entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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|---|---|---|---|---|
Q9ZE96
|
PGSA_RICPR
|
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5) (Phosphatidylglycerophosphate synthase) (PGP synthase)
|
MRIDKNLPNYLTIARIMVIPVIILLFYINNSLARKLGALLFVLASITDFFDGYIARKYNLVTSFGKMFDPIADKLLVGCVTIMLLKKDNVDEIPCLLILAREFLVSGLREFLALVKVSVPVSRLAKLKTFLQMFALSILILGSKGSGIIYLDIVGEIILWIAAFLTIITGYSYFKACKTYF
|
This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
|
Q9ZE97
|
YIDC_RICPR
|
Membrane protein insertase YidC (Foldase YidC) (Membrane integrase YidC) (Membrane protein YidC)
|
MNNNIINLIAAVVLSLSIIFGWQYFFVKPEQKKQQQRIAMHKSENLNKQKLKALAEPASDIAVQEASQVQRIKIESESLTGSIALKGLRFDDLILKKYKQDLSQNSPAVRLFSPANTENAYFAEIGLVSNLNSVKLPNSNTVWNSDSEVLSPEKPVNLFWINEDGIKFLVTITVDKNYLFTIEQTIINNSDKELPVQSYGLINRKYISLEKAVNILHQGPIGCIDENLKEYSYDDIKDKKSTKFALSKVDWIGITDKYWLSSLIPDKSSRYSSNFNYALKQGTERYQVDFISPVQVIKPGENLSIKSRIFAGAKKVDLLDEYEKSYDIKLFDRAIDFGWFYIITKPVFYAMNFFYGYVGNFGISILIVTVIIKLLMFTLANKSYRSMKKMKNLQPEIDRIKNLYNNDKARLNQEIMALYKKEKVNPVAGCLPILVQIPVFFSIYKVLYVTIEMRQAPFFGWIKDLSSPDPTTIFNLFGLLPFAPPSFLMIGAWPILMAITMFLHQKMSPELADPIQAQVMKFMPLIFLFMFSSFPVGLLIYWSWNNILSIIQQYYINKFN
|
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}.
|
Q9ZE99
|
LGT_RICPR
|
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase (EC 2.5.1.145)
|
MLNELNNLFMILPNINPIIFSIGPFSISWYSLAYVVGILLGWFYATKIIEKFKPEITKKHIDDFITYAIIAIIVGGRLGYVLLYNPLKYFTNPIEILKTYEGGMSFHGATIGIIMAAYLFCQKYKINFLSLTDIITTVAPIGLFLGRIANFINCELYGRITNSSFGIIFPNSDLQPRHPSQLYEAFFEGLILFCILTYAVFRHDTLKKRGLNSGIYLIFYSLFRIIIEMFREPDIQIGFILDSLTMGQILSAPMLLLGSYLICRSNPK
|
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}.
|
Q9ZEA3
|
TILS_RICPR
|
tRNA(Ile)-lysidine synthase (EC 6.3.4.19) (tRNA(Ile)-2-lysyl-cytidine synthase) (tRNA(Ile)-lysidine synthetase)
|
MLYEKFEYNINNLIGNFGLSKIAIAVSGGSDSISLLYLANIWARKNNIELFVISVDHNLRPQSKQENYYIHTISSNLNRKYYNLSFDHQNNFSNLQERAREGRYDLMTNLCLELDVLVLLTAHHEDDYVENFCLRLERNSGIFGLSSSNIHWYNNIQIIRPLYNIPKSELVEYLVNHKIKWFEDESNLSDKYRRNIIRQKLFKEENYIKAEISLQQLKTNKLIEDELKPALISAIAEAVKIFEYGFTFLDLVKFDKFLNEVKAQIINFLLIMISGQSRSARFYSIAHILKLISQDINFKNTVHGCVIKRIQNELLIYREFGKKLPKSKILLDKSVIWDNRFCITKNQKTPDCVITYLSLADYKAIKKQLDLKHLKNLSCKNHNAILFTLPIIKILEKVIAIPHISYYDNDVWNFEVSFAPNFVSRFTHFC
|
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. {ECO:0000255|HAMAP-Rule:MF_01161}.
|
Q9ZEA4
|
RL9_RICPR
|
Large ribosomal subunit protein bL9 (50S ribosomal protein L9)
|
MEVILIKPVRKLGKIGDILKVADGFGRNYLLPQKLAIRATKSNKELIVKQKYEFEEKDKQVREEVEKINTIIKDQQLVFIRQTSDDCKLFGSVTNKDIADKLSKNISYNISHSNIILDKQIKSTGIYTVEIRLHAELTSIVTVVVARSESEAQDYLREQKAETLEDVDETA
|
Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00503}.
|
Q9ZEA5
|
RS18_RICPR
|
Small ribosomal subunit protein bS18 (30S ribosomal protein S18)
|
MLKSNNASETATSKGVDKAAKKVFFRRRKGCPLSVPNAPVIDYKNPELLIKFVSEGGRMLPSRITNVCAKKQRKLNNAIKIARILALLPFVFQAK
|
Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_00270}.
|
Q9ZEA6
|
RS6_RICPR
|
Small ribosomal subunit protein bS6 (30S ribosomal protein S6)
|
MSFYESVFIIRQDVSLNDIDKIVDDFTKIIKDNNGTIIKKEYWGLRTLAYKIGNNKKGHYYFLGIDITSNVKEELERKMKLNENIIRFLTIKADSISSEPSPILKNQSTENTPVIDVTINN
|
Binds together with bS18 to 16S ribosomal RNA.
|
Q9ZEB6
|
RECF_RICPR
|
DNA replication and repair protein RecF
|
MKNIFLHSLTLENYRNFKNLELKTDNTPIILTGENGSGKTNILEAISLFYPGRGLRSSKLTDICKTSEDYCKVKTLLQSKLGLAELSTHIKRSSNRRITEYNASKIANNELSKFTNMVWLTPQMEGIFTSSSTDRRKFLDRIVYNFDTKHAALLNKYEYYMHERNKILAEDIRDNNWLKIIEEKMADISNNIANNRLKTIRFIQQAIDDIENEFPKADLSIDGIIEQKILNVEGDIVNFIITELYKTRSKDKLLGRTSFGIHKSDFLVKHQKKNILAKFCSTGEQKAILIAIILAEINSTIKLTKITPILLLDEIFVHLDDKRRQYLMGFFNALNIQLWVTATDLDGIENFANKAQLIKL
|
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).
|
Q9ZEB9
|
DSB_RICPR
|
Putative protein-disulfide oxidoreductase RP025 (EC 1.8.-.-)
|
MRNIFIVLIFLFLSNCSEVKAQDKKYEGKQIIVQEPLQNNKTPQETNQESINSATKSVVHNNDNNQTEEVLIHDSREQKKPEIRPTKVTFKIDDNDMVLGNKKSNVIVVEYFSPTCPHCAYYHQTIFPELKKKYIDTNKIAYVIREFIATKQDLDAAILARCKGDINSFIQFHNIILQQQDKWAYSNKYRELLTDIGQLGGIPPEEYKQCLNSDKITATLIANTNLVAKAPKFIGTPSFFVNGVQTENYSIDNISKAVDKALDDETKKQINF
|
May be required for disulfide bond formation in some proteins.
|
Q9ZEC1
|
ATP6_RICPR
|
ATP synthase subunit a (ATP synthase F0 sector subunit a) (F-ATPase subunit 6)
|
MTHSPLIQFNIKKLIDIKMFGFDVSFTNSSIYMLLATTLSLTYLYLAFYNRKLIPSRLQVSAEIVYNLVADMLNQNIGIKGRKFIPLVFSLFIFILFCNLLGMTPYSFTATSHIIVTFTLALLIFLTVTIVGFIKHGVSFLTLFLPHGTPVWLAPLMIVIELFTYLARPVSLSLRLAANMMAGHVLLKVIASFTVSLMIYLKFLPIPLMVILIGFEIFIAILQAYIFTILSCMYLNDAINLH
|
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}.
|
Q9ZEC4
|
ATPF_RICPR
|
ATP synthase subunit b (ATP synthase F(0) sector subunit b) (ATPase subunit I) (F-type ATPase subunit b) (F-ATPase subunit b)
|
MNFLDESFWLTISFVIFVYLIYRPAKKAILNALDTKISEIQEKVLKAKKLKEDAALLFEQTKLQIQKLETLRSQMIEESDKATKQIIQDKTKEMEEFLERKKADAIQLIQNQKSTASKDLQDEFCDEVITLVSKYFRSAKLSEKSIAKNLMDKSDFVHNDSKATYLH
|
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}.
|
Q9ZED0
|
TSAE_RICPR
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaE (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE)
|
MHTLNSKKETKNFAKLFAQNLKPNDIVLLNGDLGAGKTFFCREIIKHFCGKNTNIISPTFNLLQIYKTPKFNIYHYDMYRIKSPEEIYELGFEEALNGNLILIEWSEIIKHLLTPPLIEVNLKVLDNNKRLCSIHKENFLFDFL
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB. TsaE seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity).
|
Q9ZED3
|
LPXD_RICPR
|
UDP-3-O-acylglucosamine N-acyltransferase (EC 2.3.1.191)
|
MVSSNFYKNLGPRKLTAIVDFLHDIIEPTKIYEDIDIYDIKILQEASPNDISFLSNPKYSEFLKTTKAAACIVPKNFTEEVNQNTVLIHAENSYFAYSKLIDFFYAPIKSYSTKIMKSAIIADSATIGKNCYIGHNVVIEDDVIIGDNSIIDAGTFIGRGVNIGKNARIEQHVSINYAIIGDDVVILVGAKIGQDGFGFSTEKGVHHKIFHIGIVKIGNNVEIGSNTTIDRGALQDTIIEDLCRIDNLVQIGHGVKIGKGSIIVAQAGIAGSSAIGKYCALGGQVGIAGHLNIGDGTQVAAQGGVAQNIEEGKIVGGSPAVPIMDWHRQSIIMKQLVKTSNSKLKK
|
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}.
|
Q9ZED5
|
LPXA_RICPR
|
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (UDP-N-acetylglucosamine acyltransferase) (EC 2.3.1.129)
|
MSNSNIHTTAIIAEGAKFGKNVKVGPYCIIGPEVVLHDNVELKSHVVIDGITEIGENTVIYPFASIGQPPQILKYANERSSTIIGSNNTIREYVTVQAGSKSGGMITRVGNNNLFMVGVHIGHDCKIGNNLVFANYVSLAGHIKVGDYAIIGGLSAVHQYTRIGEYSMIGGLSPVGADVIPFGLVSSKRAVLEGLNLIGMNRKGFDKADSLTALNAVEEIFLGEGNFVDRIKQVAEKYKNNSIVTQIIDFLNQDSSRAFCHFKK
|
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}.
|
Q9ZEE0
|
THIO_RICPR
|
Thioredoxin (Trx)
|
MVNNVTDSSFKNEVLESDLPVMVDFWAEWCGPCKMLIPIIDEISKELQDKVKVLKMNIDENPKTPSEYGIRSIPTIMLFKNGEQKDTKIGLQQKNSLLDWINKSI
|
Component of the thioredoxin-thioredoxin reductase system. Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity).
|
Q9ZEF9
|
FLOA_PRIM3
|
Flotillin-like protein FloA
|
MEVGSVLFFVVIGLAIIALAVFFTFVPIMLWISALAAGVRISIFTLVGMRLRRVIPSRVVNPLIKASKAGLGITINQLESHYLAGGNVDRVVNALIAAHRANIELTFERGAAIDLAGRDVLEAVQMSVNPKVIETPFIAGVAMDGIEVKAKARITVRANIDRLVGGAGEETIIARVGEGIVSTIGSQTDHKKVLENPDMISQTVLGKGLDSGTAFEILSIDIADIDIGKNIGAVLQTDQAEADKNIAQAKAEERRAMAVAQEQEMRAKVEEMRAKVVEAEAEVPLAMAEALRSGNIGVMDYMNIQNLTADTDMRDSIGKMSKEDDEK
|
Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity. {ECO:0000255|HAMAP-Rule:MF_01562}.
|
Q9ZEH3
|
UVRC_STAAU
|
UvrABC system protein C (Protein UvrC) (Excinuclease ABC subunit C)
|
MEDYKKRIKNKLNVVPMEPGCYLMKDRNDQVIYVGKAKKLRNRLRSYFTGAHDAKTTRLVGEIRRFEFIVTSSETESLLLELNLIKQYQPRYNILLKDDKSYPFIKITKEKYPRLLVTRTVKQGTGKYFGPYPNAYSAQETKKLLDRIYPYRKCDKMPDKLCLYYHIGQCLGPCVYDVDLSKYAQMTKEITDFLNGEDKTILKSLEERMLTASESLDFERAKEYRDLIQHIQNLTNKQKIMSSDKTIRDVFGYSVDKGWMCIQVFFIRQGNMIKRDTTMIPLQQTEEEEFYTFIGQFYSLNQHILPKEVHVPRNLDKEMIQSVVDTKIVQPARGPKKDMVDLAAHNAKVSLNNKFELISRDESRTIKAIEELGTQMGIQTPIRIEAFDNSNIQGVDPVSAMVTFVDGKPDKKNYRKYKIKTVKGPDDYKSMREVVRRRYSRVLNEGLPLPDLIIVDGGKGHMNGVIDVLQNELGLDIPVAGLQKNDKHQTSELLYGASAEIVPLKKNSQAFYLLHRIQDEVHRFAITFHRQTRQKTGLKSILDDIDGIGSKRKTLLLRSFGSIKKMKEATLEDFKNIGIPENVAKNLHEQLHK
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. {ECO:0000255|HAMAP-Rule:MF_00203}.
|
Q9ZEJ0
|
DNAK_METHO
|
Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70)
|
MAKEFILGIDLGTTNSVVSVIENGTPKILENPNGKRTTPSVVAFKNGETIIGESAKRQLESNKDSVASIKRLMGTSQTVHLNNKDYKPEEISAMILSYMKDYADKKLGQPVKKAVITVPAYFDNAQREATKNAGIIAGLDVVRIINEPTAAALAFGLNKDKNENQKILVFDLGGGTFDVSLLEMESGTFEVLATAGDNHLGGDDWDHEIVKWMVEQIKSKYNFDPTTDKMAMARLKEEAERAKITLSEQLIANISLPFLAMNENGPVNVELEITRATFESMTEHLLQRTRKPLLDVLSEAKLTWNDINEVLLVGGSTRMPAVQKLVAEVTNKKPNNSINPDEVVSVGAAIQGAILAGEIQDVLLLDVTPLTLGIVVEGDVVAPLIPRNTTIPVTKSQIFSTAVDNQTAVTIVITQGERQLARDNKILGQFNLEGIEPAPRGIPQIEVSFSIDVNGITKVTAKDKKTNKEQTITIQNTSSLSKEEVEKMVKDAEANREADQKKRHEIEVIVKAEQLSNDLEKTLKSEQAKNLGEPQKQELQKEIDEIKELINKKDIEQLEKKITEFEQKMAQAAEFLKKQQGNNNPNTNNDNPQTN
|
Acts as a chaperone.
|
Q9ZEJ6
|
DNAK1_NOSS1
|
Chaperone protein dnaK1 (HSP70-1) (Heat shock 70 kDa protein 1) (Heat shock protein 70-1)
|
MGKVVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFSKDGERVVGQMARRQTVLNPQNTFFAVKRYIGRRYNELSPESKRVPYTIRKDEVGNIKVACPRLNKEFSAEEISAMVLKKLADDASAYLGSAVTGAVITVPAYFNDSQRQATRDAGRIAGLEVLRILNEPTAASLAYGLDRGDTETILVFDLGGGTFDVSILEVGDGVFEVKATSGDTQLGGNDFDKKIVDWLAEQFLETEGVDLRRDRQALQRLMEAAEKAKIELSAVSITDINLPFITATEDGPKHLETRLTRSQFEGLCVDLLGRVRNPVKRALKDAGLRPDDIEEVVLVGGSTRMPMVKQLVRDLIGIEPSENVNPDEVVAMGAAIQAGILAGEFKDVLLLDVTPLSLGLEAIGGVMKKLIPRNTTIPVRRSDIFSTSENNQNSVEIHVVQGEREMAGDNKSLGRFKLYGIPPAPRGIPQIQVAFDIDANGILQVTALDRTTGREQSITIQGASTLSESEVNRMIQEAQKYADVDRERKERVEKRTRSEALILQGERQLREVALEFGMQFARNRRQRIDNISRELKESLKENDDRGIDQAYADLQDALYELNREVRQYYAEDEDDDLFATIKDIFVGDKDKERDLPRDSYRERDAYNNRDYGRDYGRDYGRDSRPSYDNSRPPRKSPRPSYQDNWDDDDDWL
|
Acts as a chaperone.
|
Q9ZEJ7
|
ISPT_TRIV2
|
Isoprenyl transferase (EC 2.5.1.-)
|
MTIQQTELQELPLDLKRELLPKHVAVIMDGNGRWAKRQGLPRIMGHKRGVDALKDLLRCCRDWGIQALTAYAFSTENWKRPQEEVEFLMTLFQRVLRQELREMVEENVQIQFVGNLAALPRSLQAEISRSMEATKNNRGIRFSVATNYGGRQEILQACRAIAQKVQQGLLQPDEIDEEVFERHLYTAGIADPDLLIRTSGEMRLSNFLLWQMAYGEIYITDTLWPDFDRTEFHRALCAYQQRERRFGKV
|
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. {ECO:0000255|HAMAP-Rule:MF_01139}.
|
Q9ZEQ8
|
MSRA_DICD3
|
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)
|
MIANFDKTQPIGQSDALPGRTTPMPVARLHVVNQHSMTHVPDHMEVAIFAMGCFWGVERLFWQQPGVYSTASGYCGGYTPNPTYREVCTGKTGHAEAVRVVFDPAVVSYPQLLQLFWENHNPAQGMRQGNDIGTQYRSAIYTLTTEQETAAKESYQRFQQAMRDAGNDHDITTEIQPAGPFYYAEDEHQQYLHKNPDGYCGLGGIGVCLPPQG
|
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 (By similarity).
|
Q9ZES5
|
SLAP_BACTF
|
S-layer protein (Parasporal protein)
|
MAKTNSYKKVIAGTMTAAMVAGVVSPVAAAGKSFPDVPADHWGIDSINYLVEKGAVTGNDKGMFEPGKELTRAEAATMMAQILNLPIDKDAKPSFADSQGQWYTPFIAAVEKAGVIKGTGNGFEPNGKIDRVSMASLLVEAYKLDTKVNGTPATKFKDLETLNWGKEKANILVELGISVGTTADKWEPKKTVTKAEAAQFIAKTDKQFGTEVAKVESAKAVTTQKVEVKFSKAVEKLTKEDVKLANKANNDKVLVKDVKLSEDKKSATVELYSNLAAKQTYTVDVNKVGKVEVTVGSLEAKTIEMADQTVVADEPTALKYTVKDENGTEVVSPAGIEFVTPAAEKINAKGEITLAKGTSTTVKAVYKKDGKVVAESKEVKVSAEGTAVASISNWTVAAEKADFTSKDFKQNDKVYEGDNVSVQVELKDQFNNVVNNVKAEYESLNTEVAVVDKATGKVTVLSAGKAPVKVTVKDSKGKELVSKTVEIEAFAQKAMKEIKLEKTNVALSTKDVTDFKVKAPVLDQYGKEFAAPVEVKVLDKDGKELKEQKLVAKYENKELVLNAHGQEAGKYTVELTAKSGKKEVKSKLALELKAPGVFSKFDVRGLENELDKYVTEENKKNEMVVSVLPVDANGLVLREKEAATLKVTTTDKDGKVVDATSGQVAVNDAAGTITVGNEAKAGETYKVTVVADGKLITTHSFKVVDTAPAAKKLAVDFTSTSLNEVAQGSELKTALLNILSVDGVPATTAGATVTDVKFVSADTNVVSEETAKFGTKGSTSIFVKELTVKKGEQTQKVELDKPVRVDVSIKEVKEVK
|
The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
|
Q9ZEU3
|
EFTU_APPPP
|
Elongation factor Tu (EF-Tu)
|
MSSKVFLRDKVHVNVGTIGHVDHGKTTLTAAITKILSTKGLAENKSYDQIDKTKEEKERGITINTTHVSYETVKRHYAHVDCPGHADYVKNMITGAAQMDAGILVVSAYHGVMPQTREHVLLAGQVGISKLIVFLNKCDLVKEEEWIHLVEMEVRELLNEYKFDGDKTPFVRGSALKALEGTDVEGINKLLEVLDEYIEDPIRDVEKPFLMPVEGVHTITGRGTVATGRVERGKIKISEEVEIIGLKETKKAIITGLEMFKKELDFAQAGDNVGILLRGITRDQIERGQVLAKPGSLNAYHKFLSQVYILTQQEGGRHTAFFSNYRPQFYFRTTDVTGFIKLKKDVKMVLPGDRTELIVELNHPIAIEAGTKFSIREGGRTIGAGTVTEIIE
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}.
