTGGAVQSLSQVRSRKLFVTNNASRSADEVAAHLCELGFTATGEDVVTSAQSAAHLLAGQLAPGARVLIVGTEALANEVAAVGLRPVRRFEDRPDAVVQGLSMTTGWSDLAEAALAIRAGALWVAANVDPTLPTERGLLPGNGSMVAALRTATGMDPRVAGKPAPALMTEAVARGDFRAALVVGDRLDTDIEGANAAGLPSLMVLTGVNSAWDAVYAEPVRRPTYIGHDLRSLHQDSKLLAVAPQPGWQIDVGGGAVTVCANGDVDDLEFIDDGLSIVRAVASAVWEARAADLHQRPLRIEAGDERARAALQRWSLMRSDHPVTSVGTQ
|
Dephosphorylates D-glycerol 3-phosphate (sn-glycerol 1-phosphate). Is the final enzyme involved in the recycling/catabolism of glycerophospholipid polar heads. To a lesser extent, is also able to act on glycerol 2-phosphate and D-ribulose 5-phosphate, but cannot use D-glyceraldehyde 3-phosphate, dihydroxyacetone-phosphate, UMP or GMP as substrates.
|
O33283
|
EPHG_MYCTU
|
Epoxide hydrolase EphG (EH) (EC 3.3.2.10) (Cholesterol-5,6-oxide hydrolase) (EC 3.3.2.11)
|
MAELTETSPETPETTEAIRAVEAFLNALQNEDFDTVDAALGDDLVYENVGFSRIRGGRRTATLLRRMQGRVGFEVKIHRIGADGAAVLTERTDALIIGPLRVQFWVCGVFEVDDGRITLWRDYFDVYDMFKGLLRGLVALVVPSLKATL
|
Epoxide hydrolase capable of hydrolyzing long or bulky lipophilic epoxides such as 9,10-epoxystearic acid and cholesterol 5,6-oxide in vitro. The physiological substrates have yet to be identified, but could be fatty acid or steroid derivatives.
|
O33289
|
ARGA_MYCTU
|
Amino-acid acetyltransferase (EC 2.3.1.1) (N-acetylglutamate synthase) (AGS) (NAGS)
|
MTERPRDCRPVVRRARTSDVPAIKQLVDTYAGKILLEKNLVTLYEAVQEFWVAEHPDLYGKVVGCGALHVLWSDLGEIRTVAVDPAMTGHGIGHAIVDRLLQVARDLQLQRVFVLTFETEFFARHGFTEIEGTPVTAEVFDEMCRSYDIGVAEFLDLSYVKPNILGNSRMLLVL
|
Catalyzes the conversion of L-glutamate to alpha-N-acetyl-L-glutamate. L-glutamine is a significantly better substrate compared to L-glutamate.
|
O33336
|
PPTT_MYCTU
|
4'-phosphopantetheinyl transferase PptT (PPTase) (EC 2.7.8.7)
|
MTVGTLVASVLPATVFEDLAYAELYSDPPGLTPLPEEAPLIARSVAKRRNEFITVRHCARIALDQLGVPPAPILKGDKGEPCWPDGMVGSLTHCAGYRGAVVGRRDAVRSVGIDAEPHDVLPNGVLDAISLPAERADMPRTMPAALHWDRILFCAKEATYKAWFPLTKRWLGFEDAHITFETDSTGWTGRFVSRILIDGSTLSGPPLTTLRGRWSVERGLVLTAIVL
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. Involved in post-translational modification of various type-I polyketide synthases required for the formation of both mycolic acids and lipid virulence factors. Acts on Pks13, Mas, PpsA, PpsB, PpsC and PpsD. Also acts on AcpM, the meromycolate extension acyl carrier protein. In addition, is involved in the activation of the acyl carrier protein MbtL and the nonribosomal peptides synthases MbtB and MbtE, which are involved in the biosynthesis of the siderophore mycobactin.
|
O33348
|
RELG_MYCTU
|
Toxin RelG (EC 3.1.-.-) (Putative endoribonuclease RelG)
|
MPYTVRFTTTARRDLHKLPPRILAAVVEFAFGDLSREPLRVGKPLRRELAGTFSARRGTYRLLYRIDDEHTTVVILRVDHRADIYRR
|
Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity and preferentially cleaves at the 3'-end of purine ribonucleotides (By similarity). Overexpression in M.tuberculosis or M.smegmatis inhibits colony formation in a bacteriostatic rather than bacteriocidal fashion. Its toxic effect is neutralized by coexpression with cognate antitoxin RelB2 (shown only for M.smegmatis). Overexpression also increases the number of gentamicin-tolerant and levofloxacin-tolerant persister cells. {ECO:0000250, ECO:0000269|PubMed:19114484, ECO:0000269|PubMed:20011113, ECO:0000269|PubMed:20061486, ECO:0000269|PubMed:20498855}. In combination with cognate antitoxin RelF represses its own promoter. Has been seen to bind DNA in complex with antitoxin RelF but not alone.
|
O33363
|
GDSL_MYCTU
|
GDSL lipase Rv0518 (EC 3.1.1.-)
|
MSRPGTYVIGLTLLVGLVVGNPGCPRSYRPLTLDYRLNPVAVIGDSYTTGTDEGGLGSKSWTARTWQMLAARGVRIAADVAAEGRAGYGVPGDHGNVFEDLTARAVQPDDALVVFFGSRNDQGMDPEDPEMLAEKVRDTFDLARHRAPSASLLVIAPPWPTADVPGPMLRIRDVLGAQARAAGAVFVDPIADHWFVDRPELIGADGVHPNDAGHEYLADKIAPLISMELVG
|
GDSL lipase that catalyzes the hydrolysis of p-nitrophenyl (pNP) esters. pNP-decanoate (C10) is the preferred substrate. It can also use pNP-octanoate (C8), pNP-dodecanoate (C12) and pNP-tetradecanoate (C14). Has lower activity with pNP-butyrate (C4), pNP-palmitate (C16) and pNP-stearate (C18). Does not show phospholipase A1 activity. Might help bacteria to utilize available lipids for its growth as well as provide resistance to various intracellular stresses by cell wall modulation resulting in enhanced intracellular survival.
