RPOBC_HELPJ
ID RPOBC_HELPJ Reviewed; 2890 AA.
AC Q9ZK23;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=jhp_1121;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(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 -!- 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; AE001439; AAD06699.1; -; Genomic_DNA.
DR PIR; B71846; B71846.
DR RefSeq; WP_000037845.1; NC_000921.1.
DR SMR; Q9ZK23; -.
DR IntAct; Q9ZK23; 1.
DR STRING; 85963.jhp_1121; -.
DR EnsemblBacteria; AAD06699; AAD06699; jhp_1121.
DR KEGG; hpj:jhp_1121; -.
DR eggNOG; COG0085; Bacteria.
DR eggNOG; COG0086; Bacteria.
DR OMA; QTEKIDD; -.
DR Proteomes; UP000000804; 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 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..2890
FT /note="Bifunctional DNA-directed RNA polymerase subunit
FT beta-beta'"
FT /id="PRO_0000048004"
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; 323750 MW; 6667F0E2EF92B817 CRC64;
MSKKIPLKNR LRADFTKTPT DLEVPNLLLL QRDSYDSFLY SKDGKESGIE KVFKSIFPIQ
DEHNRITLEY AGCEFGKSKY TVREAMERGI TYSIPLKIKV RLILWEKDTK SGEKNGIKDI
KEQSIFIREI PLMTERTSFI INGVERVVVN QLYRSPGVIF KEEESSTSSN KLIYTGQIIP
DRGSWLYFEY DSKDVLYARI NKRRKVPVTI LFRAMDYQKQ DIIKMFYPLV KVRYENDKYL
IPFASLDANQ RMEFDