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UniProt_function_text_descriptions

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Q9ZJG8
YIDC_HELPJ
Membrane protein insertase YidC (Foldase YidC) (Membrane integrase YidC) (Membrane protein YidC)
MDKNNNNNLRLILAIALSFLFIALYSYFFQEPNKTTTETTKQETTNNHTATSPTASNTITQDFSVTQTIPQESLLSTISFEHAKIEIDSLGRIKQVYLKDKKYLTPKEKGFLEHVSHLFSSKENSQPSLKELPLLAADKLKPLEVRFLDPTLNNKAFNTPYSASKTTLGPNEQLVLTQDLGTLSIIKTLTFYDDLHYDLKIAFKSPNNLIPSYVITNGYRPVADLDSYTFSGVLLENTDKKIEKIEDKDAKEIKRFSNTLFLSSVDRYFTTLLFTKDPQGFEALIDSEIGTKNPLGFISLKNEANLHGYIGPKDYRSLKAISPMLTDVIEYGLITFFAKGVFVLLDYLYQFVGNWGWAIILLTIIVRIILYPLSYKGMVSMQKLKELAPKMKELQEKYKGEPQKLQAHMMQLYKKHGANPLGGCLPLILQIPVFFAIYRVLYNAVELKSSEWVLWIHDLSIMDPYFILPLLMGASMYWHQSVTPNTMTDPMQAKIFKLLPLLFTIFLITFPAGLVLYWTTHNILSVLQQLIINKVLENKKRAHAQNIKE
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. {ECO:0000255|HAMAP-Rule:MF_01810}.
Q9ZJH0
RNPA_HELPJ
Ribonuclease P protein component (RNase P protein) (RNaseP protein) (EC 3.1.26.5) (Protein C5)
MPDELRAEKSFPSKPYDSLKNKSEFDRVYRKGFKKHNPFFSLFVLDLSKEPPKEKEGFKDPLSCRLKDRNTLCLLGLSVSKKVGNAVKRNLIKRRLRSLVTRHAALCQGFALVFVPRSDCYHLDFWALEKHFLEMLTSIKDYMNKALKDLKKGMTHTHAKQ
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. {ECO:0000255|HAMAP-Rule:MF_00227}.
Q9ZJH2
SSRP_HELPJ
SsrA-binding protein (Small protein B)
MKLIASNKKAYFDYEILETLEAGLALLGSEVKALRQTRVNLKDNFVKIIKGEAFLFGVHISYLDTIHAYYKPNERRERKLLLHKKQLLKWQMEASKERLSIVGLKLYFNQKNRAKIQIALVKGKRLHDKRQSLKEKALNKEILADLKHHFKG
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation. {ECO:0000255|HAMAP-Rule:MF_00023}.
Q9ZJH4
CSRA_HELPJ
Translational regulator CsrA
MLILSRKVNEGIVIDDNIHIKVISIDRGSVRLGFEAPESTLILRTELKEAIVSENQKASASVDESLLENIKKVIKP
A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW. {ECO:0000255|HAMAP-Rule:MF_00167}.
Q9ZJH5
PPIA_HELPJ
Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Rotamase)
MKPIKTYDIKEEELAKTAYATIKTNKGNITLELFYKDAPQAVSNFVTLAKEGFYNGLNFHRVIAGFVAQGGCPYGTGTGGPEHRIKCEVAHNPNKHQRGSISMAHAGRDTGGSQFFLCFVDLPHLDGEHTVFGKITSAESLSVLDKIKQGDIIESVVFSPSL
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Q9ZJL5
FLIW2_HELPJ
Flagellar assembly factor FliW 2
MIFDVKAPILGFETIHKMHLQKIDEIFLRLNSAEDNSVVSFTLVNPFALRKYEFEVPTPLKILLELEGAKSVLVANIMVVQTPIELSTVNYLAPLIFNLDKQLMGQVVLDSKKYPHYHLRENILSHTHE
Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum. {ECO:0000255|HAMAP-Rule:MF_01185}.
Q9ZJL6
FABZ_HELPJ
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ (EC 4.2.1.59) ((3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase) ((3R)-hydroxymyristoyl-ACP dehydrase) (Beta-hydroxyacyl-ACP dehydratase)
MEQSHQNLQSQFFIEHILQILPHRYPMLLVDRIIELQANQKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQTGGFLAFTSLWGFDPEIAKTKIVYFMTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIAERE
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. {ECO:0000255|HAMAP-Rule:MF_00406}.
Q9ZJL7
LPXA_HELPJ
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (UDP-N-acetylglucosamine acyltransferase) (EC 2.3.1.129)
MSKIAKTAIISPKAEIGKGVEIGEFCVIGDGVKLDEGVKLHNNVTLQGHTFIGKNTEIFPFAVLGTQPQDLKYKGEYSELMVGEDNLIREFCMINPGTEGGIKKTLIGDKNLLMAYVHVAHDCVIGSHCILANGVTLAGHIEIGDYVNIGGLTAIHQFVRIAKGCMIAGKSALGKDVPPYCTVEGNRAFIRGLNRHRMRQLLESKDIDFIHALYKRLFRPIPSLRESAKLELEEHANNPFVKEICSFILESSRGVAYKSSEYSSEEKQEE
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}.
Q9ZJL8
CLPX_HELPJ
ATP-dependent Clp protease ATP-binding subunit ClpX
MNETLYCSFCKKPESRDPKKRRIIFASNLNKDVCVCEYCIDVMHGELHKYDSKYDRMDSLLALKRDRLRRMESSAYEEEFLLSRIPAPKELKAVLDNYVIGQEQAKKVFSVAVYNHYKRLSFKEKLKKQDNQDSDLELEHLEEVELSKSNILLIGPTGSGKTLMAQTLAKHLDIPIAISDATSLTEAGYVGEDVENILTRLLQASDWNVQKAQKGIVFIDEIDKISRLSEHRSITRDVSGEGVQQALLKIVEGSLVNIPPKGGRKHPEGNFIQIDTSDILFICAGAFDGLAEIIKKRTTQNVLGFTQEKMSKKEQEAILHLVQTHDLVTYGLIPELIGRLPVLSTLDSISLEAMVDILQKPKNALIKQYQQLFKMDEVDLIFEEEAIKEIAKLALERKTGARGLRAIIEDFCLDIMFDLPKLKGSEVRITKDCVLKQAEPLIIAKTHSKILP
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}.
Q9ZJN2
NADC_HELPJ
Probable nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) (Quinolinate phosphoribosyltransferase [decarboxylating]) (QAPRTase)
MEIKTFLECALKEDLGHGDLFERVLEKDFKATAFVRAKQEGVFSGEKYALELLQMTGIECVQNIKDKERFKPKDTLMEIRGDFSMLLKIERTLLNLLQHSSGIATLTSRFVEALNSPKVRLLDTRKTRPLLRIFEKYSVLNGGASNHRLGLDDALMLKDTHLKHVKDLKSFLTHARKNLPFTAKIEIECESFEEAKNAMSAGADIVMCDNMSVGETKEIAAYREAHYPFVLLEASGNISLESINAYAKSGVDAISVGALIHQATFIDMHMKMA
Involved in the catabolism of quinolinic acid (QA).
Q9ZJN9
UNG_HELPJ
Uracil-DNA glycosylase (UDG) (EC 3.2.2.27)
MKLFDYAPLSLAWREFLQSEFKKPYFLEIEKRYLEALKSPKTIFPKSSNLFCAFNLTPPYAVKIILLGQDPYHSTYLENEQELPVAMGLSFSVEKNAPIPPSLKNIFKELHANLGVPVPCCGDLSAWAKRGMLLLNAILSVEKNQAASHKYIGWEAFSDQILIRLFETTTPLIVVLLGKVAQKKIALIPKNKHIIITAPHPSPLSRGFLGSGVFTSVQKAYREVYRKDFDFSL
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.
Q9ZJP2
CORA_HELPJ
Magnesium transport protein CorA
MVNVFFKQQKFVIKKRFNDFNGFDIEENEVLWFELINPTPNELATLSQEYAIHYNTDHSQRVSSVTKYWEDSSSVTINAFFTNQDENETFHMEMATFILSNNILFTIYYGTLEIFDSIQKKVLASPKKFEDGFDILTKIFEVYFEKGVECLEWINKQTSLLRKNIIFKETSTHDDILVRLSNLQEFNVALRDSFFDKRRIITALLRSNKVDSDTKNNLNIILTDFSSLVESTTVNLNSLDNIQNLFASQVNVEQNKIIKLFTVATMAMMPPTLIGTIYGMNFKFMPELEWQYGYLFALIVMAISTILPVIYFKKKGWL
Mediates influx of magnesium ions (By similarity). Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high (By similarity).
Q9ZJP5
EXBD_HELPJ
Biopolymer transport protein ExbD
MKSIRRGDGLNVVPFIDIMLVLLAIVLSISTFIAQGKIKVSLPNAKNAEKSQPNDQKVVVISVDEHDNIFVDDKPTNLEALSAVVKQTDPKTLIDLKSDKSSRFETFISIMDILKEHNHENFSISTQAQ
Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.
Q9ZJP6
EXBB_HELPJ
Biopolymer transport protein ExbB
MGGFSMAMLKDYVDVFVFAVLGVASFLALWFVIERVIFYSKVDLKAYDDIDALNLDLTKNLTILYVIFSNAPYVGLLGTVLGIMVIFYDMGVSGGMDAKTIMVGLSLALKATALGLAVAIPTLIAYNSLLRKSDVLSEKFRIMKT
Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).