|
O33407
|
ESTA_PSEAE
|
Esterase EstA (EC 3.1.1.1) (Autotransporter esterase EstA)
|
MIRMALKPLVAACLLASLSTAPQAAPSPYSTLVVFGDSLSDAGQFPDPAGPAGSTSRFTNRVGPTYQNGSGEIFGPTAPMLLGNQLGIAPGDLAASTSPVNAQQGIADGNNWAVGGYRTDQIYDSITAANGSLIERDNTLLRSRDGYLVDRARQGLGADPNALYYITGGGNDFLQGRILNDVQAQQAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPATFGGPLQPFASQLSGTFNAELTAQLSQAGANVIPLNIPLLLKEGMANPASFGLAADQNLIGTCFSGNGCTMNPTYGINGSTPDPSKLLFNDSVHPTITGQRLIADYTYSLLSAPWELTLLPEMAHGTLRAYQDELRSQWQADWENWQNVGQWRGFVGGGGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDEAWRAGVAAGFYRQKLEAGAKDSDYRMNSYMASAFVQYQENRWWADAALTGGYLDYDDLKRKFALGGGERSEKGDTNGHLWAFSARLGYDIAQQADSPWHLSPFVSADYARVEVDGYSEKGASATALDYDDQKRSSKRLGAGLQGKYAFGSDTQLFAEYAHEREYEDDTQDLTMSLNSLPGNRFTLEGYTPQDHLNRVSLGFSQKLAPELSLRGGYNWRKGEDDTQQSVSLALSLDF
|
Esterase whose enzymatic activity is required for rhamnolipid production, all kinds of cell motility (swimming, swarming, and twitching), and biofilm formation the exact role of EstA in these processes is unclear. In vitro, has pronounced esterase activities towards p-nitrophenyl esters of short acyl chain length (C4-C6) and Tween detergents. Also shows relatively high activity towards beta-naphthyl butyrate, whereas its activities towards triacylglycerols and acyls-CoA are negligible.
|
O33434
|
SOXA_PARPN
|
L-cysteine S-thiosulfotransferase subunit SoxA (EC 2.8.5.2) (Cytochrome c551 subunit diheme) (Protein SoxA) (SoxAX cytochrome complex subunit A) (Sulfur oxidizing protein A) (Thiosulfate-oxidizing multienzyme system protein SoxA) (TOMES protein SoxA)
|
MPRFTKTKGTLAATALGLALAGAAFADPVEDGLVIETDSGPVEIVTKTAPPAFLADTFDTIYSGWHFRDDSTRDLERDDFDNPAMVFVDRGLDKWNAAMGVNGESCASCHQGPESMAGLRAVMPRVDEHTGKLMIMEDYVNACVTERMGLEKWGVTSDNMKDMLSLISLQSRGMAVNVKIDGPAAPYWEHGKEIYYTRYGQLEMSCANCHEDNAGNMIRADHLSQGQINGFPTYRLKDSGMVTAQHRFVGCVRDTRAETFKAGSDDFKALELYVASRGNGLSVEGVSVRH
|
C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
|
O33469
|
PAAK_PSEPU
|
Phenylacetate-coenzyme A ligase (EC 6.2.1.30) (Phenylacetyl-CoA ligase) (PA-CoA ligase)
|
MNMYHDADRALLDPMETASVDALRQHQLERLRWSLKHAYDNVPLYRQRFAECGAHPDDLTCLEDLAKFPFTGKNDLRDNYPYGMFAVPQEEVVRLHASSGTTGKPTVVGYTQNDINTWANVVARSIRAAGGRKGDKVHVSYGYGLFTGGLGAHYGAERLGCTVIPMSGGQTEKQVQLIRDFQPDIIMVTPSYMLNLADEIERQGIDPHDLKLRLGIFGAEPWTDELRRSIEQRLGINALDIYGLSEIMGPGVAMECIETKDGPTIWEDHFYPEIIDPVTGEVLPDGQLGELVFTSLSKEALPMVRYRTRDLTRLLPGTARPMRRIGKITGRSDDMLIIRGVNVFPTQIEEQVLKIKQLSEMYEIHLYRNGNLDSVEVHVELRAECQHLDEGQRKLVIGELSKQIKTYIGISTQVHLQACGTLKRSEGKACHVYDKRLAS
|
Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). Involved in the phenylalanine metabolism. Can also use CTP and UTP as substrate.
|
O33599
|
LYTM_STAA8
|
Glycyl-glycine endopeptidase LytM (EC 3.4.24.75) (Autolysin LytM)
|
MKKLTAAAIATMGFATFTMAHQADAAETTNTQQAHTQMSTQSQDVSYGTYYTIDSNGDYHHTPDGNWNQAMFDNKEYSYTFVDAQGHTHYFYNCYPKNANANGSGQTYVNPATAGDNNDYTASQSQQHINQYGYQSNVGPDASYYSHSNNNQAYNSHDGNGKVNYPNGTSNQNGGSASKATASGHAKDASWLTSRKQLQPYGQYHGGGAHYGVDYAMPENSPVYSLTDGTVVQAGWSNYGGGNQVTIKEANSNNYQWYMHNNRLTVSAGDKVKAGDQIAYSGSTGNSTAPHVHFQRMSGGIGNQYAVDPTSYLQSR
|
Peptidoglycan hydrolase (autolysin) specifically acting on polyglycine interpeptide bridges of the cell wall peptidoglycan.
|
O33830
|
AGLA_THEMA
|
Alpha-glucosidase (EC 3.2.1.20) (Maltase)
|
MPSVKIGIIGAGSAVFSLRLVSDLCKTPGLSGSTVTLMDIDEERLDAILTIAKKYVEEVGADLKFEKTMNLDDVIIDADFVINTAMVGGHTYLEKVRQIGEKYGYYRGIDAQEFNMVSDYYTFSNYNQLKYFVDIARKIEKLSPKAWYLQAANPIFEGTTLVTRTVPIKAVGFCHGHYGVMEIVEKLGLEEEKVDWQVAGVNHGIWLNRFRYNGGNAYPLLDKWIEEKSKDWKPENPFNDQLSPAAIDMYRFYGVMPIGDTVRNSSWRYHRDLETKKKWYGEPWGGADSEIGWKWYQDTLGKVTEITKKVAKFIKENPSVRLSDLGSVLGKDLSEKQFVLEVEKILDPERKSGEQHIPFIDALLNDNKARFVVNIPNKGIIHGIDDDVVVEVPALVDKNGIHPEKIEPPLPDRVVKYYLRPRIMRMEMALEAFLTGDIRIIKELLYRDPRTKSDEQVEKVIEEILALPENEEMRKHYLKR
|
Alpha-glycosidase with a very broad specificity. Hydrolyzes maltose and other small maltooligosaccharides but is inactive against the polymeric substrate starch. AglA is not specific with respect to the configuration at the C-4 position of its substrates because glycosidic derivatives of D-galactose are also hydrolyzed. Does not cleave beta-glycosidic bonds.
