RPOBC_WOLPM
ID RPOBC_WOLPM Reviewed; 2837 AA.
AC Q73IW9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=WD_0024;
OS Wolbachia pipientis wMel.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=163164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA O'Neill S.L., Eisen J.A.;
RT "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT streamlined genome overrun by mobile genetic elements.";
RL PLoS Biol. 2:327-341(2004).
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}.
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DR EMBL; AE017196; AAS13791.1; -; Genomic_DNA.
DR SMR; Q73IW9; -.
DR STRING; 163164.WD_0024; -.
DR PRIDE; Q73IW9; -.
DR EnsemblBacteria; AAS13791; AAS13791; WD_0024.
DR KEGG; wol:WD_0024; -.
DR eggNOG; COG0085; Bacteria.
DR eggNOG; COG0086; Bacteria.
DR OMA; QTEKIDD; -.
DR Proteomes; UP000008215; 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; 1.
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..2837
FT /note="Bifunctional DNA-directed RNA polymerase subunit
FT beta-beta'"
FT /id="PRO_0000225502"
FT REGION 1..1433
FT /note="DNA-directed RNA polymerase subunit beta"
FT REGION 1436..2837
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 2235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2316
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"
SQ SEQUENCE 2837 AA; 317782 MW; E6181198748E51C8 CRC64;
MVDSSYMYAS GAFVPRVSYS RSIDLKDSLL DLVKVQKESY DSFTPKNKGN ERLEVIFHTI
FPINDPLRRA TIEFISCRVD DPKYDESECI KRGVTFSAQV IASIRLVVMQ DGISLDEYKS
IKESGDHSKL ATVVKSIEEQ KVHFCGLPMM TDKGTFIING VEKVIVSQMH RSPGVFFDSD
KGKTYNSGKL IYSARIIPYR GSWLDIEFDV KDHLYFRVDR KRKLPISVLL KALGLSNNDI
LDRFYEKIKY VKHKDGWKVP FVPDKFKGVR LPFDLMDIEG NVLLKANVRI TSRLAKKLYD
NELKEYLVPF NSICGLFLAE DLMDSASSTK ILSAGESIKL EDIKKLELLS VDEISVLNID
NLFVGPYILN TLFLDENMSY QDALYEIYRV LRPGEVPVLE IVEEFFRNLF FSPEYYDLSN
IGRLKLNSYL GLNYDEDLTV LTHEDIIEIV KKIVLLRDGQ GSVDDIDHLG NRRVRSVGEF
IENQFRTGLL KLERAIVDSM STSSLDKVSP SDFINPKVLT NVLRDFFNSS QLSQFMDQTN
PLSEITHKRR LSALGPGGLT RERAGFEVRD VHPTHYGRIC PIETPEGQNI GLINSLAIYA
RINKYGFIES PYRKVVNRVV TDQIEYLSAI DEGSHHIADT SVKLDENNCF VDDMLYCRYA
GSFVMVSSDQ VSYIDVSPKQ VISVAASLIP FLENDDANRA LMGSNMQRQA VPLLKPTAPL
VATGMESFVA SGSGAVVLAK RDGIVDSSDS NSIVIRAFDK ERVNYLDVDI YHLRKFQRSN
