RPOBC_WOLTR
ID RPOBC_WOLTR Reviewed; 2839 AA.
AC Q5GRY9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Bifunctional DNA-directed RNA polymerase subunit beta-beta';
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321, ECO:0000255|HAMAP-Rule:MF_01322};
DE Includes:
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Includes:
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoBC; OrderedLocusNames=Wbm0647;
OS Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=292805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRS;
RX PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA Koonin E., Slatko B.;
RT "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT human pathogenic nematode.";
RL PLoS Biol. 3:599-614(2005).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01321, ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01321,
CC ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01322};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta/beta' and
CC 1 omega subunit. When a sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321, ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- MISCELLANEOUS: Fusion of rpoB and rpoC occurs naturally in Helicobacter
CC species and at least some Wolbachia; the protein has been artificially
CC split in two in H.pylori. The split protein seems to function normally.
CC {ECO:0000250|UniProtKB:O25806}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the RNA polymerase
CC beta chain family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the RNA polymerase
CC beta' chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017321; AAW71235.1; -; Genomic_DNA.
DR SMR; Q5GRY9; -.
DR STRING; 292805.Wbm0647; -.
DR PRIDE; Q5GRY9; -.
DR EnsemblBacteria; AAW71235; AAW71235; Wbm0647.
DR KEGG; wbm:Wbm0647; -.
DR eggNOG; COG0085; Bacteria.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_0_1_5; -.
DR OMA; QTEKIDD; -.
DR Proteomes; UP000000534; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 2.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..2839
FT /note="Bifunctional DNA-directed RNA polymerase subunit
FT beta-beta'"
FT /id="PRO_0000225503"
FT REGION 1..1433
FT /note="DNA-directed RNA polymerase subunit beta"
FT REGION 1436..2839
FT /note="DNA-directed RNA polymerase subunit beta'"
FT BINDING 1501
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1503
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1893
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1895
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1897
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 2839 AA; 318102 MW; 6AAC907379C9F9A9 CRC64;
MVDSSYMCAS NAFIPRISYS RSIDLKDSLL DLVKVQKESY KSFTPGNHGN ERLESIFRSV
FPINDPLHRA TIEFISCRID NPKYDESECI KRGITFSARV IASIRLVIMQ DGISLDEYKS
IKGSGDHSKL STIIKFIGEQ EVHFCELPMM TDKGTFIING VEKVIVSQMH RSPGVFFDSD
KGKTYNSGKL IYSARVIPYR GSWLDIEFDV KDLLYFRIDR KRKLPISVLL KALGLSNSDI
LDRFYEKIKY IKYKNSWKVP FVPDKFKGVR LPFDLMDVEG NVLFKANVRI TSRLAKKLHD
DELKEYLVPF DSICGLFLAE DLIDSVSSTK ILSAGESIKI EDVKKLELLS IGEISVLNID
NLSVGPYILN TLFLDENMSY QDALYEIYKV LRPGEVPVLE IVEEFFHNLF FNPEYYDLSN
IGRLKLNSYL GLDYDEDLTV LTHEDIIEIV RKIVLLRDGQ GSVDDIDHLG NRRVRSVGEF
IENQFRAGLL KLERAVIDSM STSSLDKVSS PDFINPKVLT NVLRDFFNSS QLSQFMDQTN
PLSEITHKRR LSALGPGGLT RDRAGFEVRD VHPTHYGRIC PIETPEGQNI GLINSLAIYA
RVNKYGFIES PYRKVINRVA TDQIEYLSAI DEGLYYIADA SAKLDNNNRF IDDMLYCRYA
GNFVMVSSDQ VSYIDVSPKQ VISVAASLIP FLENDDANRA LMGSNMQRQA VPLLKPTAPL
VGTGIESFVA SGSGAVVLAK RDGIVDSSDS NSIVIRAFDE ERVNYLGVDI YHLKKFQRSN
HNTCINQKPL VRIGDYVKEG DVIADGPAIN SGELALGQNL LVAFMSWQGY NFEDSIIISS
EIVKKDLFTS IHIEEFECVV HDTPLGSEKI TRAIPGVNEE NLYHLDNSGI VKIGTRVGPG
YILVGKITPK PSLLLPPETK LLMTIFGEKS FDCADSSLYT SPDVEGTVID VQVFTRRGVE
ENERALLIKQ KEMNDLEKER DYIINVASEY FYDELKKLLV HSCSQDQEKL DAIEREQWWG
IGLKNRSISE QVKNLKKDFD KKVSNTIAQF KQKVEKLDEG YDLPQGVLMS VKVFIAVKHS
LQPGDKMAGR HGNKGVISRV VPVEDMPYLE DGTPVDIILN PLGVPSRMNV GQILETHVGW
ACKKLGERVG NILDEINKIN SDFCKEIRSL DDNNFAKFAA VYFDNKKTEE VRDDEITDSL
VNIPNKGLLN DELNALVENY LNSCKSAYDN LRSFLIEVYS CGSDVSICNN IRDISNSNLI
EFAHKLRNGI PVAAPVFEGP KDKNIIKLFT LAGLDPSGQT EAYDGRTGEK FDRKVTVGYM
YMLKLHHLVD DKIHARSVGP YSLVTQQPLG GKSHFGGQRF GEMECWALQA YGAAYTLQEM
LTVKSDDING RVKIYESIIK GDSNFECGTP ESFNVMIKEL RSLCLNVALK QNNVVIEDIS
HTNIAQSFDK IGISIASPEN IKSMSYGEVK DVSTANYRTF KVEKGGLFCP KIFGPVNDDE
CLCGKYKKRR HRGRICEKCG VEVTSSKVRR ERMGHIELAS PVAHIWFLKS LPSRIGALLD
MSLRDIENIL YSDNYIVIDP LVSPFEKGEI ISEKIYNEAK DDYGIDSFVA MQGVEAIREL
LTCLDLHQIR KDLRLELESV ASEIRRKKII KRLRIIENFI KSGNRPEWMI LTTIPILPPD
LRPLVSLESG RPAVSDLNHH YRTIINRNNR LRKLLSLNPP EIMIRNEKRM LQEAVDSLFD
NSRRNALTNK AGAIGYKKSI SDMLKGKQGR FRQNLLGKRV DYSGRSVIVV GPALKLNQCG
LPKRMALELF KPFVYSKLKL YGMAPTIKFA SKLIRAEKPE VWDMLEEVIK EHPVLLNRAP
TLHRLGIQAF EPILIEGKAI QLHPLVCTAF NADFDGDQMA VHVPISLEAQ LEARVLMMST
NNVLSPSNGR PIIVPSKDII LGIYYLTLQE QTDKEGDDLP FLGTFGEVEH SLSDGTLHIH
SSIKYRIEYT NSEGETCYKT IRTTPGRLIL WQIFPKHENL NFDLVNQVLT VKEVTSIVDL
IYRNCGQSAT VEFSDRLMVL GFEYATFSGI SFSRCDLVIP ETKAEHVDHA RGEIKKFSMQ
YQDGLITRSE RYNKVIDEWS KCTDMIANDM LKSISVYDRN SKYNSVYMMV NSGARGSTSQ
MKQLAGMRGL MTKPSGEIIE TPIISNFREG LNVFEYFNST HGARKGLADT ALKTANSGYL
TRRLVDVSQN CIVTKHDCKT KNGLVVRATV EGGTIVASLE SVVLGRTAAN DIYNPVTKEL
LVKAGELIDE DKVKQINIAG LDAVKIRSPL TCEVSPGVCS LCYGRDLATG KIVSIGEAVG
VIAAQSVGEP GTQLTMRTFH IGGVMTRGVE SSNIIASINA KIKLSNSNII IDKNGDKIAI
SRSCEVVLID SLGSEKLRHS IPYGAKLCVD EGKSVKIGDK IAEWDPYTLP IITEKTGTVL
YQDLKDGVSI TEVMDESTGI SSKVVKDWKL YSGGANLRPR IVLLDDNGKV MTLASGIEAC
YFIPIGAVLN VQDGQKVHAG DVITRTPRES VKTRDITGGL PRVIELFEAR RPREHAIVSE
IDGHVVFSEK DRRGKRSVLI KPLNEQISPI EYLVSRSKHV IVNEGDFVRK GDLLMDGDPD
LHDILRVLGL EALAHYMISE IQQVYRLQGV RIDNKHLEVI LKQMLQKVEI TDPGDTMYLV
GESIDKLEVD KGNDVMSNSG KRPACYLPIL QGITRASLET KSFISAASFQ ETTKVLTEAA
FCGKEDPLSG LKENVIVGRL IPAGTGLIMS KVRALSLCDN MDKYEKYFDI EAYDEKLLED
NGCHLHSGKK ESVAESRYN
