RPOBC_WOLSU
ID RPOBC_WOLSU Reviewed; 2883 AA.
AC Q7MA56;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoBC; OrderedLocusNames=WS0467;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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; BX571658; CAE09607.1; -; Genomic_DNA.
DR RefSeq; WP_011138407.1; NC_005090.1.
DR SMR; Q7MA56; -.
DR STRING; 273121.WS0467; -.
DR PRIDE; Q7MA56; -.
DR EnsemblBacteria; CAE09607; CAE09607; WS0467.
DR KEGG; wsu:WS0467; -.
DR eggNOG; COG0085; Bacteria.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_0_1_7; -.
DR OMA; QTEKIDD; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000422; 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; -; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 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; IPR037034; RNA_pol_Rpb2_2_sf.
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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..2883
FT /note="Bifunctional DNA-directed RNA polymerase subunit
FT beta-beta'"
FT /id="PRO_0000048006"
FT REGION 1..1377
FT /note="DNA-directed RNA polymerase subunit beta"
FT REGION 1382..2883
FT /note="DNA-directed RNA polymerase subunit beta'"
FT BINDING 1447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1846
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1848
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1850
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 2883 AA; 321724 MW; BFC9D5472630CFB1 CRC64;
MPTTLKSGNR LRVDFTKIPQ NIAIPNLLQL QRNSYDSFLM PIENGESGIE KVFRSIFPIH
DAQNRITLEY AGCEYGKPRY TVREAMERGL TYSVPLKVKI RLVLWEKDEK TGEKLGVKDI
KEQSIFVREI PLMTDRTSFI INGVERVVVN QLHRSPGVIF KEEESATSSN KLIYTGQIIP
DRGSWLYFEY DAKDTLYVRI NKRRKVPVTI LFRALGYSKQ DVIKTFYPLM KVKAEAGKYL
MPFNPEEFIG RIEFDIRDTS GNLIIGAGKR LTQKRAKTLK EQGLEWVEYP VEILLDRHLA
EPIVDKESGE VILDTLVQLD EGKLKKIHEL GIKEFTIAND LAQGVDASII HSFVADNESL
KLLKQTEKID DDNDLAAIRI YKVMRPGEPV TKDAAKSFVQ QLFFDPERYD LTRVGRMKMN
HKLDIEVPDY VTVLTHEDII CTVKYLIRVK NGQGHIDDRD HLGNRRIRAI GELLANELHT
GLVKMQKAIR DKLTTMSGNL DELMPHDLVN SKMITSTILE FFTGGQLSQF MDQTNPLSEV
THKRRLSALG EGGLVKERAG FEVRDVHPTH YGRICPIETP EGQNIGLINT LSTYSKVNDL
GFIEAPYKKV IEGKVTDEVV YLTATQEEGL VIAPASTVLE TDGAIKEDLI ETRIDGEIVL
SEKSKVDLID LSPGMVVGVA ASLIPFLEHD DANRALMGSN MQRQAVPLLN PDAPVVGTGM
EKTVARDSWE AIKATRGGIV EKVDAKNIYI LGEDENGAYI DHYSLQKNLR TNQNTCFSQA
PIVHEGETIE AGQVIADGPN MDKGELALGK NIRVAFMPWN GYNFEDAIVV SEKLIREDTF
TSIHIYEKEI EARELKHGVE EITRDIPNVR EEELAHLDES GIVKIGTFVN AGMILVGKVS
PKGEVKPTPE ERLLRAIFGE KAGHVVNKSL YCPPSLEGTV VDVKIFTKKG YDKDQRAIAA
YEEEKARLDL EHHDKLMMLD REEMLRLTSM LSKEPLASDV VVNEKSYKKG ELIEKGDLAK
INRFAMNALV KSFPKSIQEA YDQLKSNFLE QKKNLSEEHE EKLSVLEKDD ILPSGVVKLV
KIYVATKRKL KVGDKMAGRH GNKGIVSNIV REIDMPYTKD GEPVEIVLNP LGVPSRMNIG
QILEVHLGLV GKKLGAQINE MFENQTKDWM GALRAKIIEI AQVSKMTGVD EFVSSLSDEA
LLSYARDWRR GVKFATPVFE GVNEEEFTKL FELARIDTDG KTELYDGKTG AKMKERVNVG
YMYMLKLHHL VDEKVHARST GPYSLVTQQP VGGKALFGGQ RFGEMEVWAL EAYGAAHTLK
EMLTVKSDDV EGRVKAYKAI TRGEPVKESE IPETFYVLTK ELQSLALDVT VYGETEEDSF
VPMPIKEDDR PSDFNAFQLM LASPDKIMSW SNGEVKKPET INYRTLKPER DGLFCAKIFG
PVRDYECLCG KYKKMRYKGV VCEKCGVEVT SSKVRRSRMG HIELVTPVAH IWYVNSLPSR
IGTLLGVKMK DLERVLYYEA YIVKTPGEAF YDNEGTKPVA KYDVLNEEQY QSLNQRFEHT
GFVAQMGGEA VKELLAQIDL VELLHTLREE IKATNSEAKK KTIIKRLKVV ESFINSGNRP
EWMMLTVLPV LPPDLRPLVA LDGGKFAVSD VNDLYRRVIN RNQRLKRLME LDAPEIIIRN
EKRMLQEAVD ALFDNGRNAN AVKGANKRPL KSLSEIIKGK QGRFRQNLLG KRVDFSGRSV
IVVGPNLRMD QCGLPKGMAL ELFKPHILAK LEEKGYATTL KQAKKMIEQK TNEVWECLQE
IVEGYPIMLN RAPTLHKQSI QAFHPKLIDG KAIQLHPLVC SAFNADFDGD QMAVHVPLSQ
EAITECKLLM LSSMNILLPA SGKAVTVPSQ DMVLGLYYLS LAKEGSRGEH KLFSNVDEIM
IALDADAVEI NTKIRTIVDR RPLYTTVGRM IIKSILPDFV PVSLWNKVLK KKDIAALIDH
VYKEGGLGIT ARFLDNLKDL GFKYATTAGI SISSDDIRVP DIKRKTVEAA KKKVKEIQAQ
FGAGLLTEQE RYNKIIDVWT DTNNGLGSEM MKLVQADKGG FNSIYMMADS GARGSAAQIR
QLSAMRGLMA KPDGTIIETP IISNFKEGLN VLEYFISTHG ARKGLADTAL KTANAGYLTR
KLIDVSQNVK IVMEDCGTHE GVEITDIAIG SELIEPLEER IFGRVVAEDV IDPITNEILV
SEGSLIDEEM AKKIKEAGVK AVIIRTPVTC KAEKGVCSKC YGLNLGEGKV TNPGEAVGVV
AAQSIGEPGT QLTLRTFHIG GTASRSQEER QVVVEKEGFI RYYNIKTYKN KEGKTVVANR
RNAAVLLVEP KIKAPFEGEL RVDTAHEEMV ISVIGKSETV RYSLRKSDVA KPNELAGVTG
KIEGKFYIPY GSGTKVREDG SIVEIIKDGW NIPNRIPYAS ELKVEDNAPI TQKIFSKEKG
IVKYYRLKGD HLERYKEITK GEKVTEKGIF AVIADTNDRE AIRHYIARGS IIELADGAEV
KPDSLVASPA SSEQIVIADW DPYSNPIIAE EAGVVKYEDI IPGVTVTEQV DELTGQSRLV
VNEYLPTSFK PTIVVASAAG NLIRYALDSK TAIFVGDGAE VEVADVLAKT PKALAKSKDI
TGGLPRVSEL FEARKPKDPA VLAEIDGVVS FGKPIRGKER IIITADDGRT TEYAVDKSKH
ILVHHGEFVH AGESITDGIV SSHDILRISG EKELHKYIVS EVQQVYRRQG VNIADKHIEI
IVSQMLRQVR IVDSGNTKFI EGDLVSKRHF KEENERTIRL GGEPAIAEPV LLGITRAAIG
SDSIISAASF QETTKVLTEA SIAAKIDFLE DLKENVVLGR MIPVGTGIYK NKKIRIKEKT
EGA