HNTCINQRPL VCVGDYVKKG DVIADGPAIN SGELALGKNL LVAFMSWQGY NFEDSIIISS
EVVKKDLFTS IHIEEFDCVV HDTPLGSEKI TRAIPGVNEE NLYHLDDSGI VKIGTRVGPG
YILVGKVTPK PSLSLPPETK LLMTIFGEKS FDCADSSLYT SPDVEGTVID VQVFTRRGVE
ENERALLIKQ KEINDFEEER DYIINVTSEY FYDELKKLLI NSGSQDREKF DSIEREQWWG
IGLKNQSISE QVKSLKKDFD EKVSHAIAQF KRKVEKLHEG YDLPQGVSMS VKVFIAVKHS
LQPGDKMAGR HGNKGVISRV VPVEDMPYLE DGTPVDIILN PLGVPSRMNV GQILETHVGW
ACRKLGEKVS NILDEINKIK SAFCKGIRSL NDDNFTQFAV AYLDNKKIEN IDDDEITASV
LNTPNKNALN DELNELVENY LNSCKSSYSN LRNFLIEVYS YGSNVSICND IRNISDNNLI
EFARKLRDGV PVAAPVFEGP KDEQIAKLFE LAGLDNSGQA VLYDGCSGEK FDRKVTVGYM
YMLKLHHLVD GKIHARSVGP YSLVTQQPLG GKSHFGGQRF GEMECWALQA YGAAYTLQEM
LTVKSDDING RVKIYESIIK GDSNFECGIP ESFNVMIKEL RSLCLNVDLK QNDVVIEDIS
HTNIAQPFNE VSISIASPES IKRISCGEIE DVLTANYRTF KVEKGGLFCP KVFGPVNDDE
CLCGKYKKRR HRGRICEKCG VEVTSSKVRR ERMGHIELAS PVAHIWFLKS LPSRIGALLD
MSLRDIENIL YSDNYIVIDP LVSPFEKGEI ISEKAYNEAK DSYGIDSFVA MQGVEAIREL
LTRLDLHEIR KDLRLELESV ASEIRRKKII KRLRIVENFI KSGNRPEWMI LTTIPILPPD
LRPLVSLESG RPAVSDLNHH YRTIINRNNR LRKLLSLNPP EIMIRNEKRM LQEAVDSLFD
NSRRNTLVNK AGAVGYKKSI SDMLKGKQGR FRQNLLGKRV DYSGRSVIVV GPTLKLNQCG
LPKRMALELF KPFVYSKLKM YGMAPTIKFA SKLIRAEKPE VWDMLEEVIK EHPVLLNRAP
TLHRLGIQAF EPILIEGKAI QLHPLVCTAF NADFDGDQMA VHVPISLEAQ LEARVLMMST
NNVLSPSNGR PIIVPSKDIV LGIYYLTLQE PKEDNLPSFG AFCEVEHSLS DGILHIHSSI
KYRMEYINSS GETHYKTVCT TPGRLILWQI FPKHENLGFD LINQILTVKE ITGIVDLVYR
NCGQSATVAF SDKLMVLGFE YATFSGVSFG RCDMVIPETK ATHVDHARGE IKKFSMQYQD
GLITRSERYN KVIDEWSKCT DMIANDMLKA ISIYDGNSKY NSVYMMVNSG ARGSTSQMKQ
LAGMRGLMTK PSGEIIETPI ISNFREGLNV FEYFNSTHGA RKGLADTALK TANSGYLTRR
LVDVSQNCIV AKHDCKTKNG LVVRATVEGS TIVASLESVV LGRTAANDIY NPVTKELLVK
AGELIDEDKV KQISIAGLDV VKIRSPLTCE ISPGVCSLCY GRDLATGKIV SIGEAVGVIA
AQSVGEPGTQ LTMRTFHIGG VMTRGVESSN IIASINAKIK LNNSNIIIDR NGNKIVISRS
CEVVLIDSLG SEKLKHSVPY GAKLYVDESG SVKIGDKVAE WDPYTLPIIT EKTGTVSYQD
LKDGISITEV MDESTGISSK VVKDWKLHSG GANLRPRIVL LDDNGKVMTL ASGVEACYFI
PIGAVLNVQD GQKVHAGDVI TRTPRESVKT RDITGGLPRV IELFEARRPK EHAIVSEIDG
YVAFSEKDRR GKRSILIKPV DEQISPVEYL VSRSKHVIVN ESDFVRKGDL LMDGDPDLHD
ILRVLGLEAL AHYMISEIQQ VYRLQGVRID NKHLEVILKQ MLQKVEITDP GDTMYLVGES
IDKLEVDREN DAMSNSGKRP THYLPILQGI TRASLETSSF ISAASFQETT KVLTEAAFCG
KSDPLSGLKE NVIVGRLIPA GTGLIMNKIR ALSLCDNVDK YEKYFDIETY DEEWLMDNGC
HLHSDEEESV VAYDQSN
