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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Q9PGR1 | TRUB_XYLFA | tRNA pseudouridine synthase B (EC 5.4.99.25) (tRNA pseudouridine(55) synthase) (Psi55 synthase) (tRNA pseudouridylate synthase) (tRNA-uridine isomerase) | MLMSRIAYCRLDGILLLDKPAGISSNSALQIARRLLRAKKGGHTGSLDPLATGLLPLCFGEATKIAGLLLGSTKAYDADVLLGTTTTTDDAEGAVLLTRPVPTLDAEMVDAVIPQLIGRIRQRAPIYSALKQGGEPLYAKARRGEVVNAPVREVEVHAIELLVLATPRLQLRVTCGSGTYIRSLVRDLGEILGCGAHITALRRRWVAPFQIPKMLTLDALEQALSAGRDPDSLLLPLVEGLAGFPALELDAQRLACFRLGQRLRDHSFQTGRVAVFSRDGIPAGLGEVDSEGLLVPQRLFNL | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01080}. |
Q9PGR2 | RBFA_XYLFA | Ribosome-binding factor A | MPKKSFQRAERISVQIHRDLGALVQAAVRDHGLPSMSVSDVEVTRDMAHAKVFVTALQAERSFEAVAGLKALARELRMQLAHTMRLRFVPELHFHYDDSLDRGERINTLLRDLIPPADAEKDECG | One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal heli... |
Q9PGR3 | IF2_XYLFA | Translation initiation factor IF-2 | MSQQTTIRKLAELVNTPVEKLLEQLAGAGMKFSGPDQVVTSTEKMKLLGFLRRTHGKSDVSVGAVREAPKKITLNRRRLQEVTVNAGRNKTTVNVEVRQKRTYVKTPESEYHTPTKPPIELGDAERVEILRKLEESRQRNLAEQQRLAEVDRQRVEEQERKRLEEEQAELERQKTESPVVEEVPVQSDSNSVKPVSKPISEDRTRALPRAVRPAPAARPSVSRSDDRNSNSGVRHKPRGSHVIVSDEDDSARRFAGQMHLTAAERARRGSNTRGKGGGSHRGATHRGNENSIRSSGAHGFERPTAAVVREVAVGDTITVA... | One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. {ECO:0000255|HAMAP-Rule:MF_00100}. |
Q9PGR5 | RIMP_XYLFA | Ribosome maturation factor RimP | MSDKGIEIVNLLAPKVETLGFELLGAEYLLVPSGAILRLYIDTPFAMQPECMVSIDDCERVSREVSAYLDVEEPISGNYTLEVSSPGLDRRLFTLEQFARHYNQFVKVGLKLPQHGSRRLQGKIVRVEQVDGFVVLLVNGVELAVDFNNIDKARIVPDWSALGLAPLEKSKPDTKKTSQGNKKPSNESAARQAVRGVIR | Required for maturation of 30S ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_01077}. |
Q9PGT6 | TRPD_XYLFA | Anthranilate phosphoribosyltransferase (EC 2.4.2.18) | MSMTPQKALQCIIEHREILQDEMVQLMRQIMNAEVSGIMVAAILAGLRVKKETVGEIAGAATVMREFSRKVNVQDRTHLVDIVGTGGDGWHTFNISTCAMFVAAAAGAKVAKHGNRSVSSKSGSADVLEALGASIELQPLEVAEVIGCIGVGFMFAPIHHPVMQVVSPVRREMGVRTIFNILGPLTNPADAPNILMGVFDPDLVGIQAHVLHKLGAERALVVCGRDGMDELSLGTTTLVGELRGGRVREYEVSPEDYGMAVSPISNLQVESPAESREMLLDVLAGQPGPALDVVALNAGAALYVAGVAQDIGHGVALARE... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000255|HAMAP-Rule:MF_00211}. |
Q9PGU4 | DPO3A_XYLFA | DNA polymerase III subunit alpha (EC 2.7.7.7) | MSTSSFVHLHIHTEFSLADSTIRVPEKPEQAHPKKAKQANLLSRAVELGLPALAVTDLNNLFALIKFYKAAETVGIKPISGADLLIAEPEHTPWGMTLLCRDHAGYLNLSQLISRGWLEGHRPEGGVAVHPDWVRDHHKNLFALIGRHSLAGQLFAKGRADLAEQQLADWQHVFGNGLHLELTRTGRDGEEPFNQFALQVAGIRGIPVIASNDVRFLVPSDFLAHEARVCIASGRMLDDPKRPRTYSEQQYLRSSEEMAALFTDIPDALDNTRTLAQRCNIEMRLGTYFLPNYPVPNDETLDSWIRKQSHEGLEARLLKH... | DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity). |
Q9PGW5 | GCST_XYLFA | Aminomethyltransferase (EC 2.1.2.10) (Glycine cleavage system T protein) | MIKKTILNDTHRALGAKMVDFSGWEMPIHYGSQIDEHHHVRRNAGIFDVSHMTVIDLHGTQVRPLLRRLLANSVDKLKVPGKALYSCMLNPQGGVIDDLIVYYLREDYFRFIVNAATREKDLAWINTQASAFNVRVEERADLAMLAVQGPAARAQVTNLLAETHRDAVEKLGRFAALEVASHSKKILFISRTGYTGEDGFEILLPQEETITLWNALLKTGVKPIGLGARDTLRLEAGMNLYGQDMDEQVSPYEAALGWTVMLDEGRNFIGRNVLEQQKTNGVSRQMIGLLMDEKGVLRHGQKVLTAQGEGHILSGTFSPT... | The glycine cleavage system catalyzes the degradation of glycine. {ECO:0000255|HAMAP-Rule:MF_00259}. |
Q9PGW7 | GCSH_XYLFA | Glycine cleavage system H protein | MSDIPGDLKFLKSHEWVRIEDNNRAIVGISDHAQNLLGDLVYVELPNIGDHLDAGTTAAVIESVKAASDIYSPVTGKVIEVNTTLSDKPETINEDPYGEGWIMVIEMQAPEEISDLLSPDDYTKVLESDEH | The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. {ECO:0000255|HAMAP-Rule:MF_00272}. |
Q9PGX4 | RF3_XYLFA | Peptide chain release factor 3 (RF-3) | MSEVVAETARRRTFAIISHPDAGKTTLTEKLLLFGGAIQMAGSVKSRKAVRHATSDWMTLEKERGISVTSSVMQFPYEGKIINLLDTPGHADFGEDTYRVLTAVDSALMVIDVAKGVEERTIKLMEVCRLRDTPIMTFINKLDREGKNPIELLDEVERVLGIQCAPVTWPIGMGKRLRGVVNLLTNEVHLYEPGRNFTRQDSTIFTSLEAPGLAERIGEQMLADLHEELELIQGASACFDPTEYLGGRQTPVFFGSGVNNFGVQPLLDFFVEHAPSPQQRDTTSRVVLPTEEKLTGFVFKIQANMDPQHRDRVAFMRVCS... | Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP (By simi... |
Q9PGZ3 | PYRE_XYLFA | Orotate phosphoribosyltransferase (OPRT) (OPRTase) (EC 2.4.2.10) | MSHYRQRFLQLALDSNALCFGEFTLKSGRISPYFFNAGHFNSGAKTAALAQCYADAIDAANMNFDLVFGPAYKGIPLATALACEYARRERDLLLAFNRKEVKNHGEGGTLIGAPLNGRKILIIDDVITAGTAIREVLRIIRNAGGTPTGIAVALNRQEIASETNRQSSVQALMAETGIPVVAIATLSDLLAFVEENASLAKFYEPLLAYKTHYGTEASD | Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}. |
Q9PGZ6 | DUT_XYLFA | Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) | MSAAVQPLQIKILDPRLGTVWLLPTYATEASAGLDLRAALDAPMTLVPGDAELLSTGVAIHLVDPSLCAVVLPRSGLGHRHGIVLGNGTGLIDSDYQGPLLVSVWNRGREAFTIEPGDRIAQLVVLPIVRVVLQVVDTFVESGRGAGGFGHTGVR | This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00116}. |
Q9PH02 | SPEA_XYLFA | Biosynthetic arginine decarboxylase (ADC) (EC 4.1.1.19) | MTWSQDLAHKTYSILHWADGYFEVNDAGQMVVMPVGRDGVRISLPEVVDAARAAGAKLPLLLRFPDILGHRLGKLQAAFAQAQSEWEYAGGYTAVYPIKVNQHRGVAGVLASHQGDGFGLEAGSKPELMAVLALSRPGGLIVCNGYKDREYIRLALIGRKLGLKTFIVIEKPSELRMVLEEAKTLGVLPGLGVRVRLASLGAGKWQNSGGDKAKFGLSPRQVLDVWKVLRGTEYADCLNVMHFHMGSQISNVRDIAKGMREATRYFVELSRLGAKITHVDVGGGLGIDYEGTRSRSDCSINYGLQAYASHIVQPLASACE... | Catalyzes the biosynthesis of agmatine from arginine. {ECO:0000255|HAMAP-Rule:MF_01417}. |