|
Q9ZEU4
|
EFG_APPPP
|
Elongation factor G (EF-G)
|
MPRKFPLEKTRNIGIMAHIDAGKTTTTERILFHTGKIHKIGETHDGDSQMDWMKQEQERGITITSAATTAFWKEHRINIIDTPGHVDFTVEVSRSLRVLDGAVAVIDAKAGVEPQTETVWRQATEYKVPRIIFVNKMDKIGASFDYAVKTLYQRLGINASPIQLPIGSENEFKGIVDLLEMTGVEFLGTSDEKFKTIEIPEYMKEFAQNKRIELIEKWHNYDEELMMDYLNGKEITVEKLKNVIRQATLKADFFPVLCGSAFKNKGVKKILDAIIDYLPSPMDVSSIVGCNFENKEIIRKTSDNEPFTALAFKVMTDPYVGKLTFFRVYAGTIKTGSYVTNATKQVKERLGRLLQMHANSREEIKEVYAGDIVAAVGLKNTTPGDTLTSINDDIILESMNFPEPVIEIAIEPKTKADQDKIGIALSKLSEEHPTFKIYTNRETAQTIIAAMGELHLEIILDRLKTEFKVEANVNQPQVAYRETLTKISTTEGKFIRQSGGRGQYGHVIIRFEPNSDKGNEFINKIVGGVIPKEYIPAVKKGLEESLSNGILAGFPLIDVKATLIDGSYHDVDSSEIAFKIAASMALKQTKNEGNLVILEPIMEVEIITPNDYIGNVIGDLTSRRGKLENQDSRENTVIIKALVPLSEMFGYATILRSNTQGRASFIMQFLKYERAPKNIAEEIIKKRN
|
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).
|
Q9ZEU5
|
RS7_APPPP
|
Small ribosomal subunit protein uS7 (30S ribosomal protein S7)
|
LKNIMPELEVRSRRIGGQKYQIPSEVRPERKQSLGLRWLVQFAQKRNEKTMQQKLAKEIIDAASGNGLAVKKREEIHRMAEANKSFAHYRW
|
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 (By similarity).
|
Q9ZEU6
|
ECTC_CHRSD
|
L-ectoine synthase (EC 4.2.1.108) (N-acetyldiaminobutyrate dehydratase)
|
MIVRNLEECRKTERFVEAENGNWDSTRLVLADDNVGFSFNITRIHPGTETHIHYKHHFEAVFCYEGEGEVETLADGKIHPIKAGDMYLLDQHDEHLLRGKEKGMTVACVFNPALTGREVHREDGSYAPVD
|
Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant.
|
Q9ZEU8
|
ECTA_CHRSD
|
L-2,4-diaminobutyric acid acetyltransferase (DABA acetyltransferase) (EC 2.3.1.178)
|
MTPTTENFTPSADLARPSVADTVIGSAKKTLFIRKPTTDDGWGIYELVKACPPLDVNSGYAYLLLATQFRDTCAVATDEEGEIVGFVSGYVKRNAPDTYFLWQVAVGEKARGTGLARRLVEAVLMRPGMGDVRHLETTITPDNEASWGLFKRLADRWQAPLNSREYFSTGQLGGEHDPENLVRIGPFEPQQI
|
Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
|
Q9ZEY9
|
REPA2_BUCAI
|
Probable replication-associated protein repA2
|
MPRKNYIYNLKPFFNPSKNERKKSTFICYAMKKVSEIDVARSHLNRALLPIDPKTGNVLPRFRRLNKHRACAMRAIVPAMLYYFNINSKLVEASIEKLADECGLSTLSDSGNKSITRASRLISEFLEPMGFVKCKKINSKSMSNYIPKKIFLTPMFFMLCGISPSEINHFLSKKIKPLKKLKKQEKSAFISFTDMKIISQLDERSARTKILNALINYYTASELTKIGPKGLKKKIDIEYSNLCNLYKKKS
|
This protein is essential for plasmid replication it is involved in copy control functions.
|
Q9ZF60
|
GLTI_SALTY
|
Glutamate/aspartate import solute-binding protein
|
MQLRKLTTAMLVMGLSAGLAHAEDGAPAAGSTLDKIAKNGVIVVGHRESSVPFSYYDNQQKVVGYSQDYSNAIVEAVKKKLNKPDLQVKLIPITSQNRIPLLQNGTFDFECGSTTNNLERQKQAAFSDTIFVVGTRLLTKKGGDIKDFPDLKGKAVVVTSGTTSEILLHKLNEEQKMGMRIISAKDHGDSFRTLESGRAVAFMMDDALLAGERAKAKKPDNWEIVGKPQSQEAYGCMLRKNDPEFKKLMDDTIAQAQTSGEAEKWFDKWFKNPIPPKNLNMNFELSDEMKALFKAPNDKALN
|
Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Binds to both glutamate and aspartate.
|
Q9ZFA8
|
TRPD_CERS4
|
Anthranilate phosphoribosyltransferase (EC 2.4.2.18)
|
MSDRLKPLIGTAATRPLSREEAEFAFECLFEGEATPAQMGGLLMALRTRGETVDEYAAAASVMRAKCHKVRAPHGAIDIVGTGGDGKGTLNISTATAFVVAGAGVPVAKHGNRNLSSKSGAADALTEMGLNVMIGPEQVEACLLEAGIGFMMAPMHHPAMRHVGPVRAELGTRTIFNILGPLTNPAGVKRQLTGAFSPDLIRPMAEVLSALGSEKAWLVHGGDGTDELAISAASKVAALEGGQIREFELHPEEAGLPVHPFEEIVGGTPAENAQAFRALLDGAPGAYRDAVLLNAAAALVVADRAAHLREGVEIATDSILSGAAKAKVALLARLTNAA
|
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}.
|
Q9ZFB3
|
GERXC_BACAN
|
Spore germination protein XC
|
MKINRKGGLFLLMFLFLLTGCWDRRELEHVLFINTLGIDFKDNHYIIYPQFINFTNMAKQEGPANRNYSPAYIGKGEGKLLYDAAFDFYKSSQQKVSWEHIKSIVVTERFLKNGNLNQLNDFLSRFFQFRNTMWVFGTKEPLENILATNNIFNISSLYTIMNLPQETIRQSASVDPLRLYTFRSNYYEPGMTTRIPFLATTTEHWKQGHKAFWMLEFNEYGCIAAKSYVNHLNDSDIAGVRWTNKNTNRAPLLLKVKNRAIGELILKKPKIDTKVSIEKGKPHIVMNISLEGDIYQLMKPMPVHKVKKTLRISLKKK
|
May allow B.anthracis to germinate within phagocytic cells and therefore involved in virulence.
|
Q9ZFB4
|
GERXA_BACAN
|
Spore germination protein XA
|
MKRTVEVNESILRVWFEGCKDVKIMNRKWCADTTTTTILLVYCQHVIDHTKLKQAIAPEMCNDLLQSSFKDSNLLASNSQFSVTTLELENSNENVSRMLFEGKLLIIFQEYKRGYTIDIAKLPTRSIEQSNTEMTIRGSRDGFVEELSTNIGLIRKRLKTSSLSYDEFIIGERTQTKVGLLYLKDVASQETISQVQFKLKEINIDGVVSSAQIEEFITGDQFSLFPLIEYTGRPDYAVNCLLHGRFILLVDGSPTATIAPVSFPFFVNTAEDQNYFYLFGSFVRLLSLFGIAISIFLPGFWVALVTYHPDQIPYTLLATLSLSREGIPFPAPLEGMIMITLFELLRQAGLRIPAAFGQTLSVVGGLIIGQAAISSGFVSPSMVVMIAISVVSTFTLVNQSFTGTLSILRYGVFLMSSFLGIVGFICSILLIVIHVANLRSFGLPFLAPYSPPVFSSMLPSTFRIPFTRMKKRPKELHTYDNTRQRTNNDENK
|
May allow B.anthracis to germinate within phagocytic cells and therefore involved in virulence.
|
Q9ZFB5
|
GERXB_BACAN
|
Spore germination protein XB
|
MVNFFQIALVLIGSTGIINHVIIIPMLLDHSGRDSWISIIILSLVYIIWIPCVFIVHKYTREEHLFSWLMRNYGGFITYPLLSIIVLYLIILGTVTLKETLTFFSFYLPETPRILLGVLLSIICFYNIQRGVQSIALTTGILLPVVFLLGFFVMIANFPHKDYSLLKPIMEHGMDPVIKGMIYPAAGFVELIFILFLQHHIGSKIKLSQLIIVGIILAGITLGPTIAAIVEFGPFVAANQRYPTFEEWRLVSIGKYIEHLDFLSVYQWLVGVFIRISLVIFLIPDVLQVTKQKARNQIISILLICMVIICILPISDASFYWFLSHVFLPISAIGLFLFSMLLLVFVWVSKNKKRA
|
May allow B.anthracis to germinate within phagocytic cells and therefore involved in virulence.
|
Q9ZFC6
|
DNAK_METSS
|
Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70)
|
MAKIIGIDLGTTNSCVAVMEGGKPRVIENAEGTRTTPSIVAYQDDGEILAGAPAKRQAVTNPKNTLYAVKRLIGRRFEEKEVQKDIGLMPYTITKADNGDAWVEVRGQKMAPPPNSAEVLRKMKKTAEDYLGEEVTEAVITVPAYFNDSQRQATKDAGRIAGLEVKRIINEPTAAALAFGLDKQEGDRKIAVYDLGGGTFDISIIEIAEIDGEHQFEVLSTNGDTFLGGEDFDNRLIDFLADEFKKEKRLDLRNDLLAKQRLKEAAEKAKIELSSAQQTEVNLPYITADATGPKHLVVKITRTKFESLVEDLIERSIKPCEVALKDAGVKPSDIQDVILVGGQTRMPKVQEKVKEFFGKEPRKDVNPDEAVAVGAAIQGGVLQGDVKDVLLLDVTPLSLGIETLGGVMTKLIKKNTTIPTKASQVFSTAEDNQNAVTIQVLQGEREMAAGNKSLGQFNLSDIPPAPRGMPQIEVTFDIDANAILHVSAKDKATGKENKITIKANSGLSEEEIKRMEEDAAAYADEDRKLRELVDARNSADGMVHSVKKSLSEHGDKLEAGEKEKIEAAIKDVEDAIKGDDKEAIEAKTNALMEASQKLGEKVYAEQQAQQGGAEEAQPQGEKTVDADVVDAEFEEVKDDKK
|
Acts as a chaperone.
|
Q9ZFC7
|
GRPE_METSS
|
Protein GrpE (HSP-70 cofactor)
|
MQEENQHPEQDDISEAQDAGAAGSLDARIAELEAQLAEQQANVLYVKAEGENIRRRAAEDIDKARKFALEKFSSELLAVKDSLDAALVVENATVESYKSGVELTAKQLLSVFEKFHITEINPLGEKFDPNKHQAISMLESDQEPNSVISVLQNVRPE
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. {ECO:0000255|HAMAP-Rule:MF_01151}.
|
Q9ZFD9
|
CH10_BURVI
|
Co-chaperonin GroES (10 kDa chaperonin) (Chaperonin-10) (Cpn10)
|
MNLRPLHDRVIVKRLDQETKTASGIVIPDAAAEKPDQGEVLAIGPGKRDDKGALIALDVKVGDRVLFGKYAGQTVKVDGQELLVMREEDIMAVVNAK
|
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel. {ECO:0000255|HAMAP-Rule:MF_00580}.
|
Q9ZFE1
|
CH10_BURCE
|
Co-chaperonin GroES (10 kDa chaperonin) (Chaperonin-10) (Cpn10)
|
MNLRPLHDRVIVKRLDQETKTASGIVIPDAAAEKPDQGEVLAIGPGKRDDKGAPIALDVKVGDRVLFGKYAGQTVKVDGQELLVMREEDIMAVVNAK
|
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel. {ECO:0000255|HAMAP-Rule:MF_00580}.
|
Q9ZFF8
|
SECD_SALCH
|
Protein translocase subunit SecD
|
MLNRYPLWKYIMLVVVIIVGLLYALPNLYGEDPAVQITGVRGVAASEQTLIQVQKTLQEEKIPAKSVALEEGAILARFDTTDTQLRAREALMSVLGDKYVVALNLAPATPRWLAAIHADPMKLGLDLRGGVHFLMEVDMDTALGKLQEQNIDSLRSDLREKGIPYTTVRKENNYGLSITFRDSKARDEAIAYLTPRHRDLVISSQSGNQLRAVMTDARLSEAREYAVQQNINILRNRVNQLGVAEPVVQRQGADRIVVELPGIQDTARAKEILGATATLEFRLVNTNVDQAAAAAGRVPGDSEVKQTREGQPVVLYKRVILTGDHITDSTSSQDEYNQPQVNISLDSAGGNIMSNFTKDNIGKPMATLFVEYKDSGKKDANGRAVLVKQEEVINIANIQSRLGNSFRITGISNPNEARQLSLLLRAGALIAPIQIVEERTIGPTLGMQNIKQGLEACLAGLVVSILFMIFFYKKFGLIATSALVANLVLIVGIMSLLPGATLSMPGIAGIVLTLAVAVDANVLINERIKEELSNGRTVQQAINEGYAGAFSSIFDANITTLIKVIILYAVGTGAIKGFAITTGIGVATSMFTAIIGTRAIVNLLYGGKRVTKLSI
|
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. {ECO:0000255|HAMAP-Rule:MF_01463}.
|
Q9ZFL7
|
UXUA_GEOSE
|
Mannonate dehydratase (EC 4.2.1.8) (D-mannonate hydro-lyase)
|
MKMTFRWFGKEHDTVSLDHIRQIPGVEGIVGALYHIPVGEVWPLDDILELKRQVNEKGFHLEVIESVNVHEDIKLGLPSRDRYIENYKQTIRNLAKAGVKVICYNFMPIFDWTRSDLAKRRPDGSTVLAYEKQKIEQIDPEEMIRRIESGANGFLLPGWEPERLKTIKPLFSLYKGVTEEDLFDHLRYFLEQIVPVAEECGVRMALHPDDPPWSVFGLPRIATNKENLDRIVHMVNSPANGLTLCSGSLGANPANDVPDIFRHFLRMGRVPFAHVRNVEIHANGDFEETSHRSCDGSLNICEIMKALHEANFQGYIRPDHGRMIWGEQARPGYGLYDRALGIMYLLGIWDSLENEKKKQEGEKTCSRSIQV
|
Catalyzes the dehydration of D-mannonate.
|
Q9ZFR5
|
URED_YERPE
|
Putative urease accessory protein UreD
|
MTAQSQNIVETPSRVRAHALGVNAPELAKYQDEPAQMRSGAVGKSGYLKLRFAKREHCSILAEMERRVPSLVQKALYWDEEIPELPCVTMISTSGCILQGDRLATDVHVEAGACAHVTTQSATKVHMMNANYASQIQNFIVEEGGYLEFMPDPLIPHRNSRFITDTTISIHPTATAIYSEVLMSGRKYHHADERFGFDVYSSRVAAQNLAGKELFVEKYVLEPKVESLDAVGVMQTFDAFGNVILLTPKEHHDRILARVPAHFDIKGGDCQRRDAST
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. {ECO:0000255|HAMAP-Rule:MF_01384}.
|
Q9ZFR7
|
UREF_YERPE
|
Urease accessory protein UreF
|
MNASDLIRIMQFGDSVLPVGAFTFSNGVESAIQTGIVHDVATLKGFVLTALKQAASCDGMGVVVAHRAVVADDRDGIIRADWAVNNRKLNEESRLMATRMGKKLAEMSIHVVEHPLISWWLEQIKNGNTAGTYPVTQAVVMAAQGIGQREVVVMHQYGVAMTILSAAMRLMRVTHFDTQHILFELNHDIEKFCDIAEIGDINQMSSYVPIVDVLAAVHVKAHVRLFSN
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. {ECO:0000255|HAMAP-Rule:MF_01385}.
|
Q9ZFU3
|
PSAE_MASLA
|
Photosystem I reaction center subunit IV
|
MVQRGSKVRILRPESYWFQDIGTVASIEQGGTIRYPVIVRFDKVNYAGVNTNNFAEYELVEVEAPKAKPKK
|
Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
|
Q9ZG89
|
ENGB_CAUVC
|
GTP-binding protein EngB (GTP-binding protein CgpA)
|
MSEEQKLPKEPPILLPGAADFTEEQIEAARVFFAQPVSFIMGAVRMDAMPPSDLPEVAFAGRSNVGKSSLINGLVNQKYLARASNEPGRTREINFFLLAEKVRLVDLPGYGFARVSRSIADKFQDLGRAYLRGRANLKRVYVLIDARHGLKKVDLEALDALDVAAVSYQIVLTKADKIKPAEVDKVVAETQKAIAKRAAAFPRVLATSSEKGLGMPELRAEIVRLCIDE
|
Necessary for normal cell division and for the maintenance of normal septation. {ECO:0000255|HAMAP-Rule:MF_00321}.
|
Q9ZGW3
|
PARD_YERPE
|
Antitoxin ParD
|
MAHVTSVTLGEHLTGFVGEMIQSGRYGNISEVLRDALRLMEAREQRVQHVRDMVLAGTNVPVSHRLMDEIFSAAVKDTSV
|
Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the effect of toxin ParE (By similarity).
|
Q9ZH20
|
RLMH_DESTE
|
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)
|
MHITLLCVGKLKEDFLLLAQKEYLKRLSPYARIELVEVREESLPASGRAGALEAVLKKEGTRLLERIPDNCVTIALDRKGMMLSSKEFAGYLAELGLRGQNKLCFIIGGSAGLAGDVLARASLRLSFSKFTFPHQLMRIILLEQIYRAFKIIRGEKYHL
|
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00658}.
|
Q9ZH29
|
GTCA_LISMN
|
Cell wall teichoic acid glycosylation protein GtcA
|
MSKIRQLLNKIPWYTDQVHSIFMYLIMGGFTTIINIVTFWLCTYILNWDYRIANTIAFIASVLFAYFSNKKFVFDSYTPTWKDRLREASSFFGFRCLTYIIDILVMILLISYLSVDELWAKIWTNIIVLVLNYVFSKWIIFKVQK
|
Involved in the decoration of cell wall teichoic acid with galactose and glucose.
|
Q9ZH76
|
DNAA_STRRE
|
Chromosomal replication initiator protein DnaA
|
MADVPADLAAVWPRVLEQLLGEGRGQGVEAKDEHWIRRCQPLALVADTALLAVPNEFAKGVLEGRLAPIVSETLSRECGRPIRIAITVDDSAGEPPPAAPPAQQTPKPRYEEPELPSGPYEGYGRHRGGADQLPGTEPRPEQLPSARPDQLPTVRPAYPSEYHRPEPGAWPRPAQDEYGWQQPRLGFPERDPYASPSSQDAYGSPSQDYRPQGMDRPPYEQQRGDYDTPRAEYEPARPDYDSARPDYESARPEYDQRDPVRRELPEPPAHRGGPGADMPSAGAPGPPAAQPAPASGPGEPTARLNPKYLFDTFVIGASNRFAHAAAVAVAEAPAKAYNPLFIYGESGLGKTHLLHAIGHYARSLYPGTRVRYVSSEEFTNEFINSIRDGKGDSFRKRYREMDILLVDDIQFLADKESTQEEFFHTFNTLHNANKQIVLSSDRPPKQLVTLEDRLRNRFEWGLITDVQPPELETRIAILRKKAVQEQLNAPPEVLEFIASRISRNIRELEGALIRVTAFASLNRQPVDLGLTEIVLKDLIPGGEDSTPEITATAIMAATADYFGLTVDDLCGSSRGRQLVTARQIAMYLCRELTDLSLPKIGAQFGGRDHTTVMHADRKIRALMAERRSIYNQVTELTNRIKNG
|
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).
|
Q9ZHA2
|
SEPF_STAAU
|
Cell division protein SepF
|
MSHLALKDLFSGFFVIDDEEEVEVPDKQQQVNEAPAKEQSQQTTKQNAIKSVPQKSASRYTTTSEERNNRMSNYSKNNSRNVVTMNNATPNNASQESSKMCLFEPRVFSDTQDIADELKNRRATLVNLQRIDKVSAKRIIDFLSGTVYAIGGDIQRVGTDIFLCTPDNVEVAGSITDHIENMEHSFD
|
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA. {ECO:0000255|HAMAP-Rule:MF_01197}.
|
Q9ZHC9
|
SILA_SALTM
|
Putative cation efflux system protein SilA
|
MIEWIIRRSVANRFLVMMGALFLSIWGTWTIINTPVDALPDLSDVQVIIKTSYPGQAPQIVENQVTYPLTTTMLSVPGAKTVRGFSQFGDSYVYVIFEDGTDLYWARSRVLEYLNQVQGKLPAGVSSEIGPDATGVGWIFEYALVDRSGKHDLSELRSLQDWFLKFELKTIPNVAEVASVGGVVKQYQIQVNPVKLSQYGISLPEVKQALESSNQEAGGSSVEIAEAEYMVRASGYLQSIDDFNNIVLKTGENGVPVYLRDVARVQTGPEMRRGIAELNGQGEVAGGVVILRSGKNARDVITAVRDKLETLKASLPEGVEIVTTYDRSQLIDRAIDNLSSKLLEEFFVVAIVCALFLWHVRSALVAIISLPLGLCIAFIVMHFQGLNANIMSLGGIAIAVGAMVDAAIVMIENAHKRLEEWDHRHPGEQIDNVTRWKVITDASVEVGPALFISLLIITLSFIPIFTLEGQEGRLFGPLAFTKTYSMAGAAALAIIVIPILMGFWIRGKIPAETSNPLNRVLIKAYHPLLLRVLHWPKTTLLVAALSIFTVVWPLSQVGGEFLPKINEGDLLYMPSTLPGVSPAEAAALLQTTDKLIKSVPEVASVFGKTGKAETATDSAPLEMVETTIQLKPEDQWRPGMTIDKIIDELDRTVRLPGLANLWVPPIRNRIDMLSTGIKSPIGIKVSGTVLSDIDATAQSIEAVAKTVPGVVSVLAERLEGGRYIDIDINREKASRYGMTVGDVQLFVSSAIGGAMVGETVEGVARYPINIRYPQDYRNSPQALKQMPILTPMKQQITLGDVADINVVSGPTMLKTENARPASWIYVDARGRDMVSVVNDIKTAISEKVKLRPGTSVAFSGQFELLEHANKKLKLMVPMTVMIIFILLYLAFRRVDEALLILMSLPFALVGGIWFLYWQGFHMSVATGTGFIALAGVAAEFGVVMLMYLRHAIEAHPELSRKETFTPEGLDEALYHGAVLRVRPKAMTVAVIIAGLLPILWGTGAGSEVMSRIAAPMIGGMITAPLLSLFIIPAAYKLIWLRRHKKSVS
|
Component of the sil cation-efflux system that confers resistance to silver. May be part of a three-component cation/proton antiporter.
|
Q9ZHD0
|
SILB_SALTM
|
Putative membrane fusion protein SilB
|
MASLKIKYAAIIISSLIAGGLISVTAWQYLNSSQKTVPAEQKAPEKKVLFWYDPMKPDTKFDKPGKSPFMDMDLVPKYADESGDKSSGGIRIDPTQVQNLGLKTQKVTRGMLNYSQTIPANVSYNEYQFVIVQARSDGFVEKVYPLTIGDHVKKGTPLIDITIPEWVEAQSEFLLLSGTGGTPTQIKGVLERLRLAGMPEEDIQRLRSTRTIQTRFTIKAPIDGVITAFDLRTGMNISKDKVVAQIQGMDPVWISAAVPESIAYLLKDTSQFEISVPAYPDKTFHVEKWNILPSVDQTTRTLQVRLQVTNKDEFLKPGMNAYLKLNTQSQEMLLIPSQAVIDTGKEQRVITVDDEGKFVPKQIHVLHESQQQSGIGSGLNEGDTVVVSGLFLIDSEANITGALERMRHPEKTENSMPAMSEQPVNMHSGH
|
Component of the sil cation efflux system that confers resistance to silver. May be part of a three-component cation/proton antiporter.
|
Q9ZHD2
|
SILC_SALTM
|
Probable outer membrane lipoprotein SilC
|
MFKLKLLSISTIFILAGCVSLAPEYQRPPAPVPQQFSLSKNSLTPAVNSYQDTGWRNFFVDPQVSRLIGEALNNNRDLRMAALKVEEARAQFNVTDADRYPQLNASSGITYNGGLKGDKPTTQEYDAGLELSYELDFFGKLKNMSEADRQNYFASEEARRAVHILLVSNVSQSYFSQQLAYEQLRIARETLKNYEQSYAFVEQQLVTGSTNVLALEQARGQIESTRAEIAKREGDLAQANNALQLVLGTYRAVPSEKGIKGGEIAPVKLPPNLSSQILLQRPDIMEAEYQLKAADANIGAARAAFFPSITLTSGLSSSSTELSSLFTSGSGMWNFIPKIEIPIFNAGRNKANLKLAEIRQQQSVVNYEQKIQSAFKDVSDTLALRDSLSQQLESQQRYLDSLQITLQRARGLYASGAVSYIEVLDAERSLFATQQTILDLTYSRQVNEINLFTALGGGWVE
|
Component of the sil cation-efflux system that confers resistance to silver. May be part of a three-component cation/proton antiporter.
|
Q9ZHD3
|
SILR_SALTM
|
Probable transcriptional regulatory protein SilR
|
MKILIVEDDIKTGEYLSKGLTEAGFVVDHADNGLTGYHLAMTAEYDLVILDIMLPDVNGWDIIRMLRSAGKGMPVLLLTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGNTMITESQLKVADLSVDLVSRKVSRAGNRIVLTSKEFSLLEFFIRHQGEVLPRSLIAFFMVWVHEFLTADTNAIDVAVKRLRAKIDNDYGTKLNQTVRGVGYMLEIPDA
|
Component of the sil cation-efflux system that confers resistance to silver. Probable member of a two-component regulatory system SilS/SilR.
|
Q9ZHF3
|
PILQ_NEIMH
|
Type IV pilus biogenesis and competence protein PilQ
|
MNTKLTKIISGLFVATAAFQTASAGNITDIKVSSLPNKQKIVKVSFDKEIVNPTGFVTSSPARIALDFEQTGISMDQQVLEYADPLLSKISAAQNSSRARLVLNLNKPGQYNTEVRGNKVWIFINESDDTVSAPARPAVKAAPAAPAKQQAAAPSTKSAVSVSEPFTPAKQQAAAPFTESVVSVSAPFSPAKQQAAASAKQQAAAPAKQQAAAPAKQQAAAPAKQQAAAPAKQTNIDFRKDGKNAGIIELAALGFAGQPDISQQHDHIIVTLKNHTLPTTLQRSLDVADFKTPVQKVTLKRLNNDTQLIITTAGNWELVNKSAAPGYFTFQVLPKKQNLESGGVNNAPKTFTGRKISLDFQDVEIRTILQILAKESGMNIVASDSVNGKMTLSLKDVPWDQALDLVMQARNLDMRQQGNIVNIAPRDELLAKDKALLQAEKDIADLGALYSQNFQLKYKNVEEFRSILRLDNADTTGNRNTLISGRGSVLIDPATNTLIVTDTRSVIEKFRKLIDELDVPAQQVMIEARIVEAADGFSRDLGVKFGATGKKKLKNDTSAFGWGVNSGFGGDDKWGAETKINLPITAAANSISLVRAISSGALNLELSASESLSKTKTLANPRVLTQNRKEAKIESGYEIPFTVTSIANGGSSTNTELKKAVLGLTVTPNITPDGQIIMTVKINKDSPAQCASGNQTILCISTKNLNTQAMVENGGTLIVGGIYEEDNGNTLTKVPLLGDIPVIGNLFKTRGKKTDRRELLIFITPRIMGTAGNSLRY
|
Required for type IV pilus biogenesis and competence. Could function as a pore for exit of the pilus but also as a channel for entry of heme and antimicrobial agents and uptake of transforming DNA (By similarity).
|
Q9ZHG0
|
MCEB_KLEPN
|
Microcin E492 immunity protein
|
MTLLSFGFSPVFFSVMAFCIISRSKFYPQRTRNKVIVLILLTFFICFLYPLTKVYLVGSYGIFDKFYLFCFISTLIAIAINVVILTINGAKNERN
|
Protect the producing cell against microcin E492.
|
Q9ZHG4
|
DPO3A_THEMA
|
DNA polymerase III subunit alpha (EC 2.7.7.7)
|
MIPWVISPYSFDGSVVRFEKLALLLKRKGLKSVILADRNFHAAVKFNTIMRKHGLIPVHGLWKDGRIFVARNREEFDSLVRYYNGETHEIEDIPVFQESELTPVRYLDASEKKASIFMRKIFGLDEDVQGFPEKCEDVADILNAEAYDLRVNHRFPTPPKNWNELLIKKAEPLGEEYISRLKRELEVIKRKGFTPYIYTVEKVVEIAKKMGIKVGPGRGSAVGSLVAYLCGITEVDPIKYDLLFERFLNEERQEPPDIDVDVEDRRRKDLIKELSKSFQVYQVSTFGNLTEKSLKNLINSVLPDASLEEKNEIYKTVYGLPHHPSVHAAGVVISENPLPLPTRTEEDIPITDYDMYDLQEIGVVKIDILGLKTLSFIKDFKKEIFDYSDEKTYHLISKGKTLGVFQLEGLQARKLCRRISPRNMDELSILLALNRPGPLRSGLDVMFSNSKNVPAFFRKMFPETRGVLIYQEQIMRLAMFAGLSGTEADILRRAIAKKEREKMEPLLEKMKKGLLEKGMENAEQILEILLNFSSYAFNKSHSVAYAHITYQTAYLKAHHLEEFFKLYFAYNSSDAGKIFLAVQELRNEGYRVHPPDINISGKDLVFHGKDVYLPLTVVKGVGVTLVEQIEKIRPVSSVRELQERVTGVPRNVVESLITAGAFDKLYENRKLALEELNKRVEKDILEIRSLFGEKVEQESSNIKIGDITELEEKSMGFPLTPVHEVPTGLFARIDDVFTYGRILPVLVKRVSRNIVTDGLSVCRVRTDVPDGVHLVLLSPLQKIIKIWPFNENTRFVYRVDFTATLEKAGQNEITEVLKNGAVVRYEGYRPLTDEYRYRVVPR
|
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).
|
Q9ZHR1
|
HYBF_MORMO
|
Hydrogenase maturation factor HybF
|
MHELSLCMSAADIIREQAEQHGIARVTDVWLEVGALADVEESALHFCFDIACRDTVAQGCTLHIDVIPAQAWCWDCSREAEIMQHAGCCPHCGSERLRISEGDDLRVKSLEGE
|
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. {ECO:0000255|HAMAP-Rule:MF_02099}.
|
Q9ZHV9
|
EXBD2_VIBCH
|
Biopolymer transport protein exbD2
|
MRLGRRTSKQEEAQIDLTSMLDIVFIMLIFFIVTSSFVRESGVEVNRPTAAHAVSQKQAGIFVAITAANDIYIDKRQVDVERVQATLEHLLLDQPDASLVIQADEHAFNGTVVKVMDAAKGAGVKSIALAAEKP
|
Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.
|
Q9ZHY2
|
RECO_NEIG1
|
DNA repair protein RecO (Recombination protein O)
|
MSEYRVNHEPVFMLASSPWRESSLRVEAFSRRYGRVALLARSARKRQSELRGVLVPFVPASVSWYGSQELKTLHRAEWMGGWRQPQGRALFSGLYVNELVLKLTAREDPMSELYDALAKVMEAVCREANHIADLRRFEWKLLNALGVAPDLHADGTGGDILADKTYRLMPEEAVMPVCRDTGALSHEAGAIVEGQSLIDLREGSFRTAESLQQALKITRLLIGTLLPEGLKSRQVLEQIRQFDRNTA
|
Involved in DNA repair and RecF pathway recombination. Involved in pilin antigenic variation.
|
Q9ZI33
|
RBS_BRADU
|
Ribulose bisphosphate carboxylase small subunit (RuBisCO small subunit)
|
MKLTQGCFSFLPDLTDDQIYKQVQYCLAKGWAVNIEFTDDPHPRNTYWEMWGLPMFDLQDAAGVMMELAECRRVYGDRYIRISGFDSSPGWESVRISFLVNRPPQEAEFELVRQEVGGRAIRYTTVRKAPAHVS
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity. {ECO:0000255|HAMAP-Rule:MF_00859, ECO:0000269|PubMed:9882445}.
|
Q9ZI37
|
RL18_AQUPY
|
Large ribosomal subunit protein uL18 (50S ribosomal protein L18)
|
MPRLKTRREKRLRRHKRIRKKVFGTPERPRLCVYRSLNHFYAQIIDDTIGHTLVSASTLDPEFEKITGKRGGKSIKDAEVVAEIIARRALEKGIKKVVFDRGGFKYHGKIKAFADKCREMGLEF
|
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}.
|
Q9ZI38
|
RL6_AQUPY
|
Large ribosomal subunit protein uL6 (50S ribosomal protein L6)
|
MSRLVKKPIPYPENVKVSYDEKEHKVTVEGPKGKLELNIHPDIKVTLNQQERWIKLDRPSDRSFHKAIHGTMAALIKNMIKGVTEGFTEILEIHGLGYRAQLKGNVLELHLGKSHPDIYPIPPDVKIEVKGNEIHIHGIDKQRVGQVAAEIRSFRKPDPYKGKGIRYKGEQLSSNPERLQVRSKEVR
|
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}.