|
O33832
|
BSUHB_THEMA
|
Fructose-1,6-bisphosphatase/inositol-1-monophosphatase (FBPase/IMPase) (EC 3.1.3.11) (EC 3.1.3.25) (Inositol-1-phosphatase) (I-1-Pase)
|
MDRLDFSIKLLRKVGHLLMIHWGRVDNVEKKTGFKDIVTEIDREAQRMIVDEIRKFFPDENIMAEEGIFEKGDRLWIIDPIDGTINFVHGLPNFSISLAYVENGEVKLGVVHAPALNETLYAEEGSGAFFNGERIRVSENASLEECVGSTGSYVDFTGKFIERMEKRTRRIRILGSAALNAAYVGAGRVDFFVTWRINPWDIAAGLIIVKEAGGMVTDFSGKEANAFSKNFIFSNGLIHDEVVKVVNEVVEEIGGK
|
Phosphatase with broad specificity it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P) but displaying a 20-fold higher rate of hydrolysis of D-I-1-P than of the L isomer, 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, 5'-AMP and NAD(+). May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.
|
O33855
|
MIG_MYCAV
|
Medium-chain acyl-CoA ligase Mig (EC 6.2.1.2) (Macrophage-induced gene) (Medium-chain fatty acid acyl-CoA synthetase)
|
MSDTTTAFTVPAVAKAVAAAIPDRELIIQGDRRYTYRQVIERSNRLAAYLHSQGLGCHTEREALAGHEVGQDLLGLYAYNGNEFVEALLGAFAARVAPFNVNFRYVKSELHYLLADSEATALIYHAAFAPRVAEILPELPRLRVLIQIADESGNELLDGAVDYEDALASVSAQPPPVRHCPDDLYVLYTGGTTGMPKGVLWRQHDIFMTSFGGRNLMTGEPSSSIDEIVQRAASGPGTKLMILPPLIHGAAQWSVMTAITTGQTVVFPTVVDHLDAEDVVRTIEREKVMVVTVVGDAMARPLVAAIEKGIADVSSLAVVANGGALLTPFVKQRLIEVLPNAVVVDGVGSSETGAQMHHMSTPGAVATGTFNAGPDTFVAAEDLSAILPPGHEGMGWLAQRGYVPLGYKGDAAKTAKTFPVIDGVRYAVPGDRARHHADGHIELLGRDSVCINSGGEKIFVEEVETAIASHPAVADVVVAGRPSERWGQEVVAVVALSDGAAVDAGELIAHASNSLARYKLPKAIVFRPVIERSPSGKADYRWAREQAVNG
|
Catalyzes the activation of medium-chain fatty acids as acyl-coenzyme A (acyl-CoA). Shows maximal activity with saturated fatty acids of medium-chain length between C6 and C12. Has lower activity with tridecanoic acid (C13), tetradecanoic acid (C14) and with unsaturated fatty acids like oleic acid (C18:1), linolenic acid (C18:3) and arachidonic acid (C20:4). Shows weak activity with some aromatic carbon acids. Involved in the metabolism of fatty acid during mycobacterial survival in macrophages.
|
O34002
|
PRPC_ABDS2
|
2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) (Citrate synthase) (EC 2.3.3.16)
|
MTEPTIHKGLAGVTADVTAISKVNSDTNSLLYRGYPVQELAAKCSFEQVAYLLWNSELPNDSELKAFVNFERSHRKLDENVKGAIDLLSTACHPMDVARTAVSVLGANHARAQDSSPEANLEKAMSLLATFPSVVAYDQRRRRGEELIEPREDLDYSANFLWMTFGEEAAPEVVEAFNVSMILYAEHSFNASTFTARVITSTLADLHSAVTGAIGALKGPLHGGANEAVMHTFEEIGIRKDESLDEAATRSKAWMVDALAQKKKVMGFGHRVYKNGDSRVPTMKSALDAMIKHYDRPEMLGLYNGLEAAMEEAKQIKPNLDYPAGPTYNLMGFDTEMFTPLFIAARITGWTAHIMEQVADNALIRPLSEYNGPEQRQVP
|
Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity.
|
O34153
|
GLPK_ENTCA
|
Glycerol kinase (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase) (Glycerokinase) (GK)
|
MAEKNYVMAIDQGTTSSRAIIFDRNGKKIGSSQKEFPQYFPKSGWVEHNANEIWNSVQSVIAGAFIESGIRPEAIAGIGITNQRETTVVWDKTTGQPIANAIVWQSRQSSPIADQLKVDGHTEMIHEKTGLVIDAYFSATKVRWLLDNIEGAQEKADNGELLFGTIDSWLVWKLTDGQVHVTDYSNASRTMLYNIHKLEWDQEILDLLNIPSSMLPEVKSNSEVYGHTRSYHFYGSEVPIAGMAGDQQAALFGQMAFEKGMIKNTYGTGAFIVMNTGEEPQLSDNDLLTTIGYGINGKVYYALEGSIFVAGSAIQWLRDGLRMIETSPQSEELAAKAKGDNEVYVVPAFTGLGAPYWDSEARGAVFGLTRGTTKEDFVRATLQAVAYQSKDVIDTMKKDSGIDIPLLKVDGGAAKNDLLMQFQADILDIDVQRAANLETTALGAAYLAGLAVGFWKDLDELKSMAEEGQMFTPEMPAEERDNLYEGWKQAVAATQTFKFKAKKEGE
|
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:9162046}.
|
O34154
|
GLPK_ENTFA
|
Glycerol kinase (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase) (Glycerokinase) (GK)
|
MAEEKYIMAIDQGTTSSRAIIFDKKGNKIGSSQKEFTQYFPNAGWVEHNANEIWNSVQSVIAGSLIESGVKPTDIAGIGITNQRETTVVWDKATGLPIYNAIVWQSRQTTPIADQLKEDGYSEMIHEKTGLIIDAYFSATKVRWILDHVEGAQERAENGELMFGTIDTWLVWKLTGDTHVTDYSNASRTMLFNIHDLDWDQEILDLLNIPRVMLPKVVSNSEVYGLTKNYHFYGSEVPIAGMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGEEPQLSKNNLLTTIGYGINGKVYYALEGSIFVAGSAIQWLRDGLKMLQTAAESEAVAKASTGHNEVYVVPAFTGLGAPYWDSQARGAVFGLTRGTTREDFVKATLQAVAYQVRDIIDTMKEDTGIDIPVLKVDGGAANNDFLMQFQADILNTAVQRAHNLETTALGAAFLAGLAVGFWKDLEEIKAFQEEGQQFEPIMAEEEREDLYEGWQQAVAATQQFKRKNK
|
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:9162046}.