Q9PH36 | RL19_XYLFA | Large ribosomal subunit protein bL19 (50S ribosomal protein L19) | MSKLNKSIIAEFESAQITRQVPQFSQGDTIVVNVKVKEGNRERLQAYEGVVIATKNAGLNSAFTVRKISHGYGVERVFQTHSPIIESIEIKRRGKVRAAKLYYLRGLEGKAARIKEDLAATAQEKLARKTVTAKAG | This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. {ECO:0000255|HAMAP-Rule:MF_00402}. |
Q9PH37 | TRMD_XYLFA | tRNA (guanine-N(1)-)-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase) | MRIDVISLFPEFITQCVGFGVIGRAQERGLLDLHNWNPRDYAQGNYRRVDDRPFGGGPGMVMLIEPLRACLEAVRAADPQPAPLIYLSPQGVLLNQSRARKLAMLPRMILLCGRYEGIDERFITHEVNMELSIGDYVLSGGELGAAVVVDAVIRLQEGVLNDAESAKQDSFEAVDSLLDYPHYTHPSNHAFGNVPEVLRSGNHVAITRWRRQQSLLRTWLRRPDLIDEARLSKADRLLLDEIKRTHPMDTDQKASVSWRGV | Specifically methylates guanosine-37 in various tRNAs. |
Q9PH38 | RIMM_XYLFA | Ribosome maturation factor RimM | MKDNERRILLGRVVGGFGLRGEIKIESWTEPRDAIFRYQPWLLRSPTGTESMLNGARGYETGKRLIATFPGINDRNAVEAICGTEIYVPRSALPPPHPDEYYWVDLEGLQVHTLEGVVLGSVSHLFSNGANDVIVIHGERERLIPFVQPDYVKSVDFEAERIVVDWDPEF | An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70... |
Q9PH57 | HFQ_XYLFA | RNA-binding protein Hfq | MAKGQSLQDPFLNALRRERVPVSIYLVNGIKLQGTIESFDQFVVLLRNTVSQMVYKHAISTVVPARNVRVGPGGGYVQSGSDTLQINDDEVE | RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. {ECO:0000255|HAMAP-Rule:MF_00436}. |
Q9PHA5 | MSCL_XYLFA | Large-conductance mechanosensitive channel | MSFIREFKEFVMRGNVIDLAVAVVIGAAFGKIVTALVDKIISPLIGVMVGGIDFSKLSLTLKAATVDAAGKEVPAVVIGYGDFLNTILQFIIIAFAIFIIVKMINKVINKQPLPPETPSEDVLLLREIRDSLKK | Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell. {ECO:0000255|HAMAP-Rule:MF_00115}. |
Q9PHE1 | RECF_XYLFA | DNA replication and repair protein RecF | MHITQLVLRHFRCFDAVDFFPLPGLNFFIGENGSGKTSLLEAVHLMGYGRSFRGRVRDGLIRHGSENLEIFVDWQETDLINARRRRAGLSHYGQEWIGRLDGQKIMHLATLCAALAVITFESSSYQLINSNAELRRRFLDWGLFHVEPDFLDLWRCYTHVLKQRNSLLKQKEELAMLEAWDQKLSEVGEQLTFRRFQYLERLKQRVIPLISRITPNLKIHGLNFNHGWRRHELPLIDALFISRERDYQYGYTSLGPHRSDWTPQFASIPGVHVLSRGQGKLITLMCLLAQAQDFFDQRGEWPILALDDLASELDQKHQWR... | The RecF protein is involved in DNA metabolism it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP (By similarity). |
Q9PHE3 | DNAA_XYLFA | Chromosomal replication initiator protein DnaA | MESWSRCLERLETEFPPEDVHTWLRPLQADQRGDSVVLYAPNPFIIELVEERYLGRLRELLSYFSGIREVVLAIGSRPKTTELPVPVDTTGRLSSTVPFNGNLDTHYNFDNFVEGRSNQLARAAAWQAAQKPGDRTHNPLLLYGGTGLGKTHLMFAAGNVMRQVNPTYKVMYLRSEQFFSAMIRALQDKSMDQFKRQFHQIDALLIDDIQFFAGKDRTQEEFFHTFNALFDGKQQIILTCDRYPREVNGLEPRLKSRLAWGLSVAIDPPDFETRAAIVLAKARERGATIPDEVAFLIAKKMHSNVRDLEGALNTLVARAN... | Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity). |
Q9PHK8 | RL9_CAMJE | Large ribosomal subunit protein bL9 (50S ribosomal protein L9) | MKVLLIKDVKALGKAGEIKEVKDGYGQNFLIAKGFAKAATNEVLRKYESDKKKEAENLRFEIANLEKLKEELSKITLEISKPVGANGSLFGGVTKDEIAHALKEQSHIEIDKKSLECDTLKSLGIHEVSVKLGHAIHAKFNINIKAE | Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00503}. |
Q9PHL0 | HSLU_CAMJE | ATP-dependent protease ATPase subunit HslU (Unfoldase HslU) | MNLTPKEIVKFLDDYVIGQKKAKKIIAIALRNRYRRMQLSPELQDDIVPKNILMIGSTGVGKTEIARRLAKMMGFPFIKIEASKYTEVGFVGRDVESMVRDLANAALNLVKNEQREKNKDKIDEFIENKILEKLLPPLPKGISDEKQEEYKNSLEKMRTKLRNGDLDESTIEIEISQNMFDTNPNLPPEMGAMQDIVKVIGVGSKKVKKEMKIKDAKNALKNEAGEKILDQESIKSEALKRAENEGIIFIDEIDKIAVSSGNSNRQDPSKEGVQRDLLPIVEGSNVQTKIGTLKTDHILFIAAGAFHLSKPSDLIPELQG... | ATPase subunit of a proteasome-like degradation complex this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before ... |
Q9PHL7 | ENGB_CAMJE | Probable GTP-binding protein EngB | MIISAKFITSLVKFDENLSSNFSEVAFLGRSNVGKSSLINSLCKQKNLAKSSATPGKTQLINFFEVICRRNEEKFNINFIDLPGFGYAKVSKNLKEIWNQNLDEFLKLRTSIKLFIHLIDSRHTHLEIDVNLNDYLKRFLRPDQKILKVFTKCDKLNQSEKAKLKNEFKDSILVSNLNKFGLDSLEDIIINQTLGLDK | Necessary for normal cell division and for the maintenance of normal septation. {ECO:0000255|HAMAP-Rule:MF_00321}. |
Q9PHM1 | RLPA_CAMJE | Endolytic peptidoglycan transglycosylase RlpA (EC 4.2.2.-) | MQIKTITLKLSAVSLGALFFSGCLGTSFFSSLDNAQVYYPSNDFKSSPSSSGTKGTMKPYTINGKTYYPTVVAVGETADGIASWYGPGFHGKKTSNGETYNQNALTAAHKTLPMNTILKVTNLNNNRQVTVRVNDRGPFVNNRIIDLSKGAASQIDMIASGTAPVRLEVIGFGSSNSGNNIVHSNVNYGNSGEIANNGQIYEGGNFMVQIGAFKNPAGAQTIAARYKTYRTYSSTIRTSSVDGLNRVFLTGFRSEDEARDFAASGAFAGAFVVRE | Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. {ECO:0000255|HAMAP-Rule:MF_02071}. |
Q9PHM5 | RECN_CAMJE | DNA repair protein RecN (Recombination protein N) | MINRIFMKENLGFKKAELEISKGLTVFTGLSGAGKSVLFKGILSAFSLSESEAKIVEIEVDDKLDLESFGIESEEENVFKLLKEKNTKYFINNQSIAKKSLQNLSKTFIKYLSAKENNEFGNEKFLNLLDALEMQENTNFVSFLEDFKKDFNAYSQISNELNAILEEEKKVEELKELARAQIEKISSINPKIGEYEELLILKKKLSKKDKLEEAWSKAERIFELEKVVIEALNLSEVDASFFSECLNELRVICENQKMEDLDFDVEALLDRIENLSYLIKRYESIENALEVLKQKKYELEHYENLSFEKKELEKKFQELK... | May be involved in recombinational repair of damaged DNA. |
Q9PHN0 | MSRA_CAMJE | Peptide methionine sulfoxide reductase MsrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) | MKNIVLGGGCFWCVEAVFERLKGVINTEVGYSGGKPNPSYESVCNGDGNIEVVKINYDEKQISLLEILTLFFKIHDPTSIDKQGGDIGIQYRSIIFYENEEDKILAQNFIEEQQKIFSKKIVTKISRLQTYYKAENYHQHYFINNPDQGYCQAVIAPKLQKIQSD | Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. {ECO:0000255|HAMAP-Rule:MF_01401}. |