Q9ZJP7
NIKR_HELPJ
Putative nickel-responsive regulator
MDTPNKDDSIIRFSVSLQQNLLDELDNRIIKNGYSSRSELVRDMIREKLVEDNWVEDNPNDGSKIAVLVVIYDHHQRELNQRMIDIQHASGTHVLCTTHIHMDEHNCLETIILQGNSLEIQRLQLEIGGLRGVKFAKLTKASSFEYNE
Transcriptional regulator. {ECO:0000255|HAMAP-Rule:MF_00476}.
Q9ZJP8
NADD_HELPJ
Probable nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) (Deamido-NAD(+) diphosphorylase) (Deamido-NAD(+) pyrophosphorylase) (Nicotinate mononucleotide adenylyltransferase) (NaMN adenylyltransferase)
MNTMNSVLECKELALYGGSFDPLHKAHLAIIEQTLELLPFVQLIVLPAYQNPFKKPCFLDAKTRFKELERALKGMPRVLLSDFEIKQERAVPTIESVLHFQKLYRPKTLYLVIGADCLRHLSSWTNAKELLKRVELVVFERIGYEEIQFKGRYHPLKGIDAPISSSAIRASLGV
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Q9ZJR4
RL3_HELPJ
Large ribosomal subunit protein uL3 (50S ribosomal protein L3)
MEFLVQKIGMSRTIDANSTPVTLLKVLQAKVCQLENGKALVAYAMHKKYNKAIEGQQKKYQLSKEFNHFATLKASQQKELGDLDLSALETLKRVKASFKTKGRGFAGVMKRWNFQGGPAAHGSRFHRRPGSIGNREWPGRVQKGRKMAGHYGNELVTCQNEVLSFDKESMVLVLKGSVAGFSGAYGRIRAV
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Q9ZJR5
RL4_HELPJ
Large ribosomal subunit protein uL4 (50S ribosomal protein L4)
MSKAIVLDSHLKEKGSVELPKRYEGINSHNLYLYVKHYLSSARANTAKSKNRAEVSGGGRKPWAQKGGGRARAGSITSPVFVGGGVSHGATNKRNYNLKINKKQKRLALEYALEEKAQANKLFVVEKIAIKGVVEDNKRKHLTKEANQMFQALEQRDTLFVCLNMDEYTELAFSNLKKCLVIDVSELNAYLLAAFSSVVMEEAAFQHVVQDKTEE
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}. Forms part of the polypeptide exit tunnel. {ECO:0000255|HAMAP-Rule:MF_01328}.
Q9ZJR6
RL2_HELPJ
Large ribosomal subunit protein uL2 (50S ribosomal protein L2)
MAIKTYKPYTPSRRFMSVLDSKDITAKSSVKGLLTKLKATAGRNNNGRITSRHKERGAKKLYRIIDFKRNKYNIEGKVAAIEYDPYRNARIALVVYPDGDKRYILQPSGLKVGDSVIAAEGGLDIKVGFAMKLKNIPIGTVVHNIEMHPGAGGQLARSAGMSAQIMGRENKYTILRMPSSEMRYILSECMASVGVVGNEDFINVSIGKAGRNRHRGIRPQTRGSAMNPVDHPHGGGEGKTGTSGHPVSPWGTPAKGYKTRKKKASDKLIISRKKHK
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}.
Q9ZJR7
RS19_HELPJ
Small ribosomal subunit protein uS19 (30S ribosomal protein S19)
MSRSIKKGPFIDDHLMKKTLKAKEGKDNRPIKTWSRRSTILPEMIGFTYNVHNGRVFVPVYITENHVGYKLGEFAPTRTFKGHKGSVQKKIGK
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Q9ZJR8
RL22_HELPJ
Large ribosomal subunit protein uL22 (50S ribosomal protein L22)
MSKALLKFVRLSPTKARLIARQIQGMNAELAIASLEFTPNKAARVLSKVVASAVANGSLDAKSALIVSCRVDAGPVLRRSIPRAKGRATAIRKPTSHVFVEVAEGKEMKSSKSHKKNQAEGK
This protein binds specifically to 23S rRNA its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). {ECO:0000255|HAMAP-Rule:MF_01331}. The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}.
Q9ZJR9
RS3_HELPJ
Small ribosomal subunit protein uS3 (30S ribosomal protein S3)
MGQKVNPVGLRLGINRNWTSRWFPSTRTAPSNIDEDNKIRKFLKKELYYAGVSEIVIERAAKKLRVTVVAARPGLIIGKKGVDIEKVKEGLKTLIKKEVSINIKEVKRPQADAQLAAENVATQLEKRVAFRRAMKKVMQAALKSGAKGIKVRVSGRLAGAEIARTEWYMEGRVPLHTLRAKIDYGFAEAMTVYGIIGVKVWIFKGEVLQKGIQFEKKEEAKEEREPRRSRRGRQ
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. {ECO:0000255|HAMAP-Rule:MF_01309}.
Q9ZJS0
RL16_HELPJ
Large ribosomal subunit protein uL16 (50S ribosomal protein L16)
MLMPKRTKYRKQMKGRNRGKAHRGNSIAFGDIAIKAIEHGRIDSRQIESARVAMTRHIKRAGKVWIRVFPDKPLTAKPLETRMGKGKGSVEKWVMNIKPGRIVYEMLGIEEGLAREALALSQSKLPFKTKIVTCESENEIY
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. {ECO:0000255|HAMAP-Rule:MF_01342}.
Q9ZJS2
RL14_HELPJ
Large ribosomal subunit protein uL14 (50S ribosomal protein L14)
MIQSFTRLNVADNSGAKEIMCIKVLGGSHKRYASVGSVIVASVKKAIPNGKVKFGLVVKTVVVRTKKEIQRKNGSLVRFDDNAAVILDAKKDPVGTRIFGPVSREVRYANFMKIISLAPEVV
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}.
Q9ZJS3
RL24_HELPJ
Large ribosomal subunit protein uL24 (50S ribosomal protein L24)
MKSEIKKNDMVKVIAGDDKGKVAKVLAVLPKTSQVVVEGCKVVKKAIKPTDDNPKGGFIKKEKPMHISNVKKA
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. {ECO:0000255|HAMAP-Rule:MF_01326}.
Q9ZJS4
RL5_HELPJ
Large ribosomal subunit protein uL5 (50S ribosomal protein L5)
MFGLKQFYQNEVRAKLAQELDIKNPMLLPKLEKIVISVGAGAHAKDMKIMQNIAQTISLVAGQKAVITKAKKSVAGFKIREGMAVGAKVTLRNKRMYNFLEKLIVISLPRVKDFRGISRNGFDGRGNYTFGINEQLIFPEVVYDDIMVSHGMNITMVTSTDNDKEAFKLLELLGLPFAKVR
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits this bridge is implicated in subunit movement. Contacts the P site tRNA the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. {ECO:0000255|HAMAP-Rule:MF_01333}.
Q9ZJS5
RS14Z_HELPJ
Small ribosomal subunit protein uS14 (30S ribosomal protein S14 type Z)
MAKKSMIAKAQRKPKFQVRAYTRCRICGRPHSVYRDFGLCRVCLRKMASEGLIPGLRKASW
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. {ECO:0000255|HAMAP-Rule:MF_01364}.
Q9ZJS6
RL6_HELPJ
Large ribosomal subunit protein uL6 (50S ribosomal protein L6)
MSRIGKRIIEIPSSVQASVEGSKLLFKNNKEKHELETHNRVKITLENNQLSFQPVGEDAQFRAYWGTYGALANNIVIGLSAGFSKTLEVNGVGYKVALGHKTLDLSLGFSHPVKYPIPAGIEMVVEKNTITIKGSDKQQVGQVAAEIRSFRPPEPYKGKGVKYSNEVIIRKAGKTAKK
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}.
Q9ZJS7
RL18_HELPJ
Large ribosomal subunit protein uL18 (50S ribosomal protein L18)
MNAKALYKKKALRDRRKLRIKSKLLGDKLRPRVSVFRSNRYFYAQAIDDVKQSTITHIDGRKMGFKNTQEDAKKLGALFAEELKKAGIERAVYDRNGYLYHGVVAAFAESLRENGIVL
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. {ECO:0000255|HAMAP-Rule:MF_01337}.
Q9ZJS8
RL15_HELPJ
Large ribosomal subunit protein uL15 (50S ribosomal protein L15)
MGLENLKPAKGSVKKIKRVGRGQGSGMGKTATRGGKGQTARTGYKAKRGFEGGQQPLQRRLPKIGFRTKDSHIYSINVEKNEAIKSLEEITFSSLRALHHFPLYIEGVKLIGKDAKNLASKIKDERIKTSGQK
Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01341}.
Q9ZJS9
SECY_HELPJ
Protein translocase subunit SecY
MNKAIASKILITLGFLFLYRVLAYIPIPGVDLAAIKAFFDSNSNNALGLFNMFSGNAVSRLSIISLGIMPYITSSIIMELLSATFPNLAKMKKERDGMQKYMQIVRYLTILITLIQAVSVSVGLRSISGGANGAIMIDMQVFMIVSAFSMLTGTMLLMWIGEQITQRGVGNGISLIIFAGIVSGIPSAISGTFNLVNTGVINILMLIGIVLIVLATIFAIIYVELAERRIPISYARKVVMQNQNKRIMNYIPIKLNLSGVIPPIFASALLVFPSTILQQATSNKTLQAIADFLSPQGYAYNILMFLLIIFFAYFYSSIVFNSKDIADNLRRNGGYIPGLRPGEGTSSFLNAVASKLTLWGSLYLALISTVPWILVKAMGVPFYFGGTAVLIVVQVAIDTMKKIEAQIYMSKYKTLSAVGF
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. {ECO:0000255|HAMAP-Rule:MF_01465}.