|
O34162
|
HEMN_CUPNH
|
Oxygen-independent coproporphyrinogen III oxidase (CPO) (EC 1.3.98.3) (Coproporphyrinogen III dehydrogenase) (CPDH)
|
MIPSAITSPAPDRRALSDFRALAGRIDGNGPRYTSYPTADRFHNGPDLSLYHDALAACRADAPAPLSLYLHIPFCENICYYCGCNKIITRDHGRSARYVNYLGREMALVADRLGPRRQVLQSHWGGGTPTFLDPGEMRRVMALLHEHFELAAEGEHSIEIDPRRVDHARMALLAELGFNRVSLGVQDFDPEVQQAIHRIQPFEETRAVVDAARTLGFRSVSLDLIYGLPHQTAARFGRTIDQVLALRPDRLSVYSYAHLPHVFKPQRRIDENALPPAGEKLDILVSTIERLSAEGYVYIGMDHFALPDDDLAVAQREGRLQRNFQGYSTHAGYDQVGLGISAIGAIAGRYVQNARTLDEYYGALDHGRLPLARGVAMSADDHLRREIIGALMCNGVLDIPALEARHGIRFGTAFAPELADLAALGADGLVQCAPDRITVTPLGRLLVRRVAMVFDRYLREDAARPASTGAQAVAANDGAQPVRFVPRARYSRVV
|
Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.
|
O34313
|
NTPES_BACSU
|
Trifunctional nucleotide phosphoesterase protein YfkN [Includes: 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase (EC 3.1.3.6) (EC 3.1.4.16); 5'-nucleotidase (EC 3.1.3.5)]
|
MRIQKRRTHVENILRILLPPIMILSLILPTPPIHAEESAAPQVHLSILATTDIHANMMDYDYYSDKETADFGLARTAQLIQKHREQNPNTLLVDNGDLIQGNPLGEYAVKYQKDDIISGTKTHPIISVMNALKYDAGTLGNHEFNYGLDFLDGTIKGADFPIVNANVKTTSGENRYTPYVINEKTLIDENGNEQKVKVGYIGFVPPQIMTWDKKNLEGQVQVQDIVESANETIPKMKAEGADVIIALAHTGIEKQAQSSGAENAVFDLATKTKGIDAIISGHQHGLFPSAEYAGVAQFNVEKGTINGIPVVMPSSWGKYLGVIDLKLEKADGSWKVADSKGSIESIAGNVTSRNETVTNTIQQTHQNTLEYVRKPVGKTEADINSFFAQVKDDPSIQIVTDAQKWYAEKEMKDTEYKNLPILSAGAPFKAGGRNGANYYTNIPAGDLAIKNVGDLYLYDNTVQIVKLTGSEVKDWLEMSAGQFNQIDPAKGGDQALLNENFRSYNFDVIDGVTYQVDVTKPAKYNENGKVINADSSRIINLSYEGKPISPSQEFLVVTNNYRASGGGGFPHLTSDKIVHGSAVENRQVLMDYIIEQKTVNPKADNNWSIAPVSGTNLTFESSLLAKPFADKADDVAYVGKSANEGYGVYKLQFDDDSNPDPPKDGLWDLTVMHTNDTHAHLDDAARRMTKINEVRSETNHNILLDAGDVFSGDLYFTKWNGLADLKMMNMMGYDAMTFGNHEFDKGPTVLSDFLSGNSATVDPANRYHFEAPEFPIVSANVDVSNEPKLKSFVKKPQTFTAGEKKEAGIHPYILLDVDGEKVAVFGLTTEDTATTSSPGKSIVFNDAFETAQNTVKAIQEEEKVNKIIALTHIGHNRDLELAKKVKGIDLIIGGHTHTLVDKMEVVNNEEPTIVAQAKEYGQFLGRVDVAFDEKGVVQTDKSNLSVLPIDEHTEENPEAKQELDQFKNELEDVKNEKVGYTDVALDGQREHVRTKETNLGNFIADGMLAKAKEAAGARIAITNGGGIRAGIDKGDITLGEVLNVMPFGNTLYVADLTGKQIKEALEQGLSNVENGGGAFPQVAGIEYTFTLNNKPGHRVLEVKIESPNGDKVAINTDDTYRVATNNFVGAGGDGYSVFTEASHGEDLGYVDYEIFTEQLKKLGNKVSPKVEGRIKEVFLPTKQKDGSWTLDEDKFAIYAKNANTPFVYYGIHEGSQEKPINLKVKKDQVKLLKERESDPSLTMFNYWYSMKMPMANLKTADTAIGIKSTGELDVSLSDVYDFTVKQKGKEIKSFKEPVQLSLRMFDIEEAHNPAIYHVDRKKKAFTKTGHGSVDDDMVTGYTNHFSEYTILNSGSNNKPPAFPSDQPTGGDDGNHGGGSDKPGGKQPTDGNGGNDTPPGTQPTNGSGGNGSGGSGTDGPAGGLLPDTATSMYSILLAGFLISALGTAMYLHQRRKQNRANQA
|
Catalyzes the release of inorganic phosphate from 2',3'-cyclic nucleotides through consecutive 2',3'-phosphodiesterase and 3'- (or 2') nucleotidase activities. Also possesses a 5'-nucleotidase activity. Does not catalyze the release of inorganic phosphate from 3',5'-cyclic nucleotides. Probably plays a role in the cellular reprocessing of nucleotides present in the medium, under conditions of phosphate shortage.
|
O34327
|
RAPJ_BACSU
|
Response regulator aspartate phosphatase J (EC 3.1.3.-)
|
MRAKIPSEEVAVKLNEWYKLIRAFEADQAEALKQEIEYDLEDMEENQDLLLYFSLMEFRHRIMLDKLMPVKDSDTKPPFSDMLNEIESNQQKLTGLLEYYFYYFRGMYEFKQKNFILAIDHYKHAEEKLEYVEDEIEKAEFLFKVAEVYYHIKQTYFSMNYASQALDIYTKYELYGRRRVQCEFIIAGNLTDVYHHEKALTHLCSALEHARQLEEAYMIAAAYYNVGHCKYSLGDYKEAEGYFKTAAAIFEEHNFQQAVQAVFSLTHIYCKEGKYDKAVEAYDRGIKSAAEWEDDMYLTKFRLIHELYLGSGDLNVLTECFDLLESRQLLADAEDLLHDTAERFNQLEHYESAAFFYRRLMNIKKKLAEQRFQ
|
Involved in the regulation of sporulation (Probable). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity.