Q9PHN2 | YQGF_CAMJE | Putative pre-16S rRNA nuclease (EC 3.1.-.-) | MRALALDVGLKRIGVALCIDKKIALPLDAVLRKNRNQAANEIKNLLKIHEISLLIVGIPKGGSSEEEMTRRIKHFVSLLEFDKEICFVDESGTSKEALGYGVANTRKKDGKLDSLSAFIMIKDYFAL | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00651}. |
Q9PHP0 | HYPA_CAMJE | Hydrogenase maturation factor HypA | MHELSIVESLIELCEENALNNKAYNVQEIYVKIGRLSGIEVDLFKRCFETFKENSNICKNAKLFIELAPLEILCLKCDQTSILEENVFKCPKCQSIEYKIIQGEDLHLMRLVMK | Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. {ECO:0000255|HAMAP-Rule:MF_00213}. |
Q9PHT5 | RPPH_CAMJE | RNA pyrophosphohydrolase (EC 3.6.1.-) ((Di)nucleoside polyphosphate hydrolase) | MENEKNYRPNVAAIVLSSSYPFECKIFIARRSDMDNIWQFPQGGIDKGESVKNALFRELKEEIGTDEVEIIAEYPEWLSYDFPSKIVKKMYPYDGQIQKYFLVRLKHGATININTKHPEFDDYQFVSVKQIFEMINHFKKNIYVRVIKYFEEKGYI | Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. {ECO:0000255|HAMAP-Rule:MF_00298}. |
Q9PHT7 | TATB_CAMJE | Sec-independent protein translocase protein TatB | MSFGEIIVILVVAILVLGPDKLPEAIVQIAKILKAVKRNIDDAKSSIEKEIRINDLKEEAKKYKDEFSSTNENIRKKLSFEEFDDLKRDILDKTKVDLTFDSRDDKVKNNLSGQNLNTEEKPNLSKLETQDKNGKINV | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that... |
Q9PHT8 | TATC_CAMJE | Sec-independent protein translocase protein TatC | MFEELRPHLIELRKRLFISVACIVVMFIVCFALRSYILDILKAPLIAVLPEVAKHVNVIEVQEALFTAMKVSFFAAFIFSLPVIFWQFWKFVAPGLYDNEKRLVVPFVSFASIMFAFGACFCYFVVVPLAFKFLINFGLNEDFNPVITIGTYVDFFTKVVVAFGLAFEMPVIAFFFAKIGLIDDSFLKRHFRIAVLVIFVFSAFMTPPDVLSQFLMAGPLCGLYGLSILIVQKVNPAPKDKESDE | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. {ECO:0000255|HAMAP-Rule:MF_00902}. |
Q9PHT9 | QUEA_CAMJE | S-adenosylmethionine:tRNA ribosyltransferase-isomerase (EC 2.4.99.17) (Queuosine biosynthesis protein QueA) | MNKDLLLSSYDYTLANELIANYPTNPKEDARLLVFDRKNKEIFHTTFKNLQDFLPNCAIFFNDTKVIKARIYGNKASGGKIELFLHQPFLNSHNPLFLAQIKGRIKKDEILYFKEDLKVRVVELLNDGLRKVQFFQNDKTLDTSNLYNLLDKIGHIPLPPYIKREDEKSDLKDYQSIFAKNLGAVAAPTASLHFSETMLENLRKKHEIYHLTLHVGAGTFKSVECENIQEHKMHSEFFNIPQQACEIIDSKQAILGVGTTVTRTIEYYTRTKTKNGFCDLFLHPQNPPIRQNHLLTNFHLPKSTLIMLVSAFIGREQCLK... | Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). {ECO:0000255|HAMAP-Rule:MF_00113}. |
Q9PHU0 | LPXD_CAMJE | UDP-3-O-acylglucosamine N-acyltransferase (EC 2.3.1.191) | MKLSEIAEFLSLEYKGEDIEISALNSLLKANFTELTYCDGEKNTKDIPHTGAAAILVSKEYENLVPKDTKALITQSPHLSFAFLSKLFAKPLISTAKEKVQNIAKSARIMPNVYIGDNVNIGENVIIMAGAYIGDNVSIGDESIIHPNVVIYNDTKIGKKCHLLANCVIGSDGFGYAHNKNGEHYKIYHNGNVVLEDFVEVGACTTIDRAVFDSTIIKAGTKVDNLVQIGHNCNIGQNCIIVAQTGISGSSELGRNVIMGGQSATSGHLKIGDFSTIAARGGVSKNLEGGRVYGGFPIMLQKDWLKLQAKIAINFKEKSQ... | Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00523}. |
Q9PHW3 | EFP_CAMJE | Elongation factor P (EF-P) | MASYSMGDLKKGLKIEIDGIPFKIVEYQHVKPGKGPAFVRIKIKSFIDGKVLEKTFHAGDKCEAPNLEDKTMQYLYDDGENCQFMDTQTYEQVAISDDDVGEAKKWMLDGMMVDVLFHNGKAIGVEVPQVVELKIIETAPNFKGDTQGSNKKPATLETGAVVQIPFHVLEGEVIRVDTVRGEYIERANK | Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. {ECO:00002... |
Q9PHX1 | SYP_CAMJE | Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS) | MMRFTKFYAPSLKEAPKDASLPSHIFLTRAGFVEQIGSGLYNFLPLGKRVLDKIKNIVKEEMDKAGAQEVNLSFITPASLWQESGRYNVFGKELLRFKDRKENEFVLGPTHEEAMLSLVKNKITSYKQLPLHLYQIGLKFRDEARPRFGLLRCREFLMKDGYSFHANEEDLGREFELMYKTYSQILQRMGLDFRAVEADSGAIGGSGSKEFMVLAKNGEDDILICENCDYAANVEAAKRAKKTCQDERPEANYASKFHTPNIKTIDSLAQFFKINAFYTIKAVVKKAIYENESKLVVFFIRGSDDLQEVKAQNTCSALEL... | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two addit... |
Q9PHY2 | MDH_CAMJE | Probable malate dehydrogenase (EC 1.1.1.37) | MKITVIGAGNVGSSVAYALILREIANEIVLVDINEDLLYAKELELTQSIAALNLNIDLLCTKDYTHTKNSDIVLFSAGFARKDGQSREELLQLNTSIMLDCAKKIKDFTEDPLFIILTNPVDFLLNTLYESGIFSSKKIIAMAGVLDNARFKYELAKKLNVKMSRVDTRLIGFHNDDMVLVKSYASVKNKNISEFLNEEEFEDLENEVKTGGAKVIKHLKTSAYLAPASACIRMLESIRSGEFLPMSVILHGEFGVQNKALGVMARLGLEGVIEIMKMDLSLQEKDKLEKSLIKYQYKGE | Catalyzes the reversible oxidation of malate to oxaloacetate. |
Q9PHZ3 | HTPG_CAMJE | Chaperone protein HtpG (Heat shock protein HtpG) (High temperature protein G) | MQFQTEVNQLLQLMIHSLYSNKEIFLRELISNASDALDKLNFLSVSDDKYKSLKFEPKIEIKIDKDKKTLSISDNGIGMDKDDLINNLGTIAKSGTKSFLENLSGDAKKDSQLIGQFGVGFYSAFMVASKIEVLSKKALDDKAYLWSSDANGYEIDDANKEEQGTSITLYLKDDEFANAYKIESIIEKYSNHIQFPIFMEKEEFTPAKEGEEEGKTELKISQINKANALWRMQKSSLKAEDYERFYEQNFHDSNKPLLYLHTKSEGKLEYNSLFFIPQNAPFDLFRVDYQSGLKLYVKRVFISDDDKELLPTYLRFVRGI... | Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-Rule:MF_00505}. |
Q9PHZ4 | FLUC_CAMJE | Fluoride-specific ion channel FluC | MLNTLLVVGFGGFIGAILRMLSINLVNKFFPYSISFGTLFVNVLGSFIIGLLFSYAQNKGLSPLLKSFISTGFLGAFTTFSTFSYQNLLLLQSGNYLHFALNIILNVFLCLFAAWLGFLIFK | Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. {ECO:0000255|HAMAP-Rule:MF_00454}. |
Q9PI02 | CLPB_CAMJE | Chaperone protein ClpB | MANIQDFLTDNMLSNLESAASLAIHSKNNEVVPLHLLWALSVDSTSILNQILNKLNISKEALELEIKSRISKLATSSNVNRENIRFSNELINSLENAKGLMSANGDSYLSVDTWLISESQKSPIKEILAQFLDLREFQKELESLRAGRKMDSKTSDETLDSLNKFGIDLTLKASEGKLDPVIGREEEIERLMQILIRKTKNNPILLGEPGVGKTAIVEALAQRIIKKDVPKSLQNKKVIALDMSALIAGAKYRGEFEDRLKAVVNEVIKSENIILFIDEIHTIVGAGASEGSMDAANILKPALARGELHTIGATTLKEYR... | Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity ATP hydrolysis unfolds the denatured protein aggregates... |