Q9ZJT2
RS13_HELPJ
Small ribosomal subunit protein uS13 (30S ribosomal protein S13)
MARIAGVDLPKKKRVEYALTCKNGIGLKSSREILEAVGISFDKRVHELSEDEVSSIAKKIQQSYLVEGDLRKKVQMDIKSLMDLGNYRGIRHRKGLPVRGQTTKNNARTRKGKKKTVGSK
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. {ECO:0000255|HAMAP-Rule:MF_01315}.
Q9ZJT3
RS11_HELPJ
Small ribosomal subunit protein uS11 (30S ribosomal protein S11)
MAKRNVTAKKKVVKKNIARGVVYISATFNNTNITITDEMGNVICWSTAGGLGFKGSKKSTPYAAQQAVESALSKAKEHGVKEVGIKVQGPGSGRETAIKSVGATEGVKVLWIKDITPLPHNGCRPPKRRRV
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01310}.
Q9ZJT4
RS4_HELPJ
Small ribosomal subunit protein uS4 (30S ribosomal protein S4)
MARYRGAVERLERRFGVSLALKGERRLSGKSALDKRAYGPGQHGQRRTKTSDYGLQLKEKQKAKMMYGISEKQFRSIFVEANRLDGNTGENLIRLIERRLDNVVYRMGFATTRSSARQLVTHGHVLVDGKRLDIPSYFVRSGQKIEIKEKTKSNPQVVRAMELTAQTGIVPWIDVEKDKKYGIFTRYPEREEVVVPIEERLIVELYSK
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}.
Q9ZJU7
TRPD_HELPJ
Anthranilate phosphoribosyltransferase (EC 2.4.2.18)
MKDILNALYHQKDLNDEEVKKLFTLIIDEKVSPAQLGAVLCALKIKGESFKEISVAATTLLEHAPKPFNSGLDLIDNCGTGGDGLKTINISTIAALIASSMGLSMAKHGSRSVSSHSGSADLLENLGVNIEMNPMQLENCFKQSHFGFLFAPLYHQSFKKSAPLRKELFTKTIFNCLGPLINPLRPKIQLLGVYDKSLCKTMALALKALGVKRAMVVNGGGTDEIVLHDITHACELKNNEILEYDLSAKDFDLPPYDLKELQIENAKESVQACLDILENKGKDSHTMVVAANVASLLYLSHRAKDLKEGVSMTLEHLKTKAPYAHLQKIIRLSHA
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}.
Q9ZJU9
TRPB_HELPJ
Tryptophan synthase beta chain (EC 4.2.1.20)
MNQKAYFGEFGGSFVSELLVPALRELEQAFDTCLKDEEFQKEYFRLLKDFVGRPSPLTLCQNIVSNPKVKLYLKREDLIHGGAHKTNQALGQALLAKKMGKTRIIAETGAGQHGVATAIACALLNLKCVIFMGGKDIKRQEMNVFRMRLLGAEVREVNSGSATLKDAVNEALRDWASSYKDTHYLLGTSAGPHPYPTMVKTFQKMIGDEVKSQILEKENRLPDYVIACVGGGSNAIGIFSAFLNDKEVKLIGVEPAGLGLETNKHGATLNKGRVGILHGNKTYLLQDDEGQIAESHSISAGLDYPGVGPEHSYLKEIGRAVYESASDIEALEAFRLLCQKEGIIPALESSHALAYALKLAQKCAQEKIIVVNLSGRGDKDLSTVYNALKGGLK
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Q9ZJV0
TRPA_HELPJ
Tryptophan synthase alpha chain (EC 4.2.1.20)
MRYQNMFETLKKHKKMAFIPFVTLGDPNYELSFEIVKTLIISGVSALELGLAFSDPVADGTTIQASHLRALKHASMAKNFQLLKKIRGYNHDIPIGLLAYANLIFSYGVDGFYAQAKECGVDSVLIADMPLIEKELVIKSAQKHQIKQIFIASPNASSKDLEQVATHSQGYIYTLARSGVTGASHTLENDASAIIKTLKTFSSTPALLGFGISKKEHITNAKGMGADGVICGSALVKIIEENLNNEDAMLEKIKGFVGGMIS
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}.
Q9ZJW0
NUOH_HELPJ
NADH-quinone oxidoreductase subunit H (EC 7.1.1.-) (NADH dehydrogenase I subunit H) (NDH-1 subunit H)
MSAYIIETLIKILILVAVFSALGGFATYIERKVLAYFQRRLGPCYVGPFGLLQVAADGIKLFTKEDIIPQGANKFIFTLAPIIAMVSAFVSMAPIPFFPNFTLFGYEIKPLISDINIGFLFFLAVGSAGIYAPILAGLASNNKYSLIGSARATIQLLSFEVVSTLTILAPLMVVGSLSLVEINHYQSGGFLDWLVFKQPLAFVLFLIASYAELNRTPFDLLEHEAEIVAGYCTEYSGLKWGMFFLAEYAHLFAFSFVISIVFFGGFNAWGFIPGGIAILIKAGFFVFLSMWVRATYPHVRPDQLMNMCWKIMLPLALLNIVLTGIVILI
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. {ECO:0000255|HAMAP-Rule:MF_01350}.
Q9ZJW4
NUOD_HELPJ
NADH-quinone oxidoreductase subunit D (EC 7.1.1.-) (NADH dehydrogenase I subunit D) (NDH-1 subunit D)
MAQNFTKLNPQFENIIFEHDDNQMILNFGPQHPSSHGQLRLILELEGEKIIKATPEIGYLHRGCEKLGENMTYNEYMPTTDRLDYTSSTSNNYAYAYAVETLLNLEIPRRAQVIRTILLELNRMISHIFFISVHALDVGAMSVFLYAFKTREYGLDLMEDYCGARLTHNAIRIGGVPLDLPPNWLEGLKKFLGEMRECKKLIQGLLDKNRIWRMRLENVGVVTPKMAQSWGMSGIMLRGTGIAYDIRKEEPYELYKELDFDVPVGNYGDSYDRYCLYMLEIDESIRIIEQLIPMYAKTDTPIMAQNPHYISAPKEDIMTQNYALMQHFVLVAQGMRPPVGEVYAPTESPKGELGFFIHSEGEPYPHRLKIRAPSFYHIGALSDILVGQYLADAVTVIGSTNAVFGEVDR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01358}.
Q9ZJX1
RRF_HELPJ
Ribosome-recycling factor (RRF) (Ribosome-releasing factor)
MLQAIYNETKDLMQKSIQALNRDFSTLRSAKVSVNILDHIKVDYYGTPTALNQVGSVMSLDATTLQISPWEKNLLKEIERSIQEANIGVNPNNDGETIKLFFPPMTTEQRKLIAKDAKAMGEKAKVAVRNTRQDANNKVKKLEKDKEISEDESKKAQEQIQKITDEAIKKIDESVKNKEDAILKV
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}.
Q9ZJX2
SECG_HELPJ
Protein-export membrane protein SecG
MTSALLGLQIVLAVLIVVVVLLQKSSSIGLGAYSGSNDSLFGAKGPASFMAKLTMFLGLLFVINTIALGYFYNKEYGKSVLDETKTNKELSPLVPATGTLNPTLNPTLNPTLNPLEQAPTNPLMPTQTPKELPKEPAKTPFVESPKQNEKNEKNDAKENGIKGVEKNKENAKTPPTTHQKPKTHATTNAHTNQKKDEK
Involved in protein export. Participates in an early event of protein translocation (By similarity).
Q9ZJX9
RNR_HELPJ
Ribonuclease R (RNase R) (EC 3.1.13.1) (VacB protein homolog)
MQGFLRSLFFGVKKIPKRFAPLVEKGVLKEALQSNKDRYLLKEGFDIGKIERVKNKAFFISLAKNYPKDPLIKNLPPSFKTDALILCQIECSKKRPIAFFKAALLNADHAMIAYLAKEKNQIVAIPFKEPFKKPISLKHSQRSLLELPRHCVVKIDLKKREISEILGALEDPLIDENLSLSLFDRIKDFSKDCLDLAQYYAQLKASDFKDRINYSHIPFITIDPKDAKDFDDAIFYDKEKNTLFVAVADVSEFVPKHSSLDKEARIRGFSVYFPNSVYPMLPLSLSQGACSLKAFEKRLALVYEIPLDNLKNARLSQGVIEVRANCAYEEINHFLNTQQSSLGKDLQQSLLGFLEVALKLKKERLKKGFNFNSFENKLYLNEEGRIEKIETEKESGAHTLIEEAMLLANQSSARLLDGHFHNRGIYRTHKEPSLEQQKRLYDKLFDYEIVRPKNMGFFPFLEHALKISQEKSIEREVSRLIIKSQNLALYSPMQESHFGLGFASYTHFTSPIRRYSDLALHRLLKELLFHQAKGCSYLLEETPELCAELNALQKKAALIERDFIKRKFARLALEFLEKEFLGVVLEAKDWVVVGLKEFIGLKVLIKTNKVFKPLEKVRIKITHADLILGQVRGEITERIKEHVS
3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. {ECO:0000255|HAMAP-Rule:MF_01895}.