|
O34344
|
SDPC_BACSU
|
Sporulation delaying protein C (SdpC) (Cannibalism toxin SDP) (Killing factor SdpC) (Toxic peptide SdpC) [Cleaved into: Sporulation delaying protein (SDP)]
|
MKSKLLRLLIVSMVTILVFSLVGLSKESSTSAKENHTFSGEDYFRGLLFGQGEVGKLISNDLDPKLVKEANSTEGKKLVNDVVKFIKKDQPQYMDELKQSIDSKDPKKLIENMTKADQLIQKYAKKNENVKYSSNKVTPSCGLYAVCVAAGYLYVVGVNAVALQTAAAVTTAVWKYVAKYSSSASNNSDLEAAAAKTLKLIHQ
|
Produces a 42-residue extracellular sporulation delaying protein (SDP) that collapses the proton motive force (probably both the membrane potential and pH gradient) across the cell membrane, which leads to autolysis may form a proton channel. Induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, inducing cannibalism to provide a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation. Addition of SDP to liquid cultures halts growth, leads to increased cell permeability and eventually cell lysis in a significant subset of the population, although some cells survive and resume growth after a lag period. Effects of SDP are irreversible within 10 minutes. Addition of SDP to solid cultures induces killing, it is much more effective than SKF (AC O31422). Has antibiotic action against Gram-positive Firmicutes (L.acidophilus, M.megaterium, P.polymyxa, S.aureus, S.epidermidis) but not Actinobacteria M.luteus or Gram-negative P.aeruginosa or K.pneumoniae. SDP induces expression of the sdpR-sdpI operon. Its maturation is dependent on SdpA and SdpB. Also functions as a ligand, binds to SdpI triggering a signal transduction cascade that protects the cell against the toxic effects of its own SDP.
|
O34398
|
LIGD_BACSU
|
Bifunctional non-homologous end joining protein LigD (NHEJ DNA polymerase) [Includes: DNA ligase (Lig) (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]); DNA repair polymerase (Pol) (Polymerase/primase)]
|
MAFTMQPVLTSSPPIGAEWRYEVKYDGYRCILRIHSSGVTLTSRNGVELSSTFPEITQFAKTAFQHLEKELPLTLDGEIVCLVNPCRADFEHLQVRGRLKRPDKIQESANARPCCFLAFDLLERSGEDVTLLSYLDRKKSLRELISAAKLPASPDPYAKETIQSIPCYDHFDQLWEMVIKYDGEGIVAKKTNSKWLEKKRSSDWLKYKNFKQAYVCITGFNPNNGFLTVSVLKNGIMTPIASVSHGMRDEEKSAIREIMEQHGHQTPSGEFTLEPSICAAVQYLTILQGTLREVSFIGFEFQMDWTECTYAQVIRHSKPVHPKLQFTSLDKIIFEKNKKTKEDFIQYMIEVSDYLLPFLKNRAVTVIRYPHGSRSESFFQKNKPDYAPDFVQSFYDGSHEHIVCEDMSTLLWLCNQLALEFHVPFQTIKSRRPAEIVIDLDPPSRDDFLMAVQAANELKRLLDSFGITSYPKLSGNKGIQLYIPLSPEAFTYEETRQFTQLIAEYCTNAFPELFTTERLIKNRHCKLYLDYLQHAEGKTIICPYSTRGNELGTVAAPLYWHEVQSSLTPALFTIDTVIDRIKKQGCPFFDFYRNPQDEPLSAILHQLKKKS
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With Ku forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity (Probable). Probably involved in DNA repair during spore germination. The preference of the polymerase domain for rNTPs over dNTPs may be advantageous in dormant cells, where the dNTP pool may be limiting.
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O34403
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FPG_BACSU
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Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM) (AP lyase MutM) (EC 4.2.99.18)
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MPELPEVETVRRTLTGLVKGKTIKSVEIRWPNIIKRPAEPEEFARKLAGETIQSIGRRGKFLLFHLDHYVMVSHLRMEGKYGLHQAEEPDDKHVHVIFTMTDGTQLRYRDVRKFGTMHLFKPGEEAGELPLSQLGPEPDAEEFTSAYLKDRLAKTNRAVKTALLDQKTVVGLGNIYVDEALFRAGVHPETKANQLSDKTIKTLHAEIKNTLQEAIDAGGSTVRSYINSQGEIGMFQLQHFVYGKKDEPCKNCGTMISKIVVGGRGTHFCAKCQTKK
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Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base.
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O34425
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G3P2_BACSU
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Glyceraldehyde-3-phosphate dehydrogenase 2 (GAPDH) (EC 1.2.1.59) (NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase)
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MKVKVAINGFGRIGRMVFRKAMLDDQIQVVAINASYSAETLAHLIKYDTIHGRYDKEVVAGEDSLIVNGKKVLLLNSRDPKQLPWREYDIDIVVEATGKFNAKDKAMGHIEAGAKKVILTAPGKNEDVTIVMGVNEDQFDAERHVIISNASCTTNCLAPVVKVLDEEFGIESGLMTTVHAYTNDQKNIDNPHKDLRRARACGESIIPTTTGAAKALSLVLPHLKGKLHGLALRVPVPNVSLVDLVVDLKTDVTAEEVNEAFKRAAKTSMYGVLDYSDEPLVSTDYNTNPHSAVIDGLTTMVMEDRKVKVLAWYDNEWGYSCRVVDLIRHVAARMKHPSAV
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Involved in the gluconeogenesis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NADP. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NADP to NADPH. The reduced NADPH is then exchanged with the second NADP, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
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O34431
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ATCL_BACSU
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Calcium-transporting ATPase (EC 7.2.2.10) (Calcium pump)
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MKFHEMGQTDLLEATNTSMKQGLTEKEVKKRLDKHGPNELQEGKKTSALLLFFAQFKDFMVLVLLAATLISGFLGEYVDAVAIIAIVFVNGILGFFQERRAEQSLQALKELSTPHVMALREGSWTKIPSKELVPGDIVKFTSGDRIGADVRIVEARSLEIEESALTGESIPVVKHADKLKKPDVSLGDITNMAFMGTIVTRGSGVGVVVGTGMNTAMGKIADMLESAGTLSTPLQRRLEQLGKILIVVALLLTVLVVAVGVIQGHDLYSMFLAGVSLAVAAIPEGLPAIVTVALSLGVQRMIKQKSIVRKLPAVETLGCASIICSDKTGTMTQNKMTVTHVWSGGKTWRVAGAGYEPKGSFTLNEKEISVNEHKPLQQMLLFGALCNNSNIEKRDGEYVLDGDPTEGALLTAARKGGFSKEFVESNYRVIEEFPFDSARKMMTVIVENQDRKRYIITKGAPDVLMQRSSRIYYDGSAALFSNERKAETEAVLRHLASQALRTIAVAYRPIKAGETPSMEQAEKDLTMLGLSGIIDPPRPEVRQAIKECREAGIKTVMITGDHVETAKAIAKDLRLLPKSGKIMDGKMLNELSQEELSHVVEDVYVFARVSPEHKLKIVKAYQENGHIVAMTGDGVNDAPAIKQADIGVSMGITGTDVAKEASSLVLVDDNFATIKSAIKEGRNIYENIRKFIRYLLASNVGEILVMLFAMLLALPLPLVPIQILWVNLVTDGLPAMALGMDQPEGDVMKRKPRHPKEGVFARKLGWKVVSRGFLIGVATILAFIIVYHRNPENLAYAQTIAFATLVLAQLIHVFDCRSETSVFSRNPFQNLYLIGAVLSSILLMLVVIYYPPLQPIFHTVAITPGDWMLVIGMSAIPTFLLAGSLLTRKK
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This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium.