Q9PI04 | NTPP_CAMJE | Nucleoside triphosphate pyrophosphatase (EC 3.6.1.9) (Nucleotide pyrophosphatase) (Nucleotide PPase) | MLILASSSISRANLLKTAKIDFRQVSFDYDENLNKNISPFLYVQKIVLEKERQFLSTLGKDFQNQNLLFADSIVCIDEKILTKAKDKKEAYEMLALQNGKYASILSAFLLVKPEKRVFSLSKTTLYFKNFDENALRDYVENDLYKGKAGCIMCEGFHQNFITQQVGNLSTALGLDIQTLKAYL | Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. {ECO:0000255|HAMAP-Rule:MF_00528}. |
Q9PI16 | EFG_CAMJE | Elongation factor G (EF-G) | MSRSTPLKKVRNIGIAAHIDAGKTTTSERILFFTGMSHKIGEVHDGAATMDWMEQEKERGITITSAATTCFWKDHQINLIDTPGHVDFTIEVERSMRVLDGAVAVFCSVGGVQPQSETVWRQANKYGVPRIVFVNKMDRIGANFYNVEDQIRNRLKANPVPLQIPIGAEDNFKGVIDLVTMKALVWEDDTKPTDYVEKEIPAELKEKAEEYRTKMIEAVSETSDELMEKYLGGEELSLEEIKTGIKAGCLSLSIVPMLCGTAFKNKGVQPLLDAVVAYLPAPDEVANIKGEYEDGTEVSVKSTDDGEFAGLAFKIMTDPF... | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respective... |
Q9PI17 | RS7_CAMJE | Small ribosomal subunit protein uS7 (30S ribosomal protein S7) | MRRRKAPVREVLPDPIYGNKVITKFINSLMYDGKKSTATTIMYGALEAIDKKGGEKKGIDIFNDAIENIKPLLEVKSRRVGGATYQVPVEVRPARQQALAIRWIISFARKRSERTMIDKLAAELLDAANSKGASFKKKEDTYKMAEANKAFAHYRW | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. {ECO:0000255|HAMAP-Rule:MF_00480}. |
Q9PI18 | RS12_CAMJE | Small ribosomal subunit protein uS12 (30S ribosomal protein S12) | MPTINQLVRKERKKVLEKSKSPALKNCPQRRGVCTRVYTTTPKKPNSALRKVAKVRLTSGFEVISYIGGEGHNLQEHSIVLVRGGRVKDLPGVKYHIVRGALDTAGVAKRTVSRSKYGAKRPKAGAAK | With S4 and S5 plays an important role in translational accuracy. {ECO:0000255|HAMAP-Rule:MF_00403}. Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S su... |
Q9PI32 | RL7_CAMJE | Large ribosomal subunit protein bL12 (50S ribosomal protein L7/L12) | MAISKEDVLEYISNLSVLELSELVKEFEEKFGVSAAPVMVAGGAVAGGAVAAAEEKTEFDIVLTDGGAKKIEVIKIVRALTGLGLKEAKDAVEQTPSTLKEGVAKAEAEEAKKQLEEAGAKVELK | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. {ECO:0000255|HAMAP-Rule:MF_00368}. |
Q9PI33 | RL10_CAMJE | Large ribosomal subunit protein uL10 (50S ribosomal protein L10) | MTRSEKVEIIAKLEEGFKASEAIVVCNYRGLSTKKLEELRNNARENNVKVQIVKNTLANIALNNSGKTGLVLKDTNIYLWGEDQLSVSKVAAKFEENNDKFEIKTAHIEGEVADVAKVKALAKMPSRNELLAMLLQVWNAPITNFTIGLNALKNKKESE | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. |
Q9PI34 | RL1_CAMJE | Large ribosomal subunit protein uL1 (50S ribosomal protein L1) | MAKIAKRLKELSQKIDSNKEYALSDAIDTIKTLKSAKFDETVEIALKLNVDPRHADQMVRGSVVLPAGTGKKVRVAVIAKDAKADEAKNAGADIVGSDDLVEEIQKGNMNFDVLIATPNLMGLVGKVGRILGPKGLMPNPKTGTVTMDVAQAVNNAKSGQVNFRVDKQGNIHAGLGKVSFSKEQLWDNVSTFVKAINKHKPAAAKGRYIKNAALSLTMSPSVKLETQELLDMK | Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release. {ECO:0000255|HAMAP-Rule:MF_01318}. Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. {ECO:0000255|HAMAP-Rule:MF_01318}. |
Q9PI35 | RL11_CAMJE | Large ribosomal subunit protein uL11 (50S ribosomal protein L11) | MAKKVVGEIKLQIAATKANPSPPVGPALGQQGVNIMEFCKAFNERTKDMAGFNIPVVITVYADKSFTFITKQPPATDLIKKAAGISKGTDNPLKNKVGKLTRAQVLEIVDKKIADLNTKDRDQAAKIIAGSARSMGVEIVD | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. {ECO:0000255|HAMAP-Rule:MF_00736}. |
Q9PI36 | NUSG_CAMJE | Transcription termination/antitermination protein NusG | MSTHKWYAIQTYAGSEMAVKRAIENLVKDNGIEEQLKEIVVPTEDVIEFKNGKEKISERSLYSGYVFALLDLNTELWHRIQSLPKVGRFIGESKKPTPLTEKDINLILEKVHNRAAPKPKISFEEGENVRITEGPFANFTAIVEEYDMVRGLLKLNVSIFGRSTPVEILYSQVEKII | Participates in transcription elongation, termination and antitermination. {ECO:0000255|HAMAP-Rule:MF_00948}. |
Q9PI64 | ACP_CAMJE | Acyl carrier protein (ACP) | MATFDDVKAVVVEQLSIDADAVKMESKIIEDLGADSLDVVELIMALEEKFEVEIPDSDAEKLIKIEDVVNYIDNLKK | Carrier of the growing fatty acid chain in fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}. |
Q9PI98 | LGT_CAMJE | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase (EC 2.5.1.145) | MEFWQHIYSNFNVIAFSIFGLKVHWYGIMYVIALLLALLLAKFFVRKFQLDINEKHLDSYFIWVEIGVILGARLGYILIYDANTMYYITHPWQIFNPYINGEFVGIRGMSYHGAIIGFLIATLLFCKKYKTNPWIFLDLVALSVPLAYVFGRIGNFLNQELFGRITNVPWGIYVDGVLRHPSQLYEAFLEGIVVFIIVYLARFKQSFQGELILVYAGAYSLARFICEFYREPDFGIGFVLWGMSMGQILSFIMFITALLVYICIKFKKVNI | Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. {ECO:0000255|HAMAP-Rule:MF_01147}. |
Q9PIA5 | GATC_CAMJE | Glutamyl-tRNA(Gln) amidotransferase subunit C (Glu-ADT subunit C) (EC 6.3.5.-) | MQIDEKLLSKLEKLSALQITKNRNETIAQLSEIVNFVEKLNELDLDSQEITVSTIKGGAPLRIDEIRNSNVIDEVLDCAPKKQEHFFVVPKIIE | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated ... |
Q9PIB6 | DER_CAMJE | GTPase Der (GTP-binding protein EngA) | MQSIILIGKPNVGKSSLFNRMARQRIAITSDISGTTRDTNKTQIHIHSKKAMLIDSGGLDESDELFKNVKKNTLKVAKESDIILYLVDGKLAPDDEDRQFFYSLKKLGKPIALVINKVDNKKDEERAWEFANFGVKEIFNLSVTHNVGLDELYEWLEKFLHEEFLIPDEEENLEDFLEYYEEGKEFQFKEVDQNHIRVGIVGRVNVGKSSLLNALVKQERSVVSSIAGTTIDPVNESVVHKDKVIEFVDTAGIRKRGKIQGLERFALNRTEKILSHSQIALLVLDAHEGFNELDERIAGLVAKHYLGVIIVLNKWDKSEM... | GTPase that plays an essential role in the late steps of ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}. |