|
Q9ZI39
|
RS8_AQUPY
|
Small ribosomal subunit protein uS8 (30S ribosomal protein S8)
|
MSAVDPIADMFSAIKNAIMRRDAFLYVPSSKMKERILEVLKREGFIQDWEALKGEKYEEEFKKMKELAEKSPNPKMRRYLQQLIDYNKGTQYPLKIYLKYLDPKKRRSALTNIVRVSKGGRRVYAGVRTMPYVKRGLGIAIVSTDAGVMTDHEARKLRKGGEVIAFVW
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01302}.
|
Q9ZI40
|
RL5_AQUPY
|
Large ribosomal subunit protein uL5 (50S ribosomal protein L5)
|
MSATETKYVPRLYKKYKEEVVPKLIQKFQYKNPMQVPRLVKIVVNMGVGEAVQDIKQLERAVEDLRAITGQQPMITRARKSKAGFKLRKGMPIGCKVTLRNHTMWDFLDKVISVALPRVKDFKGLNPRSFDGRGNYAFGIAEQIVFPEIDYDKVDRIRGMDIIINTTAVSDQESLLATLTLGLPIRAM
|
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}.
|
Q9ZI41
|
RL24_AQUPY
|
Large ribosomal subunit protein uL24 (50S ribosomal protein L24)
|
MAAKIKKGDTVVVVRGKEKGKQGKVLKVYKRVKRRNKKGEPVSLAPFVIVEGVRLIKKHVKPIEGVREGGIIETEGPIDISNVMLLCPNCNKPTRVGFRIVEEGNVRRKYRYCKKCNENIDLVSEKVIKGG
|
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}.
|
Q9ZI42
|
RL14_AQUPY
|
Large ribosomal subunit protein uL14 (50S ribosomal protein L14)
|
MIQRQTYLNVADNSGAKKVQVIGIPYAPRKYATLRDVVTVTVKEALPQGNAKKGKIYRAIIVRTAKEVRRPDGSYIKFDDNACVLLNQYGEPLGTRVLGPIAREVRNKGFTKIASLAPEVV
|
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}.
|
Q9ZI43
|
RL16_AQUPY
|
Large ribosomal subunit protein uL16 (50S ribosomal protein L16)
|
MEKAEKGNPKGKAFRGNKLAFGEYGIQALDRAWITQQQIEAVRVALVRS
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q9ZI44
|
RS3_AQUPY
|
Small ribosomal subunit protein uS3 (30S ribosomal protein S3)
|
MGQKTHPIGFRLGVIKDWPSKWYPPKKDYAKLLHEDLKIKNYIKKRYKVAGVSKVEIERIVDKVRIKIHTAKPAIVIGRRGQEVDRLKKTIERMLPGKEISISVLEVKVPELDAQLVAEDIALQIERRVSHRRAMKRAIDNALKAGQKGVKVQVKGRIGGAARARKEWFLVGRMPLQTLRADIDYGFATAYTKYGILSVKVWIYKGDVLKGGKEEILKKIEEEIKQAAKEG
|
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}.
|
Q9ZI45
|
RL22_AQUPY
|
Large ribosomal subunit protein uL22 (50S ribosomal protein L22)
|
MGQLKIKDKSQREGYKPNQAIAILRYAHISPLKARLVLREIHGKDVGEALYLLKVIPKRAARIAEKLLKSAIANAEQKGLDLDRLYIKKAVADRGPILKKWIPRAHGRATMVRKRLSHITIVLEEKPEGKEEE
|
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}.
|
Q9ZI46
|
RS19_AQUPY
|
Small ribosomal subunit protein uS19 (30S ribosomal protein S19)
|
MGFKGAWNKRNRLIENPEEYYRLYKKLQRAYKLVREAIKRYGSFELLKGKTSLRDLEELLEERKQVLENLKKQLREAHKGKPKIEAEGDEQLKELIREVNRVQSEVRALEIITNRVRKYEEIYAQYKQMTEKKAYVDPKLWMRIRKMNEAGERKVVRTYSRATTIIPEFVGHTIAVHNGKTFIPVYITQDMVGHKLGEFAPTRTFKGHPDKTAKVVKKK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_00531}.
|
Q9ZI47
|
RL2_AQUPY
|
Large ribosomal subunit protein uL2 (50S ribosomal protein L2)
|
MGVRKLKPVTNGTRHAVLYDFEEIEKLVRKGKELVLVKKNKVEPEKSLLKWWHRAKGRSRQRGNITARHRGGGHKKLYRIIDFERDKSLVPAKVVSIEYDPFRSARICLLHYADGEKRYIIWPEGLKVGDTVMSISWEDAEAGKPLPEIKPGNAMPLKYIPEGTIIHNIEFMPGKGGQIARAAGTWAQVLGRSTKKGYVLVRMPSGEVRMIHERCMATIGRVGLAEHELVNVGKAGRARWLGWRPHTRGTAMNPVDHPHGGGEGRTRGKHPESPWDGRRRDTRREGVRSTPISLS
|
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}.
|
Q9ZI48
|
RL23_AQUPY
|
Large ribosomal subunit protein uL23 (50S ribosomal protein L23)
|
MSQRKPWEILIRPIITEKSNRLMEDYNKYTFEVALDASKPEIKEAVEKLFNVKVKKVNTMIVKPKKKRVWERFRQYGTTKKWKKAIVTLEKGINRHPWVCSEVRCRDGC
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}.
|
Q9ZI49
|
RL4_AQUPY
|
Large ribosomal subunit protein uL4 (50S ribosomal protein L4)
|
MKIGDVEVRDDVFNVKVKKHVLWEVVKWQLAKRRQGTHSTKTRGEVAYSGRKILPQKGTGNARHGERGVNIFVGGGVAHGPKPRDYEYPLPKKVRKLGLKMALSDKAQNDAIMFVDNIDLGEQPKTKKAVEFLKNLGVDKETLLIVIPEKNEVLYKSFRNLQNVRVLLPEGLNVYDVLWANKLVIHKECLDRIYKKVEA
|
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}.
|
Q9ZI50
|
RL3_AQUPY
|
Large ribosomal subunit protein uL3 (50S ribosomal protein L3)
|
MPLGLIGEKVGMTRVLLKDGTAIPVTVIKFPVNYVVQVKSVNTKDGYNALQVGAYEAKEKHLTKPLIGHFKKHGVPLLRRLWEFRVDNPEEFKSGQELRVQDVFKPGDLVDVWGISKGRGFAGVMKRWDFAGFPRSHGHRYHRAVGAIGQRTDPGRVWKGKKMPGHYGAKPVRVQGLFVVASLPEENAILVKGSALPGHNKGIVVLLPAVERIAYRKSQKLKQKRLQFIVENLVKEESTEVAES
|
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. {ECO:0000255|HAMAP-Rule:MF_01325}.
|
Q9ZI51
|
RS10_AQUPY
|
Small ribosomal subunit protein uS10 (30S ribosomal protein S10)
|
MEQEKIRIKLKAFDHRVLDQSVKQIIETVKRTGGVVRGPIPLPTRKRKWCVLRSPHKFDQSREHFEIRAFSRIIDITRFTPQTIEALMEINLPAGVDVEVKMRG
|
Involved in the binding of tRNA to the ribosomes. {ECO:0000255|HAMAP-Rule:MF_00508}.
|
Q9ZIN3
|
MOAB_STACT
|
Molybdenum cofactor biosynthesis protein B
|
MTKNEHVNVKLDRDIQCAVLTVSDTRTPETDKGGNLAKELLSEINVEIKPEHYAIVKDDKQAITEQLQQWLAEDVDVIITTGGTGIAQRDVTIEAVTPLLSKEIEGFGELFRYLSYAEDVGTRALLSRAVAGTVGEQLIFSVPGSTGAVKLAMNKLIKPELNHLIHELTK
|
May be involved in the biosynthesis of molybdopterin.
|
Q9ZIS7
|
RFAY_ECOLX
|
Lipopolysaccharide core heptose(II) kinase RfaY (EC 2.7.1.-)
|
MITSIRYRGFSFYYKDNDNKYKEIFDEILAYNFKTVKVLRNIDDTKVSLIDTKYGRYVFKVFAPKTKRNERFLKSFVKGDYYQNLIVETDRVRSAGLTFPNDFYFLAERKIFNYASVFIMLIEYVEGVELNDMPIIPENVKAEIKASMEKLHALNMLSGDPHRGNFIVSKDGVRIIDLSGKSCTAERKARDRLAMERHLGIANEIKDYGYYSVIYRTKLRKFIKKLKGKA
|
Catalyzes the phosphorylation of heptose(II) of the outer membrane lipopolysaccharide core.
|
Q9ZIV1
|
DNAK_MEGEL
|
Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70)
|
MSKVIGIDLGTTNSVVAVMEGGEPTVITNTEGSRLTPSVVGFSKTGERLVGQLAKRQAVSNPENTISSIKRHMGESYTVDIQGKKYTPQEISAMILQKLKEDAESYLGEKVTQAVITVPAYFNDGQRQATKDAGKIAGLDVLRIVNEPTAAALAYGLDKGGDGKILVFDLGGGTFDVSILELGDGVFEVKATNGNTHLGGDDFDNKVMEWMISEFKKETGIDLSQDKMAEQRLKEAAEKAKIELSTVLSTNINLPFITADATGPKHLDLTLTRAKFNELTEDLVQATMEPTKKAIADSGFTIDEIDKIILVGGSSRIPAVQEAIKSILGKEPSKGVNPDECVAIGAAIQAGVLVGDVKDVLLLDVTPLSLGIETLGGVFTKIIDRNTTIPTSRSQVFSTAVDNQPSVDVHVLQGRREMAADNKTLGRFELTGIPAAPRGVPRIEVTFNID
|
Acts as a chaperone.
|
Q9ZIX6
|
MUTS_THECA
|
DNA mismatch repair protein MutS
|
MPAVKMGVMLKGEGPGPLPPLLQQYVELRDRYPDYLLLFQVGDFYECFGEDAERLARALGLVLTHKTSKDFTTPMAGIPIRAFDAYAERLLRMGFGLAVADQVEPAEEAEGLVRREVTQLLTPGTLTQEALLPREANYLAAIATGDGWGLAFLDVSTGEFKATLLKSKSALYDELFRHRPAEVLLAPELRENEAFVAQFRKRFPVMLSEAPFDPEGEAPLALSRARGALLAYARATQGGALSVRPFRLYDPGAIVRLPEASLKALEVFEPLRGQDTLFGVLDETRTAPGRRLLQAWLRHPLLERGPLEARLDRVERFVREGALREGVRRLLFRLADLERLATRLELSRASPRDLAALRRRSLEILPELEGLLGEEVGLPDLSGLLEELRAALVEDPPLKVSEGGVIREGYDPDLDALRRAHADPVAYFLDLEVREKESTGIPTLKVGYNAVFGYYLEVTRPYYEKVPQEYRPVQTLKDRQRYTLPEMKERERELYRLEALIKRREEEVFIALRERARKEGEALREAARILAELDVYAALAEVAVRHGYTRPRFGERLRIRAGRHPVVRRRTAFVPNDLEMAHELVRVTGPNMAGKSTFLRQTALIALLAQIGSFVPAEEAELPLFDGIYTRIGASDDLAGGKSTFMVEMEEVALVLKEATERSLVLLDEVGRGTSSLDGVAIATALAEALHERRCYTLFATHYFELTALALPRLKNLHVAAKEEEGGLVFYHQVLPGPASKSYGVEVAEMAGLPKEVVERARALLSAMAARREGALEEVLERLLALDPDRLTPLEALRFLHELKALALGLPLGSMKG
|
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity (By similarity).