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O34450
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NAGA_BACSU
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N-acetylglucosamine-6-phosphate deacetylase (GlcNAc 6-P deacetylase) (EC 3.5.1.25)
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MAESLLIKDIAIVTENEVIKNGYVGINDGKISTVSTERPKEPYSKEIQAPADSVLLPGMIDIHIHGGYGADTMDASFSTLDIMSSRLPEEGTTSFLATTITQEHGNISQALVNAREWKAAEESSLLGAELLGIHLEGPFVSPKRAGAQPKEWIRPSDVELFKKWQQEAGGLIKIVTLAPEEDQHFELIRHLKDESIIASMGHTDADSALLSDAAKAGASHMTHLYNAMSPFHHREPGVIGTALAHDGFVTELIADGIHSHPLAAKLAFLAKGSSKLILITDSMRAKGLKDGVYEFGGQSVTVRGRTALLSDGTLAGSILKMNEGARHMREFTNCSWTDIANITSENAAKQLGIFDRKGSVTVGKDADLVIVSSDCEVILTICRGNIAFISKEADQI
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Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate.
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O34483
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HPRK_BACSU
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HPr kinase/phosphorylase (HPrK/P) (EC 2.7.11.-) (EC 2.7.4.-) (HPr kinase/phosphatase) (HPr(Ser) kinase/phosphorylase)
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MAKVRTKDVMEQFNLELISGEEGINRPITMSDLSRPGIEIAGYFTYYPRERVQLLGKTELSFFEQLPEEEKKQRMDSLCTDVTPAIILSRDMPIPQELIDASEKNGVPVLRSPLKTTRLSSRLTNFLESRLAPTTAIHGVLVDIYGVGVLITGKSGVGKSETALELVKRGHRLVADDCVEIRQEDQDTLVGNAPELIEHLLEIRGLGIINVMTLFGAGAVRSNKRITIVMNLELWEQGKQYDRLGLEEETMKIIDTEITKLTIPVRPGRNLAVIIEVAAMNFRLKRMGLNAAEQFTNKLADVIEDGEQEE
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Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of 'Ser-45' in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Also phosphorylates/dephosphorylates the HPr-like catabolite repression protein crh on 'Ser-46'. Therefore, by controlling the phosphorylation state of HPr and crh, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.
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O34507
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PRKC_BACSU
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Serine/threonine-protein kinase PrkC (Ser/Thr-protein kinase PrkC) (EC 2.7.11.1)
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MLIGKRISGRYQILRVIGGGGMANVYLAEDIILDREVAIKILRFDYANDNEFIRRFRREAQSASSLDHPNIVSIYDLGEEDDIYYIVMEYVEGMTLKEYITANGPLHPKEALNIMEQIVSAIAHAHQNQIVHRDIKPHNILIDHMGNIKVTDFGIATALSSTTITHTNSVLGSVHYLSPEQARGGLATKKSDIYALGIVLFELLTGRIPFDGESAVSIALKHLQAETPSAKRWNPSVPQSVENIILKATAKDPFHRYETAEDMEADIKTAFDADRLNEKRFTIQEDEEMTKAIPIIKDEELAKAAGEKEAEVTTAQENKTKKNGKRKKWPWVLLTICLVFITAGILAVTVFPSLFMPKDVKIPDVSGMEYEKAAGLLEKEGLQVDSEVLEISDEKIEEGLMVKTDPKADTTVKEGATVTLYKSTGKAKTEIGDVTGQTVDQAKKALKDQGFNHVTVNEVNDEKNAGTVIDQNPSAGTELVPSEDQVKLTVSIGPEDITLRDLKTYSKEAASGYLEDNGLKLVEKEAYSDDVPEGQVVKQKPAAGTAVKPGNEVEVTFSLGPEKKPAKTVKEKVKIPYEPENEGDELQVQIAVDDADHSISDTYEEFKIKEPTERTIELKIEPGQKGYYQVMVNNKVVSYKTIEYPKDE
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Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA) the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests that they form a functional couple in vivo. Might also be involved in sporulation and biofilm formation. Does not seem to be involved in stress response.
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O34508
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AEEP_BACSU
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L-Ala-D/L-Glu epimerase (AE epimerase) (AEE) (EC 5.1.1.20)
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MKIIRIETSRIAVPLTKPFKTALRTVYTAESVIVRITYDSGAVGWGEAPPTLVITGDSMDSIESAIHHVLKPALLGKSLAGYEAILHDIQHLLTGNMSAKAAVEMALYDGWAQMCGLPLYQMLGGYRDTLETDYTVSVNSPEEMAADAENYLKQGFQTLKIKVGKDDIATDIARIQEIRKRVGSAVKLRLDANQGWRPKEAVTAIRKMEDAGLGIELVEQPVHKDDLAGLKKVTDATDTPIMADESVFTPRQAFEVLQTRSADLINIKLMKAGGISGAEKINAMAEACGVECMVGSMIETKLGITAAAHFAASKRNITRFDFDAPLMLKTDVFNGGITYSGSTISMPGKPGLGIIGAALLKGEKEQ
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Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has probably a role in the metabolism of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of the other Ala-X dipeptides L-Ala-L-Asp, L-Ala-L-Leu, L-Ala-L-Met, and L-Ala-L-Ser. Is not able to epimerize other L-Ala-X dipeptides. Is also active with L-Ser-L-Glu and, oddly, L-Pro-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala.