Q9ZJY0
Y1168_HELPJ
Protein jhp_1168
MYRKDLDNYLKQRLPKAVFLYGEFDFFIHYYIQTISALFKGNNPDTETSLFYASDYEKSQIATLLEQDSLFGGSSLVILKLDFALHKKFKENDINPFLKALERPSHNRLIIGLYNAKSDTTKYKYTSEIIVKFFQKSPLKDEAICVRFFTPKAWESLKFLQERANFLHLDISGHLLNALFEINNEDLSVSFNDLDKLAVLNAPITLEDIQELSSNAGDMDLQKLILGLFLKKSVLDIYDYLLKEGKKDADILRGLERYFYQLFLFFAHIKTTGLMDAKEVLGYAPPKEIVENYAKNALRLKEAGYKRVFEIFRLWHLQSMQGQKELGFLYLTPIQKIINP
Could be the functional equivalent of DNA polymerase III delta subunit (HolA).
Q9ZJY1
RS6_HELPJ
Small ribosomal subunit protein bS6 (30S ribosomal protein S6)
MRHYETMFILKPTLVEEEIKSKIEFYREVITKHHGVIETSLDMGMRNLAYEIKKHKRGYYYVAYFKADPSMILELERLYRINEDVLRFIVIKYESKKEVEAWHALVDRANKKPSHAKEKHEKTEHTHSHHAEEAKSTESHSE
Binds together with bS18 to 16S ribosomal RNA.
Q9ZJY2
SSB_HELPJ
Single-stranded DNA-binding protein (SSB)
MFNKVIMVGRLTRNVELKYLPSGSAAATIGLATSRRFKKQDGTLGEEVCFIDARLFGRTAEIANQYLSKGSSVLIEGRLTYESWMDQTGKKNSRHTITADSLQFMDKKSDNPQANSMQDSMTHENFNNAYPTNYNAPSQDPFSQAQSYPQNAYTKENSQAQPSKYQNSVPEINIDEEEIPF
Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. {ECO:0000255|HAMAP-Rule:MF_00984}.
Q9ZJY6
NTPP_HELPJ
Nucleoside triphosphate pyrophosphatase (EC 3.6.1.9) (Nucleotide pyrophosphatase) (Nucleotide PPase)
MELILGSQSSARANLLKEHGIKFEQKALYFDEESLKTTDPREFVYLACKGKLEKAKELLANNCAIVVADSVVSVGNRMQRKAKNKREALEFLKRQNGNEIEVLTCSALISPVLEWLDLSVFRARLKAFDCSEIEKYLESGLWQGSAGCVRLEDFHKPYIKSSSKNLSVGLGLNVEGLLGALKLGVKLSLL
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}.
Q9ZJY8
AMIF_HELPJ
Formamidase (EC 3.5.1.49) (Formamide amidohydrolase)
MGSIGSMGKPIEGFLVAAIQFPVPIVNSRKDIDHNIESIIRTLHATKAGYPGVELIIFPEYSTQGLNTAKWLSEEFLLDVPGKETELYAKACKEAKVYGVLSIMERNPDSNENPYNTAIIIDPQGKIILKYRKLFPWNPIEPWYPGDLGMPVCEGPGGSKLAVCICHDGMIPELAREAAYKGCNVYIRISGYSTQVNDQWILTNRSNAWHNLMYTVSVNLAGYDNVFYYFGEGQICNFDGTTLVQGHRNPWEIVTGEIYPKMADNARLSWGLENNIYNLGHRGYVAKPGGEHDAGLTYIKDLAAGKYKLPWEDHMKIKDGSIYGYPTTGGRFGK
Is an aliphatic amidase with a restricted substrate specificity, as it only hydrolyzes formamide. {ECO:0000255|HAMAP-Rule:MF_01243}.
Q9ZJZ8
RPPH_HELPJ
RNA pyrophosphohydrolase (EC 3.6.1.-) ((Di)nucleoside polyphosphate hydrolase)
MLHKKYRPNVAAIIMSPDYPNTCEVFIAERIDIEGAWQFPQGGIDEGETPLEALYRELLEEIGTNEIEILAQYPRWIAYDFPSNMEHKFYSFDGQKQRYFLVRLKHVNNIDLNKHTPEFRSYQFIQLKDLLKKIVPFKRQVYRQVIAYFRKEGYLGC
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}.
Q9ZK01
FLUC_HELPJ
Fluoride-specific ion channel FluC
MNLVFLWAALGGAIGSSLRYFVGKMMPSKFLMFESFPLGTFSVNLIGCFIIGFMGHLAAKKVFGDDFGIFFVTGVLGGFTTFSSYGLDTLKLLQKSQYLEAISYVLGTNLLGLIGVAIGWFLAKNFVGVN
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. {ECO:0000255|HAMAP-Rule:MF_00454}.
Q9ZK05
ISPT_HELPJ
Isoprenyl transferase (EC 2.5.1.-)
MDSTLKHLAIIMDGNGRWAKLKNKARAYGHKKGVKTLKDITIWCANHKLECLTLYAFSTENWKRPKSEVDFLMKMLKKYLKDERSTYLDNNIRFRAIGDLEGFSKELRDTILRLENDTRYFKDFTQVLALNYGSKNELSRAFKSLLENPPNHINNIESLENEISHRLDTHDLPEVDLLLRTGGEMRLSNFLLWQSSYAELFFTPILWPDFTPKDLENIISDFYKRVRKFGELKC
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. {ECO:0000255|HAMAP-Rule:MF_01139}.
Q9ZK20
NUSG_HELPJ
Transcription termination/antitermination protein NusG
MMDWYAIQTYSGSEQSVKKAIENLANDHDIRDRIQEIIVPTEDIIEVSKKSKTKVMERSLYPGYVFIKVDLDTVLWHKIQSLPRVSRFIGENKKPTPLSEADIGHILEKMNNRAAPKPKIFFEQGEVVRVVEGPFANFTATVEEYDVEHRKLKLNVSIFGRTTPIEILYSQVEKII
Participates in transcription elongation, termination and antitermination. {ECO:0000255|HAMAP-Rule:MF_00948}.
Q9ZK21
RL1_HELPJ
Large ribosomal subunit protein uL1 (50S ribosomal protein L1)
MAKKVFKRLEKLFSKIQNDKVYGVEHGVEVVKSLASAKFDETVEVALRLGVDPRHADQMVRGAVVLLHGTGKKVRVAVFAKDIKQDEAKNAGADVVGGDDLAEEIKNGRIDFDMVIATPDMMAVVGKVGRILGPKGLMPNPKTGTVTMDIAKAVTNAKSGQVNFRVDKKGNVHAPIGKASFPEEKIKENMLELVKTINRLKPSSAKGKYIRNAALSLTMSPSVNLDAQELMDIK
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}.
Q9ZK22
RL10_HELPJ
Large ribosomal subunit protein uL10 (50S ribosomal protein L10)
MQKQHQRQHKVELVANLKSQFDSAKALLICDYKGLSVKKLEALRNKARIQGIKVQVIKNTLAHIAMKEVGCADLDLKETNVFLWGDDQIALSKLVFDFQKEHKDHFVLKAGLFDKESVSVAHVEAVSKLPSKEELMGMLLSVWTAPARYFVTGLDNLRKAKEEN
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
Q9ZK24
EFG_HELPJ
Elongation factor G (EF-G)
MARKTPLNRIRNIGIAAHIDAGKTTTSERILFYTGVSHKIGEVHDGAATMDWMEQEKERGITITSAATTCFWKDHQINLIDTPGHVDFTIEVERSMRVLDGAVSVFCSVGGVQPQSETVWRQANKYGVPRIVFVNKMDRIGANFYNVENQIKQRLKANPVPINIPIGAEDTFIGVIDLVQMKAIVWNNETMGAKYDVEEIPSDLLEKAKQYREKLVEAVAEQDEALMEKYLGGEELDIEEIKKGIKTGCLNMSFVPMLCGSSFKNKGVQTLLDAVIDYLPAPTEVVDIKGIDPKTEEEVFVKSSDDGEFAGLAFKIMTDPFVGQLTFVRVYRGKLESGSYVYNSTKDKKERVGRLLKMHSNKREDIKEVYAGEICAFVGLKDTLTGDTLCDEKNAVVLERMEFPEPVIHIAVEPKTKADQEKMGVALGKLAEEDPSFRVMTQEETGQTLIGGMGELHLEIIVDRLKREFKVEAEIGQPQVAFRETIRSSVSKEHKYAKQSGGRGQYGHVFIKLEPKEPGSGYEFVNEISGGVIPKEYIPAVDKGIQEAMQNGVLAGYPVVDFKVTLYDGSYHDVDSSEMAFKIAGSMAFKEASRAANPVLLEPMMKVEVEVPEEYMGDVIGDLNRRRGQINSMDDRLGLKIVNAFVPLVEMFGYSTDLRSATQGRGTYSMEFDHYGEVPSNIAKEIVEKRKG
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, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Q9ZK31
SOTB_HELPJ
Probable sugar efflux transporter
MMITKQSYQRFALMRVFVFSLSAFIFNTTEFVPVALLSDIAKSFEMESATVGLMITAYAWVVSLGSLPLMLLSAKIERKRLLLFLFALFIFSHILSALAWNFWVLLLSRMGIAFAHSIFWSITASLVIRVAPRNKKQQALGLLALGSSLAMILGLPLGRIIGQILDWRSTFGVIGGVATLIMLLMWKLLPHLPSRNAGTLASVPILMKRPLLVGIYLLVIMVISGHFTTYSYIEPFIIQISQFSPDITTLMLFVFGLAGVVGSFLFGRLYAKNSRKFIAFAMVLVICPQLLLFVFKNLEWVIFLQIFLWGIGITSLTIALQMRVLQLAPDATDVASAIFSGSYNVGIGSGALFGSIVIHQLGLEYIGFVGGALGLLALFWLRFITIKFKKT
Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites. {ECO:0000255|HAMAP-Rule:MF_00517}.