Q9PIB9 | RISB_CAMJE | 6,7-dimethyl-8-ribityllumazine synthase (DMRL synthase) (LS) (Lumazine synthase) (EC 2.5.1.78) | MNIIEGKLNLDSNTKIAIINARFNHIITDRLVEGAKDAFLRHGGKEENLSLILVPGAFELPYALKKAIESKKFDAICCVGAVIRGSTPHFDYVSAETTKGIANVSLNHNIPVSFGVLTTDTIEQAIERAGSKAGNKGFEAMTTVIEMLNLSKEL | Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}. |
Q9PIC0 | NUSB_CAMJE | Transcription antitermination protein NusB (Antitermination factor NusB) | MATRHQVRQSVISLLYAFELNSQNNVFVDEILDEKKIRNEQKNFTLNLYNGILDNLNNIDETLNSFLNDNQITALGHVERAILRLGAYELLFTDTPSAIVINEAIELAKELANDNSPKFINGVLDALIKAKK | Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons. {ECO:0000255|HAMAP-Rule:MF_00073}. |
Q9PIF1 | TRPA_CAMJE | Tryptophan synthase alpha chain (EC 4.2.1.20) | MVDFRKFYKENANVAYTVLGYPNLQTSEAFLQRLDQSPIDILELGVAYSDPIADGEIIADAAKIALDQGVDIHSVFELLARIKTKKALVFMVYYNLIFSYGLEKFVKKAKSLGICALIVPELSFEESDDLIKECERYNIALITLVSVTTPKERVKKLVKHAKGFIYLLASIGITGTKSVEEAILQDKVKEIRSFTNLPIFVGFGIQNNQDVKRMRKVADGVIVGTSIVKCFKQGNLDIIMKDIEEIFKK | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}. |
Q9PIF2 | TRPB_CAMJE | Tryptophan synthase beta chain (EC 4.2.1.20) | MKKAYYGDFGGQFLPESAMFALNELEGAFLKFSKDKLFKKELNELLKTYVGRPTPLYFARNLSKKYQHEIYLKREDLNHTGAHKINNAIAQALLAKKMGKKKIIAETGAGQHGLATATAAALLGLECEIYMGATDVQRQALNVYKMELLGAKIHAVQSGLKTLKEATTAAIQAWVGDIKNIFYVVGSAVGPYPYPKMVMHFQSIIGKECKMQLQKLNKKVDYIIAAVGGGSNAAGIFYDFIKDENVKLIGIEAGGLGIDTPYHAATLNKGKTGIIHGMKTKVLQDDLGNILPVHSVSAGLDYPGIGPLHAFLFESKRAQY... | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000255|HAMAP-Rule:MF_00133}. |
Q9PIH4 | EX7L_CAMJE | Exodeoxyribonuclease 7 large subunit (EC 3.1.11.6) (Exodeoxyribonuclease VII large subunit) (Exonuclease VII large subunit) | MTPTELNLKAKALLETHFDDIVLSGEISKITLHGSGHWYFDLKDERSSIACAMFKGANLKVGFKPAVGDFLELCGSVSLYPESGRYQFIATSMKKAGFGDLEAQFLALKERLQKEGLFDPRFKKSLPKFPKKVGIITSKTSAALQDMLKLIHQKEYFLAKIYIFDALTQGNNAPFSLIQALKKADDMDLDVLIIARGGGSREDLFCFNDENLAREIFKAKTPIISAIGHEIDYVISDFVADFRAPTPSAAIDTLFYSKLDIEQSLDLMEEKLMQLWNYKIQNYENLLLNLSKFFKFNSLPKIIDEKIKQSHNIEKQLNHL... | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. {ECO:0000255|HAMAP-Rule:MF_00378}. |
Q9PII7 | PTH_CAMJE | Peptidyl-tRNA hydrolase (PTH) (EC 3.1.1.29) | MILVVGLGNIGVEYENTRHNVGFMLIDLLLKESNFTNLTNSKFKGELFKIGSSLLLLKPSTYMNNSGLSVKAVNDFYKCERMIVIHDDIDINLGALRFKKGGSSGGHNGLKSIDTLCGNDYERVRIGVGKGENVISHVLGKFKSEEEITLSKVLEHAKKALLELIENDDLSAISSKYSLKA | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. {ECO:0000255|HAMAP-Rule:MF_00083}. |
Q9PII8 | RL25_CAMJE | Large ribosomal subunit protein bL25 (50S ribosomal protein L25) (General stress protein CTC) | MLEGIVRESIGRKAAKALKRDGYLIANIYGKGLENINAAFKVNEFIKEVRKKTTLIFDVKVGSQTLSVVVVDYQKDPVTAELKHVDLKVAQKGVISKYMVPVKITGTAIGLKNKGVLIQSKRRLKVKCAAENLPNFFELDVSKLDVGDALLVRDIVVPAGVTMIDADRVAVVGVEKAR | This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. {ECO:0000255|HAMAP-Rule:MF_01334}. |
Q9PIK6 | SURE_CAMJE | 5'-nucleotidase SurE (EC 3.1.3.5) (Nucleoside 5'-monophosphate phosphohydrolase) | MKEILITNDDGYESEGLKKLIKMLTKEFKAKITIVAPASEKSACSHSITLTKPLRFVKVGKRFYKLDDGTPADCVYLALHALYKKRLPDLVISGINKGANVGEDITYSGTCAGAMEAVLQGIPAIALSQFYKKSEKELDYKNALQITKKIIQNIFDKGFPLEKKEFLNINFPAKSKIKGIKICKAGKRVYNFEAHSNVNPRGVEYYWLAAANLDFEDEKNSDIALLKKGYATITPIMLDLTAYERMKKVKKWLKANDE | Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. {ECO:0000255|HAMAP-Rule:MF_00060}. |
Q9PIK8 | LPXB_CAMJE | Lipid-A-disaccharide synthase (EC 2.4.1.182) | MKTFLVCALEPSANLHLKEVLKAYKKDFGEFELHGIYDESLCKEFDLNSKPLYSSHEFSAMGFIEVLPLIFKAKKAIKELANLSFTQKINGILCIDSPAFNIPFAKALKKAGSKIPRIYYILPQVWAWKKGRIPIIESHFDILASILPFDNQFFNKSTYIGHPLLDEIKEFKNQEDINHTFSKKDDEKTIAFLPGSRRSEIRRLMPIFKELSQKFKGKKILCVPSFNLEKLEVYGDISEFKIESNTPKVLKKADFAFICSGTATLEAALVGTPFVLAYKAKAIDIFIAKLFVKLKHIGLANIFCDFAGKEALNPEFLQDK... | Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. |
Q9PIK9 | GREA_CAMJE | Transcription elongation factor GreA (Transcript cleavage factor GreA) | MQKEPMSQFGYDKLAAELKDLKDNQRPAVVIEIDTARSHGDLKENAEYHAAREKQALIESRIAELSDLLARAQVIDPSSYEHDSVKFGSSVVIMDLDTEKESKYTLVGICEGNLDKGYISIASPIAKAMLGKKEGDDFKVRLPKGESEFEILSINYEPLKF | Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factor... |
Q9PIL5 | TAL_CAMJE | Transaldolase (EC 2.2.1.2) | MKNFSLWCDFIENSFLDNEFLNLLSHGINGATSNPAIFKNAILNSPIYKDKILKLKEKKTKDIYEELAISDIQKAADKLAPLFYQKNDGFISIEIDPRLHDNTTLSLGEAKRLYSAIGKENIMIKIPATKASYEVMYELMKNGISVNATLIFSLEQSQKCFEALNAGLVEFRKNNIALKEQNTRTPQAVISIFVSRFDRLLNPKAKEQNRIGILNANLAYNNIYSKNEPNIRALFASTGVKGDDLPKDYYIKELLFENSVNTAPLDAIEAFKGKMHFKKPLMNFEIYTELNQIISQSEREKACNDLLSDGLEQFCIAFED... | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. |
Q9PIM0 | CLPX_CAMJE | ATP-dependent Clp protease ATP-binding subunit ClpX | MEFLSIGVKIMPRKCSFCNEVENPQRRILANENDDAFICEYCVEGAYSIIYGEEKEFKEPKQSHNTEFKDITPKELKAYLDRYVIGQDRAKKVFSVGVYNHYKRLFKAELQDDDTELFKSNILLVGPTGSGKTLLAQTLAKFLDVPIAICDATSLTEAGYVGEDVENILTRLLQAADGDVQRAQKGIVFIDEIDKIARMSENRSITRDVSGEGVQQALLKIIEGSLVNIPPRGGRKHPNQEFIQIDTSNILFVCGGAFDGLETILKRKLGDKVVGFFDDAKEENKALLEKIEPDDLVHFGLIPELIGRLHVIASLNELNE... | ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. {ECO:0000255|HAMAP-Rule:MF_00175}. |
Q9PIM1 | LPXA_CAMJE | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (UDP-N-acetylglucosamine acyltransferase) (EC 2.3.1.129) | MKKIHPSAVIEEGAQLGDDVVIEAYAYVSKDAKIGNNVVIKQGARILSDTTIGDHSRVFSYAIVGDIPQDISYKEEQKSGVVIGKNATIREFATINSGTAKGDGFTRIGDNAFIMAYCHIAHDCLLGNNIILANNATLAGHVELGDFTVVGGLTPIHQFVKVGEGCMIAGASALSQDIVPFCLAEGNRASIRSLNLVGIRRRFDKDEVDRLSRAFKTLFRQGDLKENAKNLLENQESENVKKMCHFILETKRGIPVYRGKNNA | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}. |
Q9PIN2 | ZUPT_CAMJE | Zinc transporter ZupT | MQFTFEQIFIAMLLTLFAGFSTAIGSIIAFFSRKDDLRVLSLGLGFSAGVMIYISFMEILPTALKDFKNHYDSHWAELLGLACFFGGILISLLIDKLIPEDVNPHEPKEDLSELKICPLPQKGQNPPKFHPGEKLHQINTKALKRTGIFTALAIAIHNFPEGFATFISSLDNLTLGIAIAIAVAIHNIPEGLAVSLPIYHATGDKKKAFIYSALSGFAEPLGAFVGALILLPFIGDLTLAISFAVIAGIMVFISLDELLPAAKTYDKAHDSLYGLIAGMAIMALSLNLLGQ | Mediates zinc uptake. May also transport other divalent cations. {ECO:0000255|HAMAP-Rule:MF_00548}. |
Q9PIQ0 | RL20_CAMJE | Large ribosomal subunit protein bL20 (50S ribosomal protein L20) | MARVKTGVVRRRRHKKVLKLARGFYSGRRKHFRKAKEQLERSLVYAYRDRRRKKRDFRRLWIVRINAACRLNDLSYSRFINGLKKAGIELDRKILADLAMNDAAAFAKIAEAAKKAL | Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. {ECO:0000255|HAMAP-Rule:MF_00382}. |
Q9PIQ3 | HEMTB_CAMJE | Bacteriohemerythrin | MTYNEKIISMNNDLLDHQHKELFEISKKLSLMNQRHVGTKELKIVLRELLIMINRHFSDEEAFMREIEYPYINHHTRIHRKIILEIEEIIISEAKFVNIMTEKLNLVVQDFIFKHTAKEDSKIVKYYEEKFKK | Oxygen-binding protein. May be involved in a storage mechanism or for delivery to oxygen-requiring enzymes. The oxygen-binding site contains two iron atoms. {ECO:0000255|HAMAP-Rule:MF_00556}. |
Q9PIR0 | RRF_CAMJE | Ribosome-recycling factor (RRF) (Ribosome-releasing factor) | MLNEIFNKQKTQSEKSLEALKKDFTTLRTGKVNIHILDHITVDYYGTQTPLNQVATVLASDASTISITPWEKPLLKTIESAIAAANIGVNPNNDGESVKLFFPPMTREQREENVKQAKAMGEKAKVSIRNIRKDANDAVKKLEKDKAISEDEAKKAYDEVQKLTDTYTTKIDEGVKSKESELLKV | Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another. {ECO:0000255|HAMAP-Rule:MF_00040}. |
Q9PIS2 | IF3_CAMJE | Translation initiation factor IF-3 | MSKEKEVLLNEEIRADEIRCVGDDGKVYGIISSDEALEIANRLGLDLVMIAADAKPPVCKIMDYGKFRYQQEKKQKEAKKKQKVIDIKEIKLSVKIAQNDINYKVKHALEFLEQGKHVRFRVFLKGREMATPEAGVALLEKIWTMIENEANRDKEPNFEGRYVNMLVTPKKA | IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins. {ECO:0000255|HAMAP-Rule:MF_00080}. |
Q9PIT8 | DEF_CAMJE | Peptide deformylase (PDF) (EC 3.5.1.88) (Polypeptide deformylase) | MVRKIITYPNPRLFLNSEIVNKFDTELHTLLDDMYETMIASNGVGLAAIQVDIPLRVLLVNIFDENDEQKKEDLLEIINPEIIPLDEEMITCTEGCLSVPDFFEEVKRYNHILLKYQDRFGEFKELEAKGFLAVAIQHENDHLNGHLFIEKISFAKRQKFDKEFKKKKKNHKKEK | Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. {ECO:0000255|HAMAP-Rule:MF_00163}. |
Q9PIW1 | MNTP_CAMJE | Putative manganese efflux pump MntP | MDFYSLIFLSCALGMDAFAVSLCKGFSVKKLHLKHYLIVGIYFGGFQALMPTIGYFIGITFASFIASIDHWIAFILLSLIGLKMIKESLENENCDSNANQFGFKTMLALAIATSIDALAVGVSFAFLNVNLLLAIFLIGIITFILCIIALKIGNKFGIYLKNKAELLGGLVLIILGVKILIEHLFFD | Probably functions as a manganese efflux pump. {ECO:0000255|HAMAP-Rule:MF_01521}. |
Q9PIX2 | RL31_CAMJE | Large ribosomal subunit protein bL31 (50S ribosomal protein L31) | MKKEIHPEYVECKVSCACGNTFTTKSNKAELRVDICSNCHPFFTGSEKIVDAAGRVEKFKKKYAMQ | Binds the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00501}. |
Q9PIY9 | RIMP_CAMJE | Ribosome maturation factor RimP | MNLEALCKEAGLSFYDDELVSENGRKIYRIYVQKEGGVNLDDCARLSEILSPIFDVESPVNGEYFLEVSSPGLERKLSKIEHFAKSIGELVKITTNEKEKFEAKIIAVDDENITLENLENKEKTTINFNDIKKARTFVEW | Required for maturation of 30S ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_01077}. |
Q9PIZ0 | RBFA_CAMJE | Ribosome-binding factor A | MNPSEIKKLRTESILKELIPEALANLDDENLKNLCVVDVECKKGRYDAFVYLDKMFFNVHEQEKILSSLKKASRALQNYCMSEQGWYRCPNFHFKFDDRLEYQNHMDALFEKIKKDKNES | One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal heli... |
Q9PIZ1 | IF2_CAMJE | Translation initiation factor IF-2 | MAKIRIHEIAKELGYDSKEIIEKANELGLGIKTASNAVEPEIAAAIYEYIQTREIPEAFKKNIKTPTAKKPKKENIKEQEKLNESEKKEPKKEEKLKQEVKKEELKIEKENAKEEEKQEIIDAHKPQSLASATLAKRRGLVIVKKKKDEEEIQVKKEEVKNSNDISINNEERLSLKTMFSNADESLKKKKKEKKSFVASKKESTEKMNFLDEHDFGDISLDDEDEVVLPDFSVKEQEKPQNINKKQPNFIRQAVGNSAGFGFEGGIQRRSRKKPSKKIEKKEVEEVGSVAISKEIRVYEFADKIGKSTSEVISKLFMLGM... | One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. {ECO:0000255|HAMAP-Rule:MF_00100}. |
Q9PIZ3 | KHSE_CAMJE | Homoserine kinase (HK) (HSK) (EC 2.7.1.39) | MKILVPATSANLGPGFDCLGLSLKLFNETQIQKSGVFSISIGGEGSDNIFLKKNNIFVNIFYEIYEKLSGKKDNFRFIFQNNIPLSRGLGSSSAVIVGAIASAYYMSGFKVEKECILDEALIYENHPDNIAPATLGGFVCSLVEKNKVYSIKKEIDKDLAAVVVIPNLAMSTEQSRQALAKNLSFNDAVFNLSHASFLTACFLEKKYEFLKFASQDKLHEINRMKNLPELFEVQKFALENKALMSTLSGSGSSFFSLAFKDDALALAKKIQTKFKDFRVQYLEFDDNGFEIC | Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. {ECO:0000255|HAMAP-Rule:MF_00384}. |
Q9PJ01 | RLMH_CAMJE | Ribosomal RNA large subunit methyltransferase H (EC 2.1.1.177) (23S rRNA (pseudouridine1915-N3)-methyltransferase) (23S rRNA m3Psi1915 methyltransferase) (rRNA (pseudouridine-N3-)-methyltransferase RlmH) | MENNLQVNIFCIQKSDEFKTCSEKYSKLISKYATLKEINVFNKKIALAQNLNAIEAKKSYEEAFMPYKKGYCIALDEKGKDLTSIEFAKLIQDKNELSFFIGGAYGLREEFNQSLDFRLSLSKLTLAHQFVKTLLLEQIYRAFCINNNHPYHK | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00658}. |