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O34513
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TMCAL_BACSU
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tRNA(Met) cytidine acetate ligase (EC 6.3.4.-)
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MKAVGLVVEYNPFHNGHLYHAQTAKLQTGCDTAVAVMSGHFLQRGEPAVVSKWARTKMALQSGVDLVIELPYLYAVQKADIFARGSVSILNELECEALFFGSENGDIKPFLETAQLIDEHKHILNDRIKEELKKGASYPAAAAIAFSSILHTESALDLSKPNNILGYQYVTSILTGGYPMKPYTTARISSDYHDADLPEGENHIASATSIRKAMIGQNLEACLRFLPAASARELAAYRKSFGLWHTPESYFSYLKYSLSTVTARELQQVYEVEEGLEHRIIRSIRKSSSYQEFMELLKTKRYTWTRLQRMNTHILTRTKKQDMQKLLDNDKAPYIRLLGMTKKGQAYLSEKKKALSVPLVSKLSSFSHPALDLDVKASRIYSLPIEEPLRTEFDLQEYGHAPIRYDEDEQHFLNV
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Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. {ECO:0000255|HAMAP-Rule:MF_01539, ECO:0000269|PubMed:30150682}.
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O34525
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SPPA_BACSU
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Putative signal peptide peptidase SppA (EC 3.4.21.-)
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MNAKRWIALVIALGIFGVSIIVSISMSFFESVKGAQTDLTSLTDESQEKTLENGSPSSKIAVLEVSGTIQDNGDSSSLLGADGYNHRTFLKNLERAKDDKTVKGIVLKVNSPGGGVYESAEIHKKLEEIKKETKKPIYVSMGSMAASGGYYISTAADKIFATPETLTGSLGVIMESVNYSKLADKLGISFETIKSGAHKDIMSPSREMTKEEKNIMQSMVDNSYEGFVDVISKGRGMPKAEVKKIADGRVYDGRQAKKLNLVDELGFYDDTITAMKKDHKDLKNASVISYEESFGLGSLFSMGANKMFKSEIDFLNMREILSQSGSPRMMYLYAK
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Digestion of cleaved signal peptides (By similarity). Required for efficient processing of precursors under conditions of hyper-secretion. Has a preference for leucine-rich substrate peptides. {ECO:0000250, ECO:0000269|PubMed:10455123}.
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O34527
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CYMR_BACSU
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HTH-type transcriptional regulator CymR (Cysteine metabolism repressor)
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MKISTKGRYGLTIMIELAKKHGEGPTSLKSIAQTNNLSEHYLEQLVSPLRNAGLVKSIRGAYGGYVLGSEPDAITAGDIIRVLEGPISPVEVLEDEEPAKRELWIRIRDAVKEVLDSTTLEDLASYTDGEQEAYMFYI
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Master repressor of cysteine metabolism in B.subtilis. Controls the expression of genes involved either in cysteine synthesis from sulfide (cysK), sulfonates (ssu), or methionine (mccAB) or in cystine uptake (tcyP). Activity of CymR is positively regulated by CysK in response to cysteine availability. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.
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O34530
|
RSGA_BACSU
|
Small ribosomal subunit biogenesis GTPase RsgA (EC 3.6.1.-) (Ribosome-associated GTPase CpgA)
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MPEGKIIKALSGFYYVLDESEDSDKVIQCRGRGIFRKNKITPLVGDYVVYQAENDKEGYLMEIKERTNELIRPPICNVDQAVLVFSAVQPSFSTALLDRFLVLVEANDIQPIICITKMDLIEDQDTEDTIQAYAEDYRNIGYDVYLTSSKDQDSLADIIPHFQDKTTVFAGQSGVGKSSLLNAISPELGLRTNEISEHLGRGKHTTRHVELIHTSGGLVADTPGFSSLEFTDIEEEELGYTFPDIREKSSSCKFRGCLHLKEPKCAVKQAVEDGELKQYRYDHYVEFMTEIKDRKPRY
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One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase with a low level of activity and slow catalytic turnover, does not act on ATP. GTPase activity is stimulated by the presence of 30S or 70S ribosomes, phosphorylation increases stimulation. Depletion results in increased sensitivity to protein synthesis inhibitors that block the peptide channel or peptidyl transferase center on the ribosome, suggesting this protein functions in conjunction with the ribosome in vivo. Decreasing levels of protein lead to an increase in free 30S and 50S ribosomal subunits and a decrease in assembled 70S ribosomes. Suggested to serve as a specific transcription factor for proteins involved in late stages of peptidoglycan synthesis.
|
O34539
|
NDPGT_BACSU
|
NDP-glycosyltransferase YjiC (EC 2.4.1.384) (UDP-glycosyltransferase YjiC)
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MKKYHISMINIPAYGHVNPTLALVEKLCEKGHRVTYATTEEFAPAVQQAGGEALIYHTSLNIDPKQIREMMEKNDAPLSLLKESLSILPQLEELYKDDQPDLIIYDFVALAGKLFAEKLNVPVIKLCSSYAQNESFQLGNEDMLKKIREAEAEFKAYLEQEKLPAVSFEQLAVPEALNIVFMPKSFQIQHETFDDRFCFVGPSLGERKEKESLLIDKDDRPLMLISLGTAFNAWPEFYKMCIKAFRDSSWQVIMSVGKTIDPESLEDIPANFTIRQSVPQLEVLEKADLFISHGGMNSTMEAMNAGVPLVVIPQMYEQELTANRVDELGLGVYLPKEEVTVSSLQEAVQAVSSDQELLSRVKNMQKDVKEAGGAERAAAEIEAFMKKSAVPQ
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Glycosyltransferase that can glycosylate a wide range of substrates, including various flavonoids, phenyl ketones, curcuminoid, lignins, zingerone, triterpenes, stilbene and anthraquinone, using UDP-glucose or ADP-glucose as sugar donor. It also exhibits O-, N- and S-glycosylation activities towards simple aromatics. In vivo, the broad acceptor tolerance of YjiC might function as a detoxification agent against exogenous xenobiotics to make the strain adaptable to the changeable environment (Probable).