Q9ZK41
GLUP_HELPJ
Putative glucose/galactose transporter
MQKTSNTLALGSLTALFFLMGFITVLNDILIPHLKPIFDLTYFEASLIQFCFFGAYFIMGGVFGNVISKIGYPFGVVLGFVITASGCALFYPAAHFGSYGFFLGALFILASGIVCLQTAGNPFVTLLSKGKEARNLVLVQAFNSLGTTLGPIFGSLLIFSATKTSDNLSLIDKLADAKSVQMPYLGLAVFSLLLALVMYLLKLPDVEKEMPKETTQKSLFSHKHFVFGALGIFFYVGGEVAIGSFLVLSFEKLLNLDAQSSAHYLVYYWGGAMVGRFLGSALMNKIAPNKYLAFNALSSIILIALAILIGGKIALFALTFVGFFNSIMFPTIFSLATLNLGHLTSKASGVISMAIVGGALIPPIQGVVTDMLTATESNLLYAYSVPLLCYFYILFFALKGYKQEENS
Intake of glucose and galactose.
Q9ZK47
CSTA_HELPJ
Peptide transporter CstA (Carbon starvation protein A homolog)
MQKSLVSLAWVFVAILGAICLGVLALHKGESINTLWLVVASACIYSIGYRFYSHFIAYRVLKLDDSRATPACVRNDGKDFVPTDKAITFGHHFAAIAGAGPLVGPILAAQMGYLPSILWILIGSVLGGCVHDFVVLFASIRRDGKSLGEMIKLEMGKFVGMIASLGILGIMLIIIAILAMVVVKALAHSPWGFFTIAMTIPIAILMGLYMRFFRPHKILEVSVIGFILLIIAIYAGKYVSLDPKLASIFTFEAGSLAWMIMGYGFVASILPVWFLLAPRDYLSTFLKIGVIGVLVVAIVFVAPPLQIPKITPFVDGSGPVFAGSVFPFLFITVACGTISGFHALISSGTTPKMLAKESDARLVGYGSMVMESVVALMALVCAGILHPGLYFAINSPEVSIGKDIADAASVISSWGFSISAEEIREMTKNIGESSILSRTGGAPTFAIGLAMIVYHILGDPSVMAFWYHFAILFEALFILTAVDAGTRTARFMIQDLLGNIYKPLGDLSSYKAGIFATLLCVAGWGYFLYQGTIDPKGGIYTLWPLFGVSNQMLAGMALLLVTVVLFKMGRFKGAIISALPAVLILAITFYSGILKVMPKSNDSVLNNVSHVAQMQIIKEKIALTTDEKALKTLQKSFFNHAIDAILCVFFMLVALLVLIVSVRICSNAYFKNQIYPPLAETPYIKAA
Involved in peptide utilization.
Q9ZK53
FLAV_HELPJ
Flavodoxin
MGKIGIFFGTDSGNAEAIAEKISKAIGNAEVIDVAKASKEQFNGFTKVILVAPTAGAGDLQTDWEDFLGTLEASDFANKTIGLVGLGDQDTYSETFAEGIFHIYEKAKAGKVVGQTPTDGYHFEASKAVEGGKFVGLVIDEDNQDDLTDERIAKWVEQVKGSFA
Low-potential electron donor to a number of redox enzymes.
Q9ZK54
YBEY_HELPJ
Endoribonuclease YbeY (EC 3.1.-.-)
MLEIDNQTPLESDFLLLEKIADVLASTQIIELVLVSDETMREINRDLRDCDYATDVLSFPLEAIPHTPLGSVVINAPLAQENALKLGHSLEDEIALLFIHGVLHLLGYDHEKDKGEQRQKEGELIKAFDLPLSLIERTQEC
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}.
Q9ZK56
P5CR_HELPJ
Pyrroline-5-carboxylate reductase (P5C reductase) (P5CR) (EC 1.5.1.2) (PCA reductase)
MEILQFIGYGNMAQAILEGSHEILSKRFILEITGRNPEKIAPFLQEKNIQAQIVPYKDAIDIHQKFVFLLFKPYNLKDFNYQGQAKSVLSALAGVNFEALSNAINSLHYLKCMPNIASKFALSSTAVCEKSVAPSISEKALNIIESFGNCVRVGNEEQVDSSVATNGSALAFLSLVASSLKDAGIREGLNAKDSLELVKMSFKGFAKLLEKERPEMIIEQICTPKGATIEGLSVLEKKGVRGAFIKACHESVKKMRL
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. {ECO:0000255|HAMAP-Rule:MF_01925}.
Q9ZK60
FLIW1_HELPJ
Flagellar assembly factor FliW 1
MNYFLKAPILGFEHINEVRLEKIDSLFSRLMGQTNSPMALDMVLVNPYCLREYSFVIPKYIELLLELDSHSKVEVYCVVVLQKNLEDSMVNFLAPLVFNSKNGFGAQVALSMMDYPDFGFRDPLKSFVVKERERA
Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum. {ECO:0000255|HAMAP-Rule:MF_01185}.
Q9ZK65
RIMM_HELPJ
Ribosome maturation factor RimM
MLLVGRIGKSVGLNGGLKLHLESDFPECLKKGVKVSVAPINAFSCASSFKDYVIHSYEHAKNLLFLETIRTPEKAKELTNLGLFMSEAESKKLCVLKEGEFFYCDLIGLSVVEGNEILGKVIEIQRISQTDYFMVETTRSLVEKGLAKIFLIPYRDFYIQEILLQDKKITTHNAKTLLENS
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 70S ribosomes. {ECO:0000255|HAMAP-Rule:MF_00014}.
Q9ZK66
TRMD_HELPJ
tRNA (guanine-N(1)-)-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase)
MKFSVLTLFPQLILPYFEDSILKRALEKNLFELEVLNLRDFSANKYQKADHTLIGGGAGQILDPEMIENALHSVKNPKHTIFLSAVGKPFKQIDAMRLAQKKHVVLVCGRYEGFDERSIELGADEVFCIGDFILTGGELGALCLIDSIARHIQGVLGNAQSLENESFENNYLETPNFANAVFKSKEINKIPAPLEYSKGNHAKIKQLKLDLSKLRTKFYRLDLFKQHKS
Specifically methylates guanosine-37 in various tRNAs.
Q9ZK67
RL19_HELPJ
Large ribosomal subunit protein bL19 (50S ribosomal protein L19)
MKNRYIQQFEDAQLKDKSMPTFKAGDTLRLGITIKEGEKTRTQYFEGVCIAIRGNGVDKTFCVRKIGANNIGVEKIFPFYSESLASVEVLRVGRVRRAKLYYLRDRRGKAARIKEVRH
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.
Q9ZK72
FMT_HELPJ
Methionyl-tRNA formyltransferase (EC 2.1.2.9)
MRIVFMGTPSFAEVILRALVENEDKKIEVVGLFTQRDKPFGRKKELKAPETKTYILENHLNIPIFQPQSLKEPEVQILKGLKPDFIVVVAYGKILPKEVLTIAPCINLHASLLPKYRGASPIHEMILNDDRIYGISTMLMDLELDSGDILESASFLREDYLDLDALSLKLARMGATLLLSTLKNFHSITRKPQDHMQASFCKKIAKADGLVGFKDAKNLFLKSLAFKSWPEIFLENSLKLLEVELVENEKSHKEGEILAIDERGVLVGCLKGSVRIARLQAVGKKPLKAKDYLNGRRLKVGGILT
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}.
Q9ZK75
PARB_HELPJ
Probable chromosome-partitioning protein ParB
MAKNKVLGRGLADIFPEINEVYEQGLYERANRVVELGIDEVMPNPYQPRKIFSEDSLEELAQSIKEHGLLQPVLVVSENGRYHLIAGERRLRASKLAKMPTIKAIVVDIEQEKMREVALIENIQREDLNPLELARSYKELLESYQMTQEELSKIVKKSRAHVANIMRLLTLSSKVQNALLEEKITSGHAKVLVGLEEEKQELILNSIIGQKLSVRQTEDLARDFKINANFDNKKHGFKQTQTLIAEDELERFNQSLWDRYKLKAALKGKKIVLRCYKNSLLEAFMKKMMS
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).
Q9ZK77
ATPF_HELPJ
ATP synthase subunit b (ATP synthase F(0) sector subunit b) (ATPase subunit I) (F-type ATPase subunit b) (F-ATPase subunit b)
MFVVKMVLGFLILLSPLCATGLDISQTDIIERSLNFLLFVGILWYFLAKRLRSFLHSKSLEISKRLEEIQAQLKVSKEHKKKLLKELEQAKEKAELIISDANKEAYTITQKYELQTKMDVENLIKNSKALMDLEVKKIKRELVESVFKDLRESKKVSFNAQDCVNILKQRL
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-Rule:MF_01398}. Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP-Rule:MF_01398}.
Q9ZK80
ATPG_HELPJ
ATP synthase gamma chain (ATP synthase F1 sector gamma subunit) (F-ATPase gamma subunit)
MANLRDIRKKIGSVKNTQRITHAMKLVSTSKLRKAEEVARNSRAYALKLDAVFDDVLSKMKNQGIEDIQSKYFRELERLEIKKVDIIFITADKGLCGGFNTNTIKKVLACTNEYKEKDIKVRLRGIGKKGNEYFSFNGIEVLDKINNLSSMPNYERAQEFMKKVVEDYLSGKTDKVIIIHNGFKNMITQEIRVKTILPIGYKIIHQNPQPSETQETITSEPSGSEDEILDSLAEKYVEYSLYYALIDSLAAEHSARMQAMDTATNNAKDLVKTLTISYNKARQEAITTELVEINAGVEALK
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}.
