RPOBC_HELPY
ID RPOBC_HELPY Reviewed; 2890 AA.
AC O25806; Q9R3R4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=HP_1198;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1308-1465, PROTEIN SEQUENCE OF
RP 2040-2054, AND DETECTION OF FUSION PROTEIN.
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638, HP1, J-116, and SS1;
RX PubMed=9677352; DOI=10.1074/jbc.273.31.19371;
RA Zakharova N., Hoffman P.S., Berg D.E., Severinov K.;
RT "The largest subunits of RNA polymerase from gastric helicobacters are
RT tethered.";
RL J. Biol. Chem. 273:19371-19374(1998).
RN [3]
RP DIVISION OF PROTEIN INTO TWO SMALLER PROTEINS.
RC STRAIN=ATCC 700392 / 26695, and HP1;
RX PubMed=10216866; DOI=10.1046/j.1365-2958.1999.01336.x;
RA Raudonikiene A., Zakharova N., Su W.W., Jeong J.-Y., Bryden L.,
RA Hoffman P.S., Berg D.E., Severinov K.;
RT "Helicobacter pylori with separate beta- and beta'-subunits of RNA
RT polymerase is viable and can colonize conventional mice.";
RL Mol. Microbiol. 32:131-138(1999).
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 -!- INTERACTION:
CC O25806; O25676: HP_1032; NbExp=3; IntAct=EBI-7493676, EBI-527933;
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9677352}.
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:0000269|PubMed:10216866, ECO:0000305|PubMed:9677352}.
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; AE000511; AAD08242.1; -; Genomic_DNA.
DR EMBL; AF068776; AAC25190.1; -; Genomic_DNA.
DR EMBL; AF068254; AAC25712.1; -; Genomic_DNA.
DR EMBL; AF068774; AAC25188.1; -; Genomic_DNA.
DR EMBL; AF068775; AAC25189.1; -; Genomic_DNA.
DR PIR; F64669; F64669.
DR RefSeq; NP_207989.1; NC_000915.1.
DR RefSeq; WP_000037869.1; NC_018939.1.
DR SMR; O25806; -.
DR DIP; DIP-3257N; -.
DR IntAct; O25806; 35.
DR MINT; O25806; -.
DR STRING; 85962.C694_06195; -.
DR PaxDb; O25806; -.
DR PRIDE; O25806; -.
DR EnsemblBacteria; AAD08242; AAD08242; HP_1198.
DR KEGG; hpy:HP_1198; -.
DR PATRIC; fig|85962.47.peg.1287; -.
DR eggNOG; COG0085; Bacteria.
DR eggNOG; COG0086; Bacteria.
DR OMA; QTEKIDD; -.
DR PhylomeDB; O25806; -.
DR Proteomes; UP000000429; 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; 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 1: Evidence at protein level;
KW Direct protein sequencing; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..2890
FT /note="Bifunctional DNA-directed RNA polymerase subunit
FT beta-beta'"
FT /id="PRO_0000048005"
FT REGION 1..1377
FT /note="DNA-directed RNA polymerase subunit beta"
FT REGION 1384..2890
FT /note="DNA-directed RNA polymerase subunit beta'"
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 1451
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 1468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1849
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1851
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1853
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 2253
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"
FT BINDING 2263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 2890 AA; 323575 MW; 3B733A607AF07C98 CRC64;
MSKKIPLKNR LRADFTKTPT DLEVPNLLLL QRDSYDSFLY SKEGKESGIE KVFKSIFPIQ
DEHNRITLEY AGCEFGKSKY TVREAMERGI TYSIPLKIKV RLILWEKDTK SGEKNGIKDI
KEQSIFIREI PLMTERTSFI INGVERVVVN QLHRSPGVIF KEEESSTSLN KLIYTGQIIP
DRGSWLYFEY DSKDVLYARI NKRRKVPVTI LFRAMDYQKQ DIIKMFYPLV KVRYENDKYL
IPFASLDANQ RMEFDLKDPQ GKVILLAGKK LTSRKIKELK ENHLEWVEYP MDILLNRHLA
EPVMVGKEVL LDMLTQLDKN KLEKIHDLGV QEFVIINDLA LGHDASIIQS FSADSESLKL
LKQTEKIDDE NALAAIRIHK VMKPGDPVTT EVAKQFVKKL FFDPERYDLT MVGRMKMNHK
LGLHVPDYIT TLTHEDIITT VKYLMKIKNN QGKIDDRDHL GNRRIRAVGE LLANELHSGL
VKMQKTIKDK LTTMSGAFDS LMPHDLVNSK MITSTIMEFF MGGQLSQFMD QTNPLSEVTH
KRRLSALGEG GLVKDRVGFE ARDVHPTHYG RICPIETPEG QNIGLINTLS TFTRVNDLGF
IEAPYKKVVD GKVVGETIYL TAIQEDSHII APASTPIDEE GNILGDLIET RVEGEIVLNE
KSKVTLMDLS SSMLVGVAAS LIPFLEHDDA NRALMGTNMQ RQAVPLLRSD APIVGTGIEK
IIARDSWGAI KANRAGVVEK IDSKNIYILG ESKEEAYIDA YSLQKNLRTN QNTSFNQVPI
VKVGDKVGAG QIIADGPSMD RGELALGKNV RVAFMPWNGY NFEDAIVVSE CITKDDIFTS
THIYEKEVDA RELKHGVEEF TADIPDVKEE ALAHLDESGI VKVGTYVSAG MILVGKTSPK
GEIKSTPEER LLRAIFGDKA GHVVNKSLYC PPSLEGTVID VKVFTKKGYE KDARVLSAYE
EEKAKLDMEH FDRLTMLNRE ELLRVSSLLS QAILEEPFSH NGKDYKEGDQ IPKEEIASIN
RFTLASLVKK YSKEVQNHYE ITKNNFLEQK KVLGEEHEEK LSILEKDDIL PNGVIKKVKL
YIATKRKLKV GDKMAGRHGN KGIVSNIVPV ADMPYTADGE PVDIVLNPLG VPSRMNIGQI
LEMHLGLVGK EFGKQIARML EDKTKDFAKE LRAKMLEIAN AINEKDPLTI HALENCSDEE
LLEYAKDWSK GVKMAIPVFE GISQEKFYKL FELAKIAMDG KMDLYDGRTG EKMRERVNVG
YMYMIKLHHL VDEKVHARST GPYSLVTHQP VGGKALFGGQ RFGEMEVWAL EAYGAAHTLK
EMLTIKSDDI RGRENAYRAI AKGEQVGESE IPETFYVLTK ELQSLALDIN IFGDDVDEDG
APKPIVIKED DRPKDFSSFQ LTLASPEKIH SWSYGEVKKP ETINYRTLKP ERDGLFCMKI
FGPTKDYECL CGKYKKPRFK DIGTCEKCGV AITHSKVRRF RMGHIELATP VAHIWYVNSL
PSRIGTLLGV KMKDLERVLY YEAYIVKEPG EAAYDNEGTK LVMKYDILNE EQYQNISRRY
EDRGFVAQMG GEAIKDLLEE IDLITLLQSL KEEVKDTNSD AKKKKLIKRL KVVESFLNSG
NRPEWMMLTV LPVLPPDLRP LVALDGGKFA VSDVNELYRR VINRNQRLKR LMELGAPEII
VRNEKRMLQE AVDVLFDNGR STNAVKGANK RPLKSLSEII KGKQGRFRQN LLGKRVDFSG
RSVIVVGPNL KMDECGLPKN MALELFKPHL LSKLEERGYA TTLKQAKRMI EQKSNEVWEC
LQEITEGYPV LLNRAPTLHK QSIQAFHPKL IDGKAIQLHP LVCSAFNADF DGDQMAVHVP
LSQEAIAECK VLMLSSMNIL LPASGKAVAI PSQDMVLGLY YLSLEKSGVK GEHKLFSSVN
EIITAIDTKE LDIHAKIRVL DQGNIIATSA GRMIIKSILP DFIPTDLWNR PMKKKDIGVL
VDYVHKVGGI GITATFLDNL KTLGFRYATK AGISISMEDI ITPKDKQKMV EKAKVEVKKI
QQQYDQGLLT DQERYNKIID TWTEVNDKMS KEMMTAIAQD KEGFNSIYMM ADSGARGSAA
QIRQLSAMRG LMTKPDGSII ETPIISNFKE GLNVLEYFNS THGARKGLAD TALKTANAGY
LTRKLIDVSQ NVKVVSDDCG THEGIEITDI AVGSELIEPL EERIFGRVLL EDVIDPITNE
ILLYADTLID EEGAKKVVEA GIKSITIRTP VTCKAPKGVC AKCYGLNLGE GKMSYPGEAV
GVVAAQSIGE PGTQLTLRTF HVGGTASRSQ DEREIVASKE GFVRFYNLRT YTNKEGKNII
ANRRNASILV VEPKIKAPFD GELRIETVYE EVVVSVKNGD QEAKFVLRRS DIVKPSELAG
VGGKIEGKVY LPYASGHKVH KGGSIADIIQ EGWNVPNRIP YASELLVKDN DPIAQDVYAK
EKGVIKYYVL EANHLERTHG IKKGDMVSEK GLFAVIADDN GREAARHYIA RGSEILIDDN
SEVSTNSVIS KPTTNTFKTI ATWDPYNTPI IADFKGKVGF VDVIAGVTVA EKEDENTGIT
SLVVNDYIPS GYKPSLFLEG ANGEEMRYFL EPKTSIAISD GSSVEQAEVL AKIPKATVKS
RDITGGLPRV SELFEARKPK PKDVAILSEV DGIVSFGKPI RNKEHIIVTS KDGRSMDYFV
DKGKQILVHA DEFVHAGEAM TDGVISSHDI LRISGEKELY KYIVSEVQQV YRRQGVSIAD
KHIEIIVSQM LRQVRILDSG DSKFIEGDLV SKKLFKEENA RVIALKGEPA IAEPVLLGIT
RAAIGSDSII SAASFQETTK VLTEASIAMK KDFLEDLKEN VVLGRMIPVG TGMYKNKKIV
LRALEDNSKF