|
O34559
|
URHG2_BACSU
|
Unsaturated rhamnogalacturonyl hydrolase YteR (URH) (EC 3.2.1.172)
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MGSMDQSIAVKSPLTYAEALANTIMNTYTVEELPPANRWHYHQGVFLCGVLRLWEATGEKRYFEYAKAYADLLIDDNGNLLFRRDELDAIQAGLILFPLYEQTKDERYVKAAKRLRSLYGTLNRTSEGGFWHKDGYPYQMWLDGLYMGGPFALKYANLKQETELFDQVVLQESLMRKHTKDAKTGLFYHAWDEAKKMPWANEETGCSPEFWARSIGWYVMSLADMIEELPKKHPNRHVWKNTLQDMIKSICRYQDKETGLWYQIVDKGDRSDNWLESSGSCLYMYAIAKGINKGYLDRAYETTLLKAYQGLIQHKTETSEDGAFLVKDICVGTSAGFYDYYVSRERSTNDLHGAGAFILAMTELEPLFRSAGK
|
Catalyzes the hydrolysis of unsaturated rhamnogalacturonan disaccharide to yield unsaturated D-galacturonic acid and L-rhamnose. It cannot act on unsaturated glucuronyl hydrolase (UGL) substrates containing unsaturated D-glucuronic acid at the non-reducing terminus, although the active pockets of YesR and UGL are very similar.
|
O34614
|
MNMM_BACSU
|
tRNA (mnm(5)s(2)U34)-methyltransferase (EC 2.1.1.61) (5-aminomethyl-2-thiouridine methyltransferase) (MnmC-like methyltransferase) (bsMnmM) (tRNA 5-(aminomethyl)-2-thiouridylate-methyltransferase)
|
MILKKILPYSKELLKMAAGEGDIVVDATMGNGHDTQFLAELVGENGHVYAFDIQESAVANTKERLGDMYQARTTLFHKSHDKIAESLPPETHGKVAAAVFNLGYLPGGDKSITTNGSSTIKAIEQLLSIMKDEGLIVLVVYHGHPEGKAEKNDVLEFCRDLDQQTARVLTYGFINQQNDPPFIVAIEKKAQISK
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Involved in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34.
|
O34676
|
KAMA_BACSU
|
L-lysine 2,3-aminomutase (LAM) (EC 5.4.3.2) (KAM)
|
MKNKWYKPKRHWKEIELWKDVPEEKWNDWLWQLTHTVRTLDDLKKVINLTEDEEEGVRISTKTIPLNITPYYASLMDPDNPRCPVRMQSVPLSEEMHKTKYDLEDPLHEDEDSPVPGLTHRYPDRVLFLVTNQCSMYCRYCTRRRFSGQIGMGVPKKQLDAAIAYIRETPEIRDCLISGGDGLLINDQILEYILKELRSIPHLEVIRIGTRAPVVFPQRITDHLCEILKKYHPVWLNTHFNTSIEMTEESVEACEKLVNAGVPVGNQAVVLAGINDSVPIMKKLMHDLVKIRVRPYYIYQCDLSEGIGHFRAPVSKGLEIIEGLRGHTSGYAVPTFVVDAPGGGGKIALQPNYVLSQSPDKVILRNFEGVITSYPEPENYIPNQADAYFESVFPETADKKEPIGLSAIFADKEVSFTPENVDRIKRREAYIANPEHETLKDRREKRDQLKEKKFLAQQKKQKETECGGDSS
|
Catalyzes the interconversion of L-alpha-lysine and L-beta-lysine.
|
O34680
|
YDIP_BACSU
|
Type II methyltransferase M2.BsuMI (M2.BsuMI) (EC 2.1.1.37) (BsuMI modification methylase subunit YdiP) (Cytosine-specific methyltransferase M2.BsuMI)
|
MKVVSLFSGIGGIELGLHQSGHTTEIFCEVDPLAKAVLSKNFPGVKIEDDINEIRELPSCDLVAAGFPCQDLSQAGGKEGIDGSRSGLVKKLFELIEKKEHANRPPWILIENVPYMLRLNRGKAMSYLTSVLSELGYTWAYRTVDARCFGLPQRRHRVILLASLFEDPKDVIFSQDHSEPDLDGKPSVVDHSNYYGFYWTEGLRGVGWAREAVPPIKCGSSVGIASPPAVWSPYEDIVGTINIRDAERLQGFPEDWTNITTETGKDIKEGARWRLVGNAVSVRVSKWIGENLSQPKGSISDFEGELVTKTWPSAAWGYGDKKYKVPVSKWVANTEQIAISEFLNHPLKPLSARALNGFLGRAARCTNVNYSDEFINSLERCKDRQLQKV
|
A methylase, recognizes the double-stranded sequence 5'-YTCGAR-3', methylates C-3 on both strands, and protects the DNA from cleavage by the BsuMI endonuclease.
|
O34693
|
RQCH_BACSU
|
Rqc2 homolog RqcH (RqcH)
|
MSFDGMFTYGMTHELNEKIMGGRITKIHQPYKHDVIFHIRAKGKNQKLLLSAHPSYSRVHITAQAYENPSEPPMFCMLLRKHIEGGFIEKIEQAGLDRIMIFHIKSRNEIGDETVRKLYVEIMGRHSNIILTDAAENVIIDGLKHLSPSMNSYRTVLPGQDYKLPPAQDKISPLEASEDDILRHLSFQEGRLDKQIVDHFSGVSPLFAKEAVHRAGLANKVTLPKALLALFAEVKEHRFIPNITTVNGKEYFYLLELTHLKGEARRFDSLSELLDRFYFGKAERDRVKQQAQDLERFVVNERKKNANKIKKLEKTLEYSENAKEFQLYGELLTANLYMLKKGDKQAEVINYYDEESPTITIPLNPNKTPSENAQAYFTKYQKAKNSVAVVEEQIRLAQEEIEYFDQLIQQLSSASPRDISEIREELVEGKYLRPKQQKGQKKQKPHNPVLETYESTSGLTILVGKNNRQNEYLTTRVAARDDIWLHTKDIPGSHVVIRSSEPDEQTIMEAATIAAYFSKAKDSSSVPVDYTKIRHVKKPNGAKPGFVTYDSQHTVFVTPDADTVIKLKKS
|
Part of the ribosome quality control system (RQC). Recruits Ala-charged tRNA and directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal Ala extensions (Ala tail). The Ala tail promotes nascent chain degradation. Selectively binds tRNA(Ala)(UGC), which is presumably the sole source of tRNA(Ala) used for Ala tailing directed by this protein. May add between 1 and at least 8 Ala residues detection of the Ala tail requires either deletion of clpP or its inhibition. Binds to 50S ribosomal subunits, at least 30% of which contain a P-site tRNA and thus are obstructed.
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