Q9ZK82
ATPE_HELPJ
ATP synthase epsilon chain (ATP synthase F1 sector epsilon subunit) (F-ATPase epsilon subunit)
MALLKISVVVPEGEVYTGEVKSVVLPGVEGEFGVLYGHSNMITLLQAGVVEIETENQKEHIAINWGYAEVTNERVDILADGAVFIKKGSDDRDDAISRAKKLLEDASSDRLAVSSVLAKIESL
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Q9ZK86
TOLB_HELPJ
Tol-Pal system protein TolB
MKYLWLFLIYAIGLFATDKTLDIIKTIQKLPKIEVRYSIDNDANYALKLHEVLANDLKTSQHFDVSQNKEQGAINYAELKDKKVHLVALVSVAVENGNKISRLKLYDVDTGTLKKTFDYPIVSLDLYPFAAHNMAIVVNDYLKAPSIAWMKRLIVFSKYIGPGITNIALADYTMRYQKEIIKNNRLNIFPKWANAEQTEFYYTQYGEKTPMILKYNIQKATHENIASSQGMAVVSSVSSDGSKILMSLAPDGQPDVYLYDTHKKTKTKITRYPGIDVSGVFLEDDKSMAFVSDRSGYPNIYMKKLGLKESAEQLLYEGRSNESIDAYKDSIVYVSRENLNEFGKTVFNLNLIALNSKYIRRLTVNGSNQMPRFSMDGRNIMYIKKTSQEYAMGLILLDYNQSFLFPLKNVKIQAFDW
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}.
Q9ZKB1
6PGL_HELPJ
6-phosphogluconolactonase (6PGL) (EC 3.1.1.31)
MGYQLFEFENLEDCHKALIERFKEFFNAALKKHHQVSVAFSGGRSPISLLQKLSVLDLKWHECLISLVDERIIEASHEDSNAKLLHDYLLQNNALKASFTPLLPEKISGDTNELLDFANQHFKQPHLAILGMGTDGHTASLFPETSAFLNEEKENIVLTKPTNAPYERLSMSINALENCEKLFLSISGVEKRGVLEKALKENAPYSLPIARILHSKKVTTEVFYAKN
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Q9ZKB2
G6PD_HELPJ
Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49)
MLDFDLVLFGATGDLAMRKLFVSLYEIYIHYGFKNDSRIIASGRKELSNEEFLALLCEKTQLHSREKGEEFLTHISYLRVRLDNPKDFEELSKIATNNKPLIFYFSISPSFFATTAQNLAQNALNHANTRLILEKPLGHDLKTCKEIFQSISAFFKEEQIFRIDHYLGKKGVQNILELRLNNPILNILWDQISAVEICVYETLGVEERGEFYDKIGALRDMVQNHLLQVLSLIATDLPNDLKDLRQEKIKVLKTLQPPKDFTKQVIRAQYQGYRDENKVHKESQTETFVAIKAFLDTPKFKGVPFYLKHAKKMPRNQASVKIHFNAVNTLEFFLSQDKITLTLKDHQNPLILETHNKQEFLQPYAKLLYDAIPNNHYNFAHQLELEASWVFIDTLIEGFINNATPLYSYESHNLNESEFLKPLYQ
Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966}.
Q9ZKB3
EDD_HELPJ
Phosphogluconate dehydratase (EC 4.2.1.12)
MPKHSLEQIKEKITERSKKTRELYLENTFNPKNQPKIESLGCANIAHVTASMPEHLKMPLGSHKRKHFAIITAYNDMLSAHQPFKNYPDLIKKELQEHNAYASVASGVPAMCDGITQGYEGMELSLFSRDVIALSTAVGLSHNVFDGAFFLGVCDKIVPGLLIGALSFGNLASVFVPSGPMVSGIENYKKAKARQDFAMGKINREELLKVEMQSYHDVGTCTFYGTANSNQMMMEFMGLHVANSSFINPNNPLRKVLVEESAKRLASGKVLPLAKLIDEKSILNALIGLMATGGSTNHTLHLIAIARSCGVILNWDDFDAISNLIPLLAKVYPNGSADVNAFEACGGLAFVIKELLKEGLLFEDTHTIMDTETQKGMQNYTKTPFLENDQLVYKDAVSHSLNTDILRPVSEPFAANGGLKILKGNLGRAVIKISAIKDEHRKVKARAIVFKTQSEFLERFKNKELERDFVAVLPFQGPKSNGMPELHKLTTNLGALQDMGYKVALVTDGRMSGASGKVPSAIHLSPEGALNGAIIKIKDGDLIELDAPNNALNVLEKDFEKRGINPLFLETLENLEKPTFGLGRELFTSLRLNANTAEEGGMSFGIKV
Catalyzes the dehydration of 6-phospho-D-gluconate to 2-dehydro-3-deoxy-6-phospho-D-gluconate. {ECO:0000255|HAMAP-Rule:MF_02094}.
Q9ZKD2
RSME_HELPJ
Ribosomal RNA small subunit methyltransferase E (EC 2.1.1.193) (16S rRNA m3U1498 methyltransferase)
MRFVYHPLAKEPTLKIEGESYIHLYRSRRIKSASRLDLRNLKDGFLYTYEHAEIAKKHALLRLVGVQPLEIMANKKTHLILSVIEIKNIEKILPFLNQLGVSKLSLFYADFSQRNEKIDSAKLERFQKILIHSCEQCGRSVLMELEAFSNTKEALKAYPKASVLDFNGETLPASADFEKGVIIGPEGGFSEQERGYFKEREIYRIPLDMVLKSESACVFVASIAQI
Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Q9ZKE5
CMOA_HELPJ
Carboxy-S-adenosyl-L-methionine synthase (Cx-SAM synthase) (EC 2.1.3.-)
MKDTLFNESLNKRFCFDEKVAHVFDDMLERSIPYYHEMLNLGAYFIAQNLKENVYHKSLPKPLIYDLGCSTGNFFIALNQQIQQDIELVGIDNSMPMLKKAQEKLKDFNNVRFECMDFLEVKFKEASAFSLLFVLQFVRPMQREVLLKKIYNSLALNGVLLVGEKIMSEDRILDKQMIELYYLYKQNQGYSHNEIAFKREALENVLVPYSLKENIALLESVGFKHVEALFKWVNFTLLVARKT
Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM). {ECO:0000255|HAMAP-Rule:MF_01589}.
Q9ZKF6
RS1_HELPJ
Small ribosomal subunit protein bS1 (30S ribosomal protein S1)
MSKIADDQYFNDEEEDFAKLLEKEETLEKGTIKEGLIVSINENDGYAMVSVGGKTEGRLALNEITDEKGQLMYQKNDPIVVHVSEKGEHPSVSYKKAISQQKIQAKIEELGENYENAIIEGKIVGKNKGGYIVESQGVEYFLSRSHSSLKNDANHIGKRIKACIIRVDKENHSINISRKRFFEVNDKRQLEISKELLEATEPVLGVVRQITPFGIFVKFKGIDGLVHYSEISHKGPVNPEKYYKEGDEVYVKAIAYDEEKRRLSLSIKATIEDPWEEIQDKLKPGYAIKVVVSNIEHYGVFVDIGNDIEGFLHVSEISWDKNVSHPSHYLSVGQEIDVKIIDIDPKNRRLRVSLKQLTNRPFDVFESKHQVGDIVEGKVATLTDFGAFLNLGGVDGLLHNHDAFWDKDKKCKDHYKIGDVIKVKILKINKKDKKISLSAKHLVTSPTEEFAQKHKTDSVIQGKVVSIKDFGVFIHADGIDVLIKNEDLNPLKKDEIKIGQEITCVVVAIEKSNNKVRASVHRLERKKEKEELQAFNTSDDKMTLGDILKEKL
Binds mRNA thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence (By similarity).
Q9ZKH1
CMOB_HELPJ
tRNA U34 carboxymethyltransferase (EC 2.5.1.-)
MLICNDKFNPKTLLEEIMALRPWRKGPFEISQIKIDSEWDSSIKWDLVKNATPLKDKVVADVGCNNGYYLFKMLEHKPKSLVGFDPGVLVKKQFEFLAPFFDKEKKIIYESLGVEDFHEKYPNAFDVIFCLGVLYHRKSPLEALKALYHALKIKGELVLDTLIIDSPLDIALCPKKTYAKMKNVYFIPSVSALKGWCERVGFENFEILSVLKTTPKEQRKTDFILGQSLEDFLDKTDHSKTLEGYDAPLRGYFKMLKPSKR
Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs. {ECO:0000255|HAMAP-Rule:MF_01590}.
Q9ZKM2
FTSZ_HELPJ
Cell division protein FtsZ
MVHQSEMENYNIGQASIEEVSDPAYKGAKIVVVGVGGGGSNMIKHLVEYGVHQDVTPIATNTDGQHLKNNPAPVKILLGKESTGGLGAGGVPDIGKKAAEESADEIREAIKDAKLVIVSTGLGGGTGTGATPTIVKIAKEVGALTIAIVTKPFKYEGNQKRKRAEEGLKELEQSSDSILVIPNDKILLTMKKNASTTECYREVDDVLVRAVSGISTIITKPGNINVDFADLKSALGFKGFALMGIGEATGEDSAKLAVQNAIQSPLLDDASIEGAKSIIVFFEHHPDYPMMAYSQACDFIQDQAHQDVDVKFGQHTSENIPIDHVRVTIIATGSERNSNGAGLESIATPSQPVVKPTRKVGNGEYLRIPTEEELSIPTTIRIQQD
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. {ECO:0000255|HAMAP-Rule:MF_00909}.