|
Q9ZIX8
|
OTCC_AVIPA
|
Ornithine carbamoyltransferase, catabolic (OTCase) (EC 2.1.3.3)
|
MLFNLKNRHLLSLVHHTPQEIQFLLQLAKELKQAKYTGTEQPRLKGKNIALIFEKTSTRTRCSFEVAAYDQGANVTYIDPNSSQIGHKESMKDTARVLGRMYDAIEYRGFKQAVVNELAEYAGVPVFNGLTDEFHPTQMLADVLTMMEHSDKPLSDIIYVYIGDARNNMGNSLLLIGAKLGMDVRICAPKALQPEAELVAMCQEFAQQTGARITITEDVELAVKGVDFVHTDVWVSMGEPLESWGERINLLLPYQVTPALMQRSGNPKVKFMHCLPAFHNCETEVGKKIAEKYPHLANGIEVTEEVFESPMNIAFDQAENRMHTIKAVMVASLA
|
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
|
Q9ZJ00
|
ATPE_STRSA
|
ATP synthase epsilon chain (ATP synthase F1 sector epsilon subunit) (F-ATPase epsilon subunit)
|
MAQMTVQIVTPDGLIYDHHAAFVSVKTIDGELGILPRHINTIAVLEVDQVKVRRVDDDKHIDWIAVNGGIIEIADNVITIVADSAERARDIDISRAERAKRRAELEIEEAHDKHLIDQERRAKIALQRAINRINVGTRI
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. {ECO:0000255|HAMAP-Rule:MF_00530}.
|
Q9ZJ02
|
ATPG_STRSA
|
ATP synthase gamma chain (ATP synthase F1 sector gamma subunit) (F-ATPase gamma subunit)
|
MAVSLNDIKNKIASTKNTSQITNAMQMVSAAKLGKSEEAAKNFQVYAQKVRKLVTDMLHGHEAENARHHSMLISRPVKKSAYIVITSDRGLVGGYNATILKALMELKAEYHPTGEDFEVICIGSVGADFFRARGIQPVYELRGLADQPSFDEVRKIISKTIEMYQNELFDELYVCYNHHVNSLTSQMRVEQMLPIIDLDPNEADEDYTLNLELESSRDSILDQLLPQFAESMIYGAIIDAKTAENAAGMTAMQTATDNAKKVISDLTIQYNRARQAAITQEITEIVAGASALE
|
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}.
|
Q9ZJ38
|
RLPA_HELPJ
|
Endolytic peptidoglycan transglycosylase RlpA (EC 4.2.2.-)
|
MGWALKKVCFLGVIFLISACTVKKNGVKNLSYKHESLRAYENAKDYDPTTKKATYKRNFFERHFKHHTDSQGNNTKQPLDNGMRDSNAIQRATMHPYQVGGKWYYPTKVDLGEKFDGIASWYGPNFHAKKTSNGEIYNMYAHTAAHKTLPMNTVVKVINVDNNSSTIVRINDRGPFVSNRIIDLSNAAARDIDMVQKGTASVRLIVLGFGGVISKQYEQSFNANYSKILHKEFKVGESEKSVSGGKFSLQMGAFRNQIGAQTLADKLQAENKNYSVKVAFKDDLYKVLVQGFQSEEEARDFMKKYNQNAVLTRE
|
Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. {ECO:0000255|HAMAP-Rule:MF_02071}.
|
Q9ZJ42
|
ENGB_HELPJ
|
Probable GTP-binding protein EngB
|
MIVIKDAHFLTSSNNLSQCPASLTSEMVILGRSNVGKSTFINTLLGKNLAKSSATPGKTRLANFFSTTWEDKENALTTTFNVIDLPGFGYAKVSKSLKKEWEGFLWELLSVRVSIKLFIHLIDARHLDLEIDKNAKENIQALLRPDQAYLSLFTKFDKLNKNEQHRLFLNAPKPFLINTIHFNALSSKYPTLEIVRQTLLKYLLTNPL
|
Necessary for normal cell division and for the maintenance of normal septation. {ECO:0000255|HAMAP-Rule:MF_00321}.
|
Q9ZJ65
|
SECF_HELPJ
|
Protein translocase subunit SecF
|
MELFKQVRILSFMRYSNYGVIVSAILVLLALGLLFFKGFSLGIDFAGGSLVQVRYTQNAPIKEVRDLFEKEARFKGVQVSEFGSKEEILIKFPFVETAENEDLNAIVANILKPSGDFEIRKFDTVGPRVGSELKEKGILSLILALIAIMVYVSFRYEWRFALASVVALVHDVILVASSVIVFKIDMNLEVIAALLTLIGYSINDTIIIFDRIREEMLSQKTKNATQAIDEAISSTLTRTLLTSLTVFFVVLILCVFGSKIIIGFSLPMLIGTIVGTYSSIFIAPKVALLLGFDMGKYYENEARKIKKAQEKEKMRRLYEGGQV
|
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. {ECO:0000255|HAMAP-Rule:MF_01464}.
|
Q9ZJ66
|
SECD_HELPJ
|
Protein translocase subunit SecD
|
MKLFNPRLIVFIFALLLGVGFSVPSLLETKGPKITLGLDLRGGLNMLLGVQTDEALKNKYLSLASALEYNAKKQNILLKDIKSSLEGISFELLDEDEAKKLDALLLELQGHSQFEIKKEAEFYSVKLTPLEQEELRKNTILQVIGIIRNRLDQFGLAEPVVIQQGREEISVQLPGIKTLEEERRAKDLISKSAHLQMMAVDEEHNKDAMNMTDLEAQKLGSVLLSDAEMGGKILLKAIPILDGEMLTDAKVVYDQNNQPVVSFTLDAQGAKIFGDFSGANVGKRMAIVLDNKVYSAPVIRERIGGGSGQISGNFSVAQASDLAIALRSGAMNAPIQVLEKRIVGPSLGKDSIKTSIIALVGGFILVMGFMALYYSMAGVIACMALVVNLFLIVAVMAIFGATLTLPGMAGIVLTVGIAVDANIIINERIREVLREGEGVVKAIHLGYINASRAIFDSNITSLIASVLLYAYGTGAIKGFALTTGIGILASIITAIIGTQGIYQALLPKLAQTKSLYFWFGVKNKRA
|
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. {ECO:0000255|HAMAP-Rule:MF_01463}.
|
Q9ZJ67
|
YAJC_HELPJ
|
Sec translocon accessory complex subunit YajC
|
MGQTKEIITTLLPLLVLFLIFYFLIVRPQRQQQKKHKEMIEGLTKGDKIVTQGGLIVEVLKAEANFFSVKLNDDTTAKLSKNYVAFKLDEETTPNNN
|
The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions.
|
Q9ZJ68
|
NHAA_HELPJ
|
Na(+)/H(+) antiporter NhaA (Sodium/proton antiporter NhaA)
|
MNLKKTENALSLTLKNFIKSESFGGIFLFLNAVLAMVVANSFLKESYFALWHTPFGFQVGDFFIGFSLHNWIDDVLMALFFLMIGLEIKRELLFGELSSFKKASFPVIAAIGGMIAPGLIYFFLNANTPSQHGFGIPMATDIAFALGVIMLLGKRVPTALKVFLITLAVADDLGAIVVIALFYTTNLKFAWLLGALGVVLVLAILNRLNIRSLIPYLLLGVLLWFCVHQSGIHATIAAVVLAFMIPVKIPKDSKNVELLELGKRYAETSSGVLLTKEQQEILHSIEEKASALQSPLERLEHFLAPISGYFIMPLFAFANAGVSVDSSINLEVDKVLLGVILGLCLGKPLGIFLITFISEKLKITARPKGIGWWHILGAGLLAGIGFTMSMFISNLAFTSEHKDAMEVAKIAILLGSLISGIIGALYLFALDKRAALKK
|
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. {ECO:0000255|HAMAP-Rule:MF_01844}.
|
Q9ZJ71
|
EFTS_HELPJ
|
Elongation factor Ts (EF-Ts)
|
MSGISAQLVKKLRDLTDAGMMDCKKALVEVAGDLQKAIDFLREKGLSKAAKKADRIAAEGVVALEVAPDFKSAMMVEINSETDFVAKNEGFKELVKKTLETIKTHNIHTTEELLKSPLDNKPFEEYLHSQIAVIGENILVRKIAHLKAPSSHIINGYAHSNARVGVLIAIEYNNEKNAPKVVELARNIAMHAAAMKPQVLDCKDFSLDFVKKETLALIAEIEKDNEEAKRLGKPLKNIPTFGSRIELSDEVLAHQKKAFEDELKEQGKPEKIWDKIVPGKMERFIADNTLIDQRLTLLGQFYVMDDKKTIAQVIADCSKEWDDNLKITEYVRFELGEGIEKKTENFAEEVALQMK
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Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).
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Q9ZJ80
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RECN_HELPJ
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DNA repair protein RecN (Recombination protein N)
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MRDFNNIQITRLKVRQNAVFEKLDLEFKDGLSAISGASGVGKSVLIASLLGAFGLKESNASNIEVELIAPFLDTEEYGIFREDEHEPLVISVIKKEKTRYFLNQTSLSKNTLKALLKGLIKRLSNDRFSQNELNDILMLSLLDGYIQNKNKAFSPLLDALETKFTRLEKLERERRSLEDKKRFQKDLEERLNFEKMKLERLDLKEDEYERLLEQKKLLSSKEKLNDKIALALDVLENTHKITHALESVGHSAEFLKSALLEAGALLEKEQAKLEECERLDIEKVLEKLGMLSGIIKDYGSIAHAKERLGHVKNELHNLKEIDHHCETYHKEIERLKTECLKLCEEISGFRKEYLAGFNALLSAKAKDLLLKSPSLVLEEAPMSEKGAQKLVLHLQNSQLETLSSGEYSRLRLAFMLLEMEFLKDFKGVLVLDEMDSNLSGEESLAVSKALETLSSHSQIFAISHQVHIPAVAKNHILVFKENHKSLAKTLNNEERVLEIARMIGGSENIESAISFAKEKLKV
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May be involved in recombinational repair of damaged DNA.
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Q9ZJ96
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DNAA_HELPJ
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Chromosomal replication initiator protein DnaA
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MDTNNNIEKEILALVKQNPKVSLIEYENYLSQLKYNPNASKSDIAFFYAPNKFLCTTITAKYGALLKEILSQNKVGMHLAHSVDVRIEVAPKIQVNAQSNINYKATKTSVKDSYTFENFVVGSCNNTVYEIAKKVAQSDTPPYNPVLFYGGTGLGKTHILNAIGNHALEKHKKVVLVTSEDFLTDFLKHLDNKNMDSFKKKYRHCDFFLLDDAQFLQGKPKLEEEFFHTFNELHANSKQIVLISDRSPKNIAGLEDRLKSRFEWGITAKVMPPDLETKLSIVKQKCQLNKITLPEEVMEYIAQHISDNIRQMEGAIIKISVNANLMNATIDLNLAKTVLEDLQKDHAEGSSLENILLAVAQSLNLKSSEIKVSSRQKNVALARKLVVYFARLYTPNPTLSLAQFLDLKDHSSISKMYSSVKKMLEEEKSPFILSLREEIKNRLNELNDKKTAFNSSE
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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).
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Q9ZJA6
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NUSA_HELPJ
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Transcription termination/antitermination protein NusA
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MEKISDLIECIAYEKNLPKEMISKVIQGCLLKMAQNELDPLARYLVVEENKQLQLIQLVEVLEDDDERLVNDPSKYISLSKAKEMDPSVKIKDELSYSLSLESMKQGAINRLFKDLQYQLEKALEDSHFEAFQKRLNSVLMGQVILVDHNQNTFIEIEQQFQGVLSMRHRIKGESFKIGDSIKAVLTQVKRTKKGLLLELSRTTPKMLEALLELEVPEIKDKEIEIIHCARIPGNRAKVSFFSHNSRIDPIGAAVGVKGVRINAISNELNKENIDCIEYSNVPEIYITLALAPAKILSVEIKKIPIEELSAEEKESIQERFIVNNHLQKAKVRLLDIEKSKAIGKGGVNVCLASMLTGYHIEFETIPSVKENAENENEKETPKVGVEALESLFKN
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Participates in both transcription termination and antitermination. {ECO:0000255|HAMAP-Rule:MF_00945}.
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Q9ZJA7
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SELA_HELPJ
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L-seryl-tRNA(Sec) selenium transferase (EC 2.9.1.1) (Selenocysteine synthase) (Sec synthase) (Selenocysteinyl-tRNA(Sec) synthase)
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MANITTKETPPTTPDLLKSPYQKIINASVSVFDETHGRSFFSPQFYEKIEPYLKEVLTHPIGLECDLNTAKKTNRLTPLKQLFKVCFDTEEVLIVNNNTSTVFLIANALAQQKEIIVSYGELVGGDFNLKDILLSSGARLHLVGNTNRAYLRDYRLALNENSKMLFKTHNPTFKKDTSFKDLQALAKEHGLIDYYNLGDVDLLNRTALEEILALKPSLVSFSADKSFNSAQAGIIMGQKEWVETLKNHPLYRALRVGKITLTLLFHSLNAWVNHQEEITIHALLHQTKDALLQKALKLYALLKPLELNVSIASSFSKIGNLPDKELESFCVKVQPKNTRALNCEKLYLKLFQKGVITRISCAFVCFEVFSLNGEDLEKIALVLKEILNKA
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Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00423}.
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Q9ZJC3
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PTH_HELPJ
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Peptidyl-tRNA hydrolase (PTH) (EC 3.1.1.29)
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MTLLVGLGNPTLRYDHTRHNAGFDILDSLVSELDLSFIFSPKHNAYLCVYKDFILLKPQTYMNLSGESVLSAKNFYKTKELLIVHDDLDLPLGVVKFKKGGGNGGHNGLKSIDALCSNSYYRLRVGISKGINITEHVLSKFHNNEEPLKNAAFEHAKNALKFFIESHDFNATQNRFTLKKPLQIES
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The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. {ECO:0000255|HAMAP-Rule:MF_00083}.
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Q9ZJC4
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RL25_HELPJ
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Large ribosomal subunit protein bL25 (50S ribosomal protein L25) (General stress protein CTC)
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MLEGVIRESITKANAKALKKDGYLIANIYGKGVENVNCAFKLNPFIKYLKEKKHLIFPVKLGDKTFEVVVQEYQKNPVTNELIHVDLLAVTKGVKSKFKVPVKHQGTPVGLKNKGILMLSKKRISVECAPEHLPDHYLVDVAPLDVNESILVRDLEKHENVKILDHDSIAVIGVIKAK
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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}.
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Q9ZJC5
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TAL_HELPJ
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Transaldolase (EC 2.2.1.2)
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MQEFSLWCDFIERDFLENDFLKLINKGAICGATSNPSLFCEAITKSAFYQDEIAKLKGKKAKEIYETLALKDILQASSALMPLYEKDPNNGYISLEIDPFLEDDAIKSIDEAKRLFKTLNRPNVMIKVPASESAFEVISALAQASIPINVTLVFSPKIAGEIAQILAKEARKRAVISVFVSRFDKEIDPLVPQNLQAQSGIMNATECYYQINQHANKLISTLFASTGVKSNSLAKDYYIKALCFKNSINTAPLDALNAYLLDPNTECQTPLKITEIEAFKKELKTHNIDLENTAQKLLKEGLIAFKQSFEKLLSSF
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Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
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Q9ZJC8
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YE91_HELPJ
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Putative phosphate permease jhp_1384
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MEIRNIKEFEKASKKLQKDTLKIALALLFLIGAALLALIFGQANSKGLLLIFAAVIGGYMAMNIGANDVSNNVGPAVGSKAISMGGAILIAAVCEMLGAIIAGGEVVSTIKGRIVSPEFINDAHVFINVMLASLLSGALWLHVATLIGAPVSTSHSVVGGIMGAGMAAAGMSAINWHFLSGIVASWVISPLMGALIAMFFLMLIKKTIAYKEDKKSAALKVVPYLVALMSLAFSWYLIVKVLKRLYAVGFEIQLACGCVLALLIFILFKRFVLKKAPQLENSHESVNELFNVPLIFAAALLSFAHGANDVANAIGPLAAISQTLEDASSPMGSTLNSVPLWIMVVGAAGIALGLSLYGPKLIKTVGSEITELDKMQAFCIALSAVITVLLASQLGLPVSSTHIVVGAVFGVGFLRERLREQSRRRFARIRDNIVAAHFGEDLEEIEGFLERFDKANLKEKSLMLESLKKSKNTAIALELKKKEKKSLKKVYKEEVIKRSILKKIVTAWLVTVPVSALLGALLFVALGFIEKYF
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Potential transporter for phosphate.
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Q9ZJD7
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EX7S_HELPJ
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Exodeoxyribonuclease 7 small subunit (EC 3.1.11.6) (Exodeoxyribonuclease VII small subunit) (Exonuclease VII small subunit)
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MQDELFETEKAPQKNAKNAKNAPKKSFEEHVHSLERVIDRLNDPNLSLKDGMDLYKTAMQELFLAQKLLENAYSEYEKLQTPNKKA
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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_00337}.
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Q9ZJE3
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UBIX_HELPJ
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Flavin prenyltransferase UbiX (EC 2.5.1.129)
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MKLVLGISGASGIPLALRFLEKLPKEIEIFVVASKNAHVVALEESNINLKNAMKDLRPSATFFNEQDIHASIASGSYGIHKMAIIPASMDMVAKIAHGFGGDLISRSASVMLKEKRPLLIAPREMPLSAIMLENLLKLAHSNAIIAPPMMTYYTQSKTLEAMQDFLVGKWFDSLGIENDLYPRWGMN
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Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN. {ECO:0000255|HAMAP-Rule:MF_01984}.
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Q9ZJE5
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KTHY_HELPJ
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Thymidylate kinase (EC 2.7.4.9) (dTMP kinase)
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MYVVLEGVDGAGKSTQVGLLKDRFKNALFTKEPGGTRMGESLRRIALNENISELARAFLFLSDRAEHIESVIKPALKEKKLIISDRSLISGMAYSQFSSLELNLLATQSVLPEKIILLLINKENLKQRLSLKSLDKIENQGIEKLLTIQQKLKTHAYALQEKFGCEVLELDAQKSAKNLHEKIATFIECVV
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Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
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Q9ZJF9
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DPO3A_HELPJ
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DNA polymerase III subunit alpha (EC 2.7.7.7)
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MKENKAFTHLHLHTEYSLLDGANKIKILAKRIKELGMKSVSVTDHGNMFGAIDFYTSMKKEGIKPIIGMEAYIHNDDNLSSKETKQRFHLCLFAKNQEGYENLMFLSSMAYLEGFYYFPRINKKLLREHSKGIIASSACLQGEVNYHLNTNNERNRKYGAKGYDEAKRIACEYQEIFEDDFYLEIMRHGILDQRFIDEQVIKMSLETGLKIIATNDTHYTMPNDAKAQEVAMCVAMGKTLNDKGRLKHSVHEFYIKSPEEMAKLFADIPEALENTQEIADKCVLEIDLKDDKKNPPTPPSFKFTKAYAQNEGLSFEDDASYFAHKAREGLRERLILVPEEKHEQYKERLEKEIEVITNMKFPGYMLIVWDFIRYAKEMGIPVGPGRGSAAGSLVAFALKITDIDPLKYDLLFERFLNPERVSMPDIDTDFCQRRRKEIIEYMIEKYGKYNVAQVITFNKMLAKGVIRDVARVLDMPYKEADDFAKLIPNRLGITLKGYEKNGEFIEGAWELEPKIKELVESNEVAKQVWEYSLNLENLNRNAGVHAAALVVDSQKELWHKTPLFASEKTGGIVTQYSMKYLEPVDLIKFDFLGLKTLTVIDDALKIIKTQHNIDVDFLSLDMDDPKVYKTIQSGDTVGIFQIESGMFQGLNKRLRPSSFEDIIAIIALGRPGPMESGMVDDFVNRKHGVEPIAYAFKELEPILKPTYGTIVYQEQVMQIVQTIGGFSLGEADLIRRAMGKKDAQIMADNKAKFVEGAKNLGHDGQKAANLWDLIVKFAGYGFNKSHSAAYAMITFQTAYLKTYYKHEFMAAMLTSESNKIESVARYIDEVRALEIEVMPPHINSSMQDFSVAEFKNQKGELEKKIVFGLGAVKGVGGEPIKNIIEERAKGDYKSLEDFISRVDFSKLTKKSLEPLVKSGSLDNLGYTRKTMLANLDLICDAGRAKDKANEMMQGGNSLFGAMEGGIKEQVVLDMVDLGEHDAKTLLECEYETLGIHVSGNPLDEFKEEIKGFKNLVKSIDIEELEIGSQAYLLGKIMEVKKKIGKRSGKPYGTADILDRYGKFELMLFEKQLNALEELDINKPLVFKCKIEEQEEVARLRLFEILDLESAREVKIPKARYKDPEKQKEDVREIPPMEMLASSSCSLAIVLENDVKKEFLRQIKESALKHQGKRPLYLIIKDKDKQFKIQSDLMVNEKIKDDFKGLEWRDLA
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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).
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