Q9PJ06 | YBEY_CAMJE | Endoribonuclease YbeY (EC 3.1.-.-) | MILSDEKCDFLESIASFLSPKDVELVFVDSKEMQEINLEQRKQDKTTDVLSFPLENIDESLPLGSVVINVDLAKEKAKELGHSYEEEISLLFIHAMLHLLGFDHENDNGEMREKEKELIEHFNLPKSLIVRTLED | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00009}. |
Q9PJ14 | TOLB_CAMJE | Tol-Pal system protein TolB | MKKIVAIFLVFLGSLWAEDPVIDVVNSGVVLPKIIVKDNSNLSDENLKKSFYNIIVNDLKVSSNFEVVANATETSNYIFEYTLNKNGNTLSLNVKIKAGGSDKSEQTYTLNGLEQYPFLAHKSVKASVNALGLAPVDWMDHKILIARNSSSKKSQIIMADYTLTYQKVIVDGGLNLFPKWGNKEQTLFYYTAYDHDKPTLYRYDLNTNKASKILSSGGMVVASDVNVDGSKLLVTMAPKDQPDVYLYDLNTKNLTQLTNYSGIDVNGNFIGSDDSKVVFVSDRLGYPNIFMQDLNSNSAEQVVFHGRNNSAVSTYKDFLV... | Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. {ECO:0000255|HAMAP-Rule:MF_00671}. |
Q9PJ18 | ATPE_CAMJE | ATP synthase epsilon chain (ATP synthase F1 sector epsilon subunit) (F-ATPase epsilon subunit) | MNDLINFEIVTPLGVIYQGEVKSVTLPGSEGEFGVLKGHAALVSSLKSGVIDIEKADLNHELIAIDAGHAKVDEDKICVLAKGAVWVCGSDESEIEKNLAQAKDLIKSMSSDNAALAATFSKLDNARMH | Produces ATP from ADP in the presence of a proton gradient across the membrane. {ECO:0000255|HAMAP-Rule:MF_00530}. |
Q9PJ20 | ATPG_CAMJE | ATP synthase gamma chain (ATP synthase F1 sector gamma subunit) (F-ATPase gamma subunit) | MSNLKEIKRKIKSVHNTQKTTNAMKLVSTAKLKKAEEAAKRSKIYAQKIDEILSEISFQINKIVHNEDDVRLSLFHKKEQIKTVDLIFITADKGLCGGFNIKTLKTVSEMLKEYEAKNINIRLRAIGKTGIEYFNFQKIELLEKYFHLSSSPDYEKACEVIHAAVDDFLNGNTDEVILVHNGYKNMITQELKINHLIPVEPKSIEQTHNSLLELEPEGTELLKDLMKTYFEYNMYYALIDSLAAEHSARMQAMDNATNNAKARVKQLNLAYNKARQESITTELIEIISGVESMK | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. {ECO:0000255|HAMAP-Rule:MF_00815}. |
Q9PJ25 | PARB_CAMJE | Probable chromosome-partitioning protein ParB | MGLNKDRGLSSLISDMDTVYSKELGFDKNQSTMIEIDQISPNPFQPRKNFDQEALDELANSIKEFGLIQPIIVFKKNNKFILIAGERRLRAVKALGKKEILAFIADIDENKLRELALIENIQRENLNPIELANSYKDLMQVHKITQENLAELIHKSRTQITNTLRLLNLDIRTQELIASGKISQGHAKVLVGLDQKDEKMLVDSIIGQKLNVRDTEKIVKKIKNNESLPNQEFEDEIKKLKQILNRFGFDCKNKNNDFVIHLENIDKIKKLIKMLEKL | Involved in chromosome partition. Localize to both poles of the predivisional cell following completion of DNA replication. Binds to the DNA origin of replication (By similarity). |
Q9PJ28 | FMT_CAMJE | Methionyl-tRNA formyltransferase (EC 2.1.2.9) | MKKIIFMGTPSYATCILKALVENENFKLVALFTQPDKAVGRKQILTPSDTKAFLSQNYPSIPIFTPSSLKDKNIIREIKDLNPDFIVVAAYGKILPKAILDLAPCVNLHASLLPKYRGASPIQSAILNKDEKSGVCTMLMEEGLDTGAILESLECDIKDKNSSEVFELLANLAAKIILSTLLNFDKITPKKQEESLATLCRKIKKEDGLINLQNARELYQKYLAFTPWPGVFLENGLKFLELELVDELKQNAKMGEILELEKESFLLACKQGVLRIKKLQESGKKALDGRTYLNGKRLKSEDSLC | Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. {ECO:0000255|HAMAP-Rule:MF_00182}. |
Q9PJ40 | UNG_CAMJE | Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) | MEEITINIDKIKINDDWKEFLRDEFQKKYFLEIKKQYLNAINQNIIIYPPANLIFNAFNLCPLKEIKIIILGQDPYHQPNQAMGLSFSVPKNVKIPPSLNNIFKELQNDLNITPAKSGDLSSWAKQGVLLLNSILSVEANKAASHSSWGWQEFSDAIIHKLSNEKSGLVFMLWGNYAKNKEILIDNTKHLILKAAHPSPLARTGFLGCKHFSKANEFLKKVGKIPIDWKIV | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. {ECO:0000255|HAMAP-Rule:MF_00148}. |
Q9PJB0 | DNAA_CAMJE | Chromosomal replication initiator protein DnaA | MNPSQILENLKKELSENEYENYLSNLKFNEKQSKADLLVFNAPNELMAKFIQTKYGKKIAHFYEVQSGNKAIINIQAQSAKQSNKSTKIDIAHIKAQSTILNPSFTFESFVVGDSNKYAYGACKAIAHKDKLGKLYNPIFVYGPTGLGKTHLLQAVGNASLEMGKKVIYATSENFINDFTSNLKNGSLDKFHEKYRNCDVLLIDDVQFLGKTDKIQEEFFFIFNEIKNNDGQIIMTSDNPPNMLKGITERLKSRFAHGIIADITPPQLDTKIAIIRKKCEFNDINLSNDIINYIATSLGDNIREIEGIIISLNAYATILG... | Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity). |
Q9PJB6 | TRHO_CHLMU | tRNA uridine(34) hydroxylase (EC 1.14.-.-) (tRNA hydroxylation protein O) | MEKNYYALAYYYFGPVSNPHEEIALHKQLFKTMDVSCRIYISEEGINGQFSGYQPDAERYMAWLKQRPDFATVKFKIHHIKENVFPRVTVKYRKELVALGCSVDTSKQGKHISPEEWHEKLQENRCLVLDVRNNYEWKIGHFENAVLPDIETFREFPAYADRLAQEHAPETTPVMMYCTGGIRCELYSALLLEKGFKEVYQLDGGVIAYGLKMGTGKWKGKLFVFDDRMAVPINEADPNVSPISKCSLCDIESDTYYNCANTDCNNLFLCCESCITSQKGCCSEECSQAPRIRTFSAERGNKPFRRKHLCPTIEQTRCCL... | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. {ECO:0000255|HAMAP-Rule:MF_00469}. |
Q9PJB7 | RS4_CHLMU | Small ribosomal subunit protein uS4 (30S ribosomal protein S4) | MARYCGPKNRIARRFGANIFGRGRNPLLRKPNPPGQHGMQRKKKSDYGLQLEEKQKLKACYGMILEKQLVKAYKEVVHKQGNVAQMFLEKFECRLDNIVYRLGFAKTIFAAQQLVSHGHVLVNGKKVDRRSFFVRPGMQISLKEKSRRLAIVTESLENKDQSSLPAYLSLDKAAFKGELVVSPELDQISSQLPLPVNVSVICEFLSHRT | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01306}. With S5 and S12 plays an important role in translational accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}. |
Q9PJB8 | END4_CHLMU | Probable endonuclease 4 (EC 3.1.21.2) (Endodeoxyribonuclease IV) (Endonuclease IV) | MFVLPPPQEPLLGAHTSAAGGLHNALYEGRDIGATTIQLFTANQRQWKRRSLTQNMIEQFQTALDETSLSYIMSHAGYLNNPGAPNPEILEKTRICMYQEIADCIALGISFVNFHPGAALSDSKESCLDRAITSFSQMAPLFETNPPLVVLLETTAGQGSLIGSSFEELAYLIQGIKAHIPVGVCLDTCHIFAAGYDISSPEGWEQVLKHFDEVIGLSFLRAIHLNDSIFPLGKNKDRHAPIGEGCIGSESFCFLMRDERTRKLPKYLETPGGPDLWTKEIRYLQKVS | Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. {ECO:0000255|HAMAP-Rule:MF_00152}. |
Q9PJB9 | MURJ_CHLMU | Probable lipid II flippase MurJ | MSKDDEGSLVRSLFNLLSGTFFSRLTGMLREIVMATYFGADPLVASFWLAFRTIFFLRKLLGGPILGLAFIPHFEFLRAQNISRAAFFFRSFSKFFCYSAIVFTLVIELGLGVWCSCVTGSLFDTLLLTIILLPSGIFLMMYTVNSTLLHCEKKFLSVGLAPSVVNVLWIGTVFLARNYNPRNRIFGLAIVLVIGFILEWAVTLPGVIKFLGRSTETPKERDSIRALIAPLSLGLLSMGIFQLNLLCDMWLARYINEVGPLYLMYSVRIQQLPVHLFGLGVFTVLLPAISRCVQDNEHQQGYDLLRFSLKLTVAVMLVMT... | Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. |
Q9PJC4 | RS20_CHLMU | Small ribosomal subunit protein bS20 (30S ribosomal protein S20) | MAPRKPSKKVGPQKRPSAEKRVITSKKKQLRNQSFKSRVKTTLKKFELAVQSGDVASISAGLSSVYSIADKAVKRGIFKKGKADRVKARASGRACPTA | Binds directly to 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_00500}. |
Q9PJC6 | FOLB_CHLMU | Probable dihydroneopterin aldolase (DHNA) (EC 4.1.2.25) (7,8-dihydroneopterin aldolase) | MYRLDVTNFRVWVSIGVSEQERYHKQPILVSVSLVFREEPKVCSTDEISDGICYAALVSLIEQTAANHPCALLERLAKVLLEKLEESLAQFVCKIDLRVSKERPPIPNLLSPVSFSISKEVP | Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. |
Q9PJC9 | CADD_CHLMU | 4-aminobenzoate synthase (EC 1.3.3.-) (para-aminobenzoate synthase) (PABA synthase) | MESRKGIKEVSMNFLDQLDAIIQNKHMLEHPFYMKWSKGELTKEQLQAYAKDYYLHIKAFPKYLSAIHSRCDDLEARKLLLDNLMDEENGYPNHIDLWKQFVFALGVSSEELEAHEPSEAAKAKVATFMRWCTGDSLAAGVAALYSYESQIPCVAKEKIRGLIEYFGFSNPEDYAYFTEHEEADVRHAREEKALIEMLSRDDSDKVLEASREVTQSLYGFLDSFLEPATCCHCHKA | Involved in de novo para-aminobenzoate (PABA) biosynthesis. Acts as a self-sacrificing or 'suicide' enzyme that utilizes its own active site tyrosine residue(s) as the substrate for PABA synthesis. The side chain of the tyrosine residue is released from the protein backbone via cleavage of the C(alpha)-C(beta) bond, le... |
Q9PJD2 | UNG_CHLMU | Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) | MHEAFTIEQLPQSWQEQLKDEWSQPYWSQLLTFLKSEYANATVYPKKEHVFSALRSTPFDQVKVVILGQDPYHGEGQAHGLSFSVPKGQALPPSLRNIFQELQADLGIRNETGCLQTWADQGVLLLNTVLTVRAGEAFSHAGRGWEHFTDAIVTKLIQNRTHIIFVLWGSAARKKCDLLFQTKHQHAILACPHPSPLAAHRGFFGCCHFSKINYLLKKQGKPMINWKIA | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. |
Q9PJG0 | SAMHT_CHLMU | S-adenosylmethionine/S-adenosylhomocysteine transporter (SAM/SAH transporter) (SAMHT) | MMLVLRFANLYVEPMAIFLIFLNAFIWSSSFALSKSAMDAASPLFVTGSRMVLAGIVLFGLLLFKRESFRLPRQAVMPIVLLSVIGFYLTNVLEFIGLQGLSSSKACFIYGFSPFTAAFCSYVQLREVVTWKKLGGLSLGLVSYLVYLLFGGGEDVSEWGWQLGMPELLLIVATCLSSYGWTLLRKLERQCESLSITAINAYAMVIAGILSLAHSAITEVWNPLPVENPVLFLQSIGALVIFSNLICYNLFAKLLRSFSSTFLSFCNLVMPLFASFFGWLLLGESFPPGLLFAVGFMVLGCRLIYHEEFRQGYVLSSE | Transports S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH). Allows bacteria to acquire SAM from the eukaryotic host cell and to likely remove the toxic by-product SAH (By similarity). |
Q9PJG5 | MUTL_CHLMU | DNA mismatch repair protein MutL | MSLSSSRIRLLDSATVNQIAAGEVIENAASVVKELIENALDAGADEISIETLGGGKGQIVVRDNGIGMDADEVAVAIQRHATSKISHFADIFSLASFGFRGEALPAIASISKMEIHTAKVNGLGSKTLIEKGEPVCCEACPRQPGTTISVNSLFYNVPMRQSFQKSPQMDRLAIRRLLENSILSTEGIKWTWISERRQELNIAKNQGFTERVALVMGEAFVNEAFLIDKRQNELHLTGFLGSPSMHRSTRQGQRLFINNRAVESSFISRKVAEAYAWMLPAQRYPAFVLKLSVPPMWCDFNVHPQKTEVRLLQEGQIGAL... | This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part ... |
Q9PJJ7 | DPO3A_CHLMU | DNA polymerase III subunit alpha (EC 2.7.7.7) | MTWIPLHCHSQYSILDATCSIKKFVAKAVEYHIPALALTDHGNLFGAVDFYKTCKQNAIKPIIGCELYVAPSSRFDKKKERKSQVANHLILLCKDEEGYRNLCLLSSLAYTEGFYYFPRIDRELLKQHSKGLICLSACLSGSIAQAALESEEALEKDLLWYQDLFQEDFFSEVQLHKSSEEKIALFEEEWLRQNYYQFIEKQLKVKDAVLTVSKRLGISSVATNDIHYLDPDDWLAHEILLNVQSREPIRTAKQNTYVPNPKRKTYPSREFYFKSPQEMAELFADHPETISNTLIVADRCNLELDFVTKHYPIYVPEDLQ... | DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity). |
Q9PJJ8 | UHPT_CHLMU | Probable hexose phosphate transport protein | MNLWTKIFQPPRHIKEISDPELVKKQYKYWRVRIFYSMFFGYVFFYFTRKSFTFAMPTLIADLGFDKAQLGIIGSTLYITYGISKFVSGVMSDQSNPRYFMATGLIITGLSNIFFGLSSTVPLFVLFWGINGWFQGWGWPPCARLLTHWYSKSERGTWWSVWSTSHNIGGALIPVLTGIAIDYAGWRGAMFIPGIICIIMGFILIDRLRDTPQSLGLPAIEKFKKEDLSHPHEETTADILEEEAERELSTKEILFTYVLSNKWLWFLSFASFFIYVVRMAVNDWSALYLIETKNYSTVKANLCVSLFEIGGLFGMLLAGW... | Transport protein for sugar phosphate uptake. |
Q9PJK3 | THIO_CHLMU | Thioredoxin (Trx) | MVQIVSQDNFADSIASGLVLVDFFAEWCGPCKMLTPVLEALAAELPYVTILKLDIDASPRPAEQFGVSSIPTLILFKDGKEVERSVGLKDKDSLVKLISKHQ | Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. |
Q9PJL1 | LPXA_CHLMU | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (UDP-N-acetylglucosamine acyltransferase) (EC 2.3.1.129) | MTNIHPTAIVEDGAQIGNNVTIEPYAIVKKNVKLCDDVVVKSYAYIDGFTTIGRGTTIWPSAMIGNKPQDLKFKGEKTFVEIGEHCEIREFAMITSSTFEGTTVSIGNNCLIMPWAHIAHNCSVGNNVVFSTHVQLAGHVQVGDCVTIGSMVGVHQFVRIGSYAMVGAMSGIRRDIPPFTIGTGNPYALGGVNKVGLQRRRVPFETRLALIKTFKRVFRSGESFQDSLGSVLEDFGDVPEVRHFVEFCRQPSKRGIERGIDCEASLDEPIDKKEGAFVES | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}. |
Q9PJL2 | FMT_CHLMU | Methionyl-tRNA formyltransferase (EC 2.1.2.9) | MLNLRVVYLGTPQFAATVLETLVDARIHVVGVVTRADKPQKRSSKPIASPVKQLALSKNIPLLQPTKTTDPAFLAQLREWQADVFVVVAYGVILKQELLDIPKYGCYNLHAGLLPAYRGAAPIQRCIIAGETLSGNTVIRMDAGMDTGDIANVNHVAIGEDMTAGELAEALAGSGGELILKTLQEIEAGTVRHIPQDSAKATLAPKLTKEEGLVKWDAPASQVYAHIRGVSPAPGAWTRFLSQGKEPRRLGILSARMESSSGSHSPGEVLGVSGEDLLVACRQGVLRLCIVQPEGKVFMKAKDFFNGQSRSVALLF | Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. {ECO:0000255|HAMAP-Rule:MF_00182}. |
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