Q9ZKM3
FTSA_HELPJ
Cell division protein FtsA
MEHKEIVIGVDIGSRKICAIVAEFKDGILRIIGTAHQDSKEINSKAIKRGRINSLAHASNAIKEVINSAKKMAGLNADEDRNNPISSFRESYHPKTKAIVSFSGAYTESIRDVTGVASTKDNVVTIDEINRAINNACAKAGLDNDKHILHALPYRFTLDKQEVNDPLGMSGTRLEVFIHIVYTEKNNIENLEKIMIQSGVEIENIVINSYAASIATLSNDERELGVACVDMGGETCNLTIYSGNSIRYNKYLPVGSHHLTTDLSHMLNTPFPYAEEVKIKYGDLSFESGAETPSQSVQIPTTGSDGHESHIVPLSEIQTIMRERALETFKIIHRSIQDSGFEEHLGGGVVLTGGMALMKGIKELARTHFTNYPVRLATPVEKYNIMGMFEDLKDPRFSVVVGLILYKAGGHTNYERDSKGIIRYHESDDYIRKAHQSNPTPHIHSSPTERNLSDLKTPSAPLNTAKNDDFLPIKPTEQKGFFQNLLDKISKIF
Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. {ECO:0000255|HAMAP-Rule:MF_02033}.
Q9ZKM6
GATC_HELPJ
Glutamyl-tRNA(Gln) amidotransferase subunit C (Glu-ADT subunit C) (EC 6.3.5.-)
MQIDDALLQRLEKLSMLEIKDEHKESVKGHLAEVLGFVENIFALETNNLKTDTHLSTPLREDEPKSQPHIAKEILSQNKHSQDHYFVVPKIIE
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 phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Q9ZKP2
GTPC1_HELPJ
GTP cyclohydrolase 1 type 2 (EC 3.5.4.16) (GTP cyclohydrolase I)
MALVKEVLEVLNRLSPFELQESWDNSGLNVGSGNSEFSQIIACLEITLQIALNAQENALIITHHPLIFKPLKTLNDEAYPGNILKILIQKNISVISMHTNFDKTHLNKHFARALLRFDGLIEKGLMLVKENANIEFDVLLEKIKLSLGVGQLACVKSSQMIKDLAFVCGSGASMFSSLKAQSCLITGDVKYHDAMIAQSLGISLIDATHYYSERGFALIVAEILHSFNYLVTIENFKNPLQII
Converts GTP to dihydroneopterin triphosphate.
Q9ZKP6
LGT_HELPJ
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase (EC 2.5.1.145)
MNAWNTIYERFNPIAFSLGGIEVHWYGLAYACAIVVAFYMALRMIQKDPKRFPIERKEFESYFLWAELGIVLGARIGYVLIYEPNSSYYLTHFWQIFNPFDSHGNFIGIRGMSYHGGLVGFLIASYLYSRKDLKKLLIYLDLIAISLPLGYVFGRIGNFLNQELFGRIVPKDSHLGQIIGIMVDNELRYPSQLIEAFLEGVVVFLMVMWAKKHTKTHGLLIVVYGLGYSLMRFIAEFYREPDSQLGVYFLNLSMGQILSVFMVIVSLGILLYATKNSKKIKEE
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}.
Q9ZKP7
RDXA_HELPJ
Oxygen-insensitive NADPH nitroreductase (EC 1.-.-.-)
MKFLDHEKRRQLLNERHSCKMFDSHYEFSSTELEEIAEIARLSPSSYNTQPWHFVMVTNKDLKKQIAAHSYFNEEMIKSASALMVVCSLKPSELLPTSHYMQNLYPESYKVRVIPSFAQMLGVRFNHSMQKLESYILEQCYIAVGQICMGVSLMGLDSCIIGGFDPLKVGEILEERINKPKIVCLIALGKRVAEASKKSRKSKVDAITWL
Reduction of a variety of nitroaromatic compounds using NADPH as source of reducing equivalents two electrons are transferred.
Q9ZKQ2
RLMH_HELPJ
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)
MRCVVYSIAKNSPLELVKSYQKQCKRFDCELELVDLFPKNTANAQKVSKELAQKSYSLAFEPYLSPKAKNIALHPEAQRGDSFAFSKMLENHLNINFFIAGAYGFEEKFLKDCQAWSLSEMTFSHEVAKIVLCEQIYRALSIIFKHPYHK
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00658}.
Q9ZKQ7
DADA_HELPJ
D-amino acid dehydrogenase (DAD) (EC 1.4.5.1)
MKKEVVVIGGGIVGLSCAYSMHKLGHKVCVIEKSDGTNGTSFGNAGLISAFKKAPLSCPGVVLDTLKLMLKNQAPLKFHFGLNLKLYQWILKFMTSANAKSTHRTIALFERYGWLSIDMYHQMLKDGMDFWYKEDGLLMIYTLEESFEKKLKTCDNSGAYKILNVKETKEYMPIANDNICGSVLLTENAHVDPGEVVRSLQQYLQNAGVEFLYNEEVIDFEFKNNLIEGVITHKEKIQAETIILATGANPTLIKKTKNDFLMMGAKGYSITFKMPEELKPKTSSLFADIFMAMTPRRDTVRITSKLELNTNNALIDKEQIANMKKNLAAFTQPFEMKDAIEWCGFRPLTPNDIPYLGYDKRYKNLIHATGLGWLGITFGPAIGKIIANLSQDGANEKNADIMLFSAFFRD
Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity is mostly active on D-proline, and to a lesser extent, on several other D-amino acids such as D-alanine, D-phenylalanine and D-serine. Mediates electron transport from D-proline to coenzyme Q1 in vitro, and is involved in the electron transport chain from D-proline to the c-type cytochrome in vivo.
Q9ZKS0
SURE_HELPJ
5'-nucleotidase SurE (EC 3.1.3.5) (Nucleoside 5'-monophosphate phosphohydrolase)
MKKILLTNDDGYHAKGIKALEQALENMAEIYVVAPKHEKSACSQCITITAPLRAEKIKGKEGRHYRIDDGTPSDCVYLAINELFKHVCFDLVISGINLGSNMGEDTIYSGTVAGAIEGTIQGVPSIAISQILSNKNKNTPLSFDLAQKIIQDLVQNVFTKGYPLKGRKLLNVNVPNCSLQEYKGERITPKGYRLYKKEVHKRTDPKNESYFWLGLHPLKWQKRENEDRLSDFDAIASNHASITPLNLDLTSYDDLKSLESWHEGMLK
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. {ECO:0000255|HAMAP-Rule:MF_00060}.
Q9ZKS6
RECR_HELPJ
Recombination protein RecR
MNTYKNSLNHFLNLVDCLEKIPNVGKKSAFKMAYHLGLENPYLALKITHALRNALENLKTCASCNALSETEVSEICSDESRQNSQLCMVLHPRDVFILEDLKDFLGRYYVLNSIEDVDFNALEKRLIGENIKEIIFAFPPTLANDSLMLYIEDKLQHLHLTFTKIAQGVPTGVNFENIDSVSLSRAFNSRIKA
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. {ECO:0000255|HAMAP-Rule:MF_00017}.
Q9ZKU8
HYPB_HELPJ
Hydrogenase/urease maturation factor HypB
MSEQRKESLQNNPNLSKKDIKIVEKILSKNDIKAAEMKERYLKEGLYVLNFMSSPGSGKTTMLENLADFKDFKFCVVEGDLQTNRDADRLRKKGVSAHQITTGEACHLEASMIEGAFDLLKDEGALEKSDFLIIENVGNLVCPSSYNLGAAMNIVLLSVPEGDDKVLKYPTMFMCADAVIISKADMIEVFNFRVSQVKEDMQKLKPEAPIFLMSSKDPKSLEDFKNFLLEKKRENYQSTHSF
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion.
Q9ZKW2
Y889_HELPJ
Probable iron chelatin transport system permease protein jhp_0822
MLKTYHIALACVILAVVVLLFGGESLSLEEWQEVCLNVKNHFLHNEELSSLSVIILEIRLPRVILALLVGASLSGSGVVMQTILRNPLVDPFLLGISSGAMLGVAMAIAVVESNIAILAFFGAILPSLAVLAMNRVLGNSVLSLVLSGVVLSAFLSALAGAIKFFVIPQKAQAIVVWLLGSLSLSSYKDCLIAFIGLSLGFIPLFLLRWRINLLSLSDAQSLSLGINPVLLRSLCLVCVSVASALAVSVSGTIGWIGLVIPHVARLFFGANLQKLLLSSLLMGAFFLLLADVVAKTITPYDLPVGIATSVLGAPFFLWLLFRTRGV
Part of a binding-protein-dependent transport system for an iron chelatin probably responsible for the translocation of the substrate across the membrane.
Q9ZKW3
Y888_HELPJ
Probable iron chelatin transport ATP-binding protein jhp_0821
MVLEVKNLSFKYSQKLILDKLSFSVPKNSITSILAPNGSGKTTLLKCLLGLLKPLEETEIKACNKDILPLKPYEKAKLIAYIPQVEYYAFNFSVLDFVLMGKATHLNLFAMPKAKHIKEATSVLERLDLESLKDQGINDLSGGQRQMVLLARSLLQRTPLLLLDEPTSALDLKNQALFFDAIKDEMKKRELSVLVNIHDPNLVARHSTHVVMLKDKKLFLQASTPIAMTSHNLSALYDTPLEAIWHDDKLVVYAL
Part of a binding-protein-dependent transport system for an iron chelatin. Probably responsible for energy coupling to the transport system (Potential).
Q9ZKW7
MURJ_HELPJ
Probable lipid II flippase MurJ
MANILGAGVYSDIFFVAFKLPNLFRRIFAEGSFSQSFLPSFIRSSIKGGFASLVGLIFCGVLFMWCLLVALNPLWLTKLLAYGFDEETLKLCTPIVAINFWYLLLVFITTFLGALLQYKHSFFASAYSASLLNLCMILALLISKEKTHLEALYYLSYGVLLGGVAQILLHFYPLVKLGLWDLLFKGLLGFKTKNTNKKEYRLNRAKKDLKAFFKQFFPSVLGNSSAQIASFLDTTIASFLASGSVSYLYYANRVFQLPLALFAIAISTALFPSIAIALKNNQQDLILQRLQKAWFFLVGVLLLCSIGGIMLSKEITELLFERGQFSPKDTLITSQVFSLYLLGLLPFGLTKLFSLWLYAKLEQKKAAKISLISLFLGLAASLSLMPLLGVLGLALANSLSGLFLFVLTIKAFGFQSFLGIIKNLKSWLVILFLACVEILLLLAFKSWVTHLYLFYYFQGF
Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_02078}.
Q9ZKW9
RUVA_HELPJ
Holliday junction branch migration complex subunit RuvA
MIVGLIGVVEKISALEAHIEVQGVVYGVQVSMRTAALLQTGQKARLKILQVIKEDAHLLYGFLEESEKILFERLLKINGVGGRIALAILSSFSPNEFENIIATKEVKRLQQVPGIGKKLADKIMVDLIGFFIQDENRPARNEVFLALESLGFKSAEINPVLKTLKPHLSIEAAIKEALQQLRS
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA. {ECO:0000255|HAMAP-Rule:MF_00031}.
Q9ZKY2
LPXB_HELPJ
Lipid-A-disaccharide synthase (EC 2.4.1.182)
MPTILVSALEASSNIHLEELRHNLPKDYRFIGVFESKEALYSPREFSIMGFRDVIGRLGFLLKAHKEMVQLAKQADMVLLMDSSSFNIPLAKKIKKQDPHKKIMYYILPQVWAWKKWRAKSLEKYCDFLGAILPFEVGYYQKKAQYVGHPLLDEIKYYKKDIKGETLVFMPGSRKSEIAKMFPLFVKAAQILEQNEGFKRRVLVVPSFFKGLDLKALYGEDIKLFEISYDAHKSLFEAEFAFICSGTATLEAALIGTPFALAYRAKTMDFLIARMLVNLHYIGLANIFYNALNNETPGLGESQLHPELIQHFLSVEGLLKAYEEMDRERYFKESLRLREYLKHGSARKIAEEMAFLLNLT
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.
Q9ZKY3
DUT_HELPJ
Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase)
MKIKIQKIHPNALIPKYQTEGSSGFDLHAVEEVVIKPHSVGLVRIGICLSLEVGYELQVRTRSGLALNHQVMVLNSPGTVDNDYRGEIKVILANLSDKDFKVQVGDRIAQGVVQKTYKAEFIECEQLDETSRGSGGFGSTGVSKA
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}.
Q9ZKY5
PGBB_HELPJ
Plasminogen-binding protein PgbB
MNKPFLILLIALIAFSGCNMRKYFKPAKHQIKGEAYFPNHLQESIVSSNRYGAILKNGAVIGDKGLTQLRIGKNFNYESSFLNESQGFFILAQDCLNKIDKKTSKSRAAKTEETELKLKGVEAEVQDKVCHQVELISNNPNASQQSIVIPLETFALSASVKGNLLAVVLADNSANLYDITSQKLLFSEKGSPSTTINSLMAMPIFMDTVVVFPMLDGRLLVVDYVHGNPTPIRNIVISSDKFFNNITYLIVDGNNMIASTGKRILSVVSGQEFNYDGDIVDLLYDKGTLYVLTLDGQILQMDKSLRELNSVKLPFASLNTIVLNNNKLYSLEKRGYVIEVDLNDFDSYNVYKTPTIGSFKFFSSNRLDKGVFYDKNRVYYDRYYLDYNDFKPKLYPHAAEFKTSQKGEKGNAPIYLQERHKAKENKQPLEENKVKPRNSGFEEEEVKTRRPEPTKDQNNAIQQGETKNNESKNTPISKENAAKKEAPKPSSKEEKRRLKEEKKKAKAEQRAREFEQRAREHQERDEKELEERRKALEMNKK
Binds plasminogen, specifically, and in a concentration and lysine-dependent manner. Plasminogen is the precursor of plasmin, a serine protease that cleaves fibrin, fibronectin, laminin and vitronectin. Acquisition of plasminogen/plasmin could enable H.pylori to degrade host components (By similarity).
Q9ZKZ2
GUAC_HELPJ
GMP reductase (EC 1.7.1.7) (Guanosine 5'-monophosphate oxidoreductase) (Guanosine monophosphate reductase)
MKVFDYEDVQLIPNKCIVNSRSECDTTVILGKHAFKMPIVPANMQTIINESIAEFLAENGYFYIMHRFNGSARIPFVKKMKERQLISSISVGVKKEECLFVEELAKQGLTPDYITIDIAHGHSNSVIEMIQRIKTRLPETFVIAGNVGTPEAVRELENAGADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEESSGETKIENGIAYKEYFGSASEFQKGEKKNIEGKKIWIQHKGSLKNTLIEMHQDLQSSISYAGGRDLEAIRKVDYVIVKNSIFNGDTI
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. {ECO:0000255|HAMAP-Rule:MF_01511}.
Q9ZL08
DBH_HELPJ
DNA-binding protein HU
MNKAEFIDLVKKAGKYNSKREAEEAINAFTLAVETALSKGESVELVGFGKFETAEQKGKEGKVPGSDKTYKTEDKRVPKFKPGKILKQKVEEGK
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
Q9ZL09
DER_HELPJ
GTPase Der (GTP-binding protein EngA)
MNTSHKTLKTIAILGQPNVGKSSLFNRLARERIAITSDFAGTTRDINKRKIALNGHEVELLDTGGMAKDALLSKEIKALNLKAAQMSDLILYVVDGKSIPSDEDLKLFREVFKTNPNCFLVINKIDNDKEKERSYAFSSFGTPKSFNISVSHNRGISALIDAVLNALNLNQIIEQDLDADILESLETPNNALEETKEEEIIQVGIIGRVNVGKSSLLNALTKKERSLVSSVAGTTIDPIDETILIGDQKICFVDTAGIRHRGKILGIEKYALDRTQKALEKSHIALLVLDVSAPFVELDEKISSLADKHSLGIILILNKWDIRYAPYEEIMATLKRKFRFLEYAPVITTSCLKARHIDEIKHKIIEVYECFSKRIPTSSLNSVIFQATQKHPLPSDGGKLVKVYYATQFATKPPQISLIMNRPKALHFSYKRYLINTLRKEFNFLGTPLILNAKDKKSVQQN
GTPase that plays an essential role in the late steps of ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}.
Q9ZL13
GATA_HELPJ
Glutamyl-tRNA(Gln) amidotransferase subunit A (Glu-ADT subunit A) (EC 6.3.5.7)
MITLKQALSLSQDELETLKNEIDAKVRASDLNAYIKAPSLNGASAKGVPILIKDNISVKGWEITCSSKILEGYVAPYHASAIENLHQNGMAGFGLSNMDEFAMGSTTESSCYGITKNPRDKNIVPGGSSGGSAAAVAGGLTVAALGSDTGGSIRQPASYCGCVGLKPTYGRVSRYGVIAYRSSFDQIRPITQNVEDASILFDAISGYDSKDSTSANLKPTHTFINLIRDKRFKIAILRDHINDASNEVQLAYENTIKALKEMGHEVVEKKMLDSHYQISIYYIISMAEASSNLARFDGVRYGRRAQNVKDLKELYLKSRSEGFGDEVKRRIMLGNFVLSSGYYDAYYLKAQQMRLMIKEQYNKIFEEVDLIFTPVAPTTAYLFNYHASPLEMYLSDIYTIGANLSGLPALSLPVAKDPLGLPIGMQFIAKAFDEQSLLDVSYALEQELDLKLD
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) (By similarity).
Q9ZL15
ATP6_HELPJ
ATP synthase subunit a (ATP synthase F0 sector subunit a) (F-ATPase subunit 6)
MEHRVFTIANFFSSNHDFITGFFVVLTAVLMFFISLGASRKMQMVPMGLQNVYESIISAILSVAKDIIGEELARKYFPLAGTIALYVFFSNMIGIIPGFESPTASWSFTLVLALIVFFYYHFEGIRVQGFFKYFAHFAGPVKWLAPFMFPIEIISHFSRIVSLSFRLFGNIKGDDMFLLIMLLLVPWAVPVAPFMVLFFMGILQAFVFMILTYVYLAGAVLTDEGH
Key component of the proton channel it plays a direct role in the translocation of protons across the membrane. {ECO:0000255|HAMAP-Rule:MF_01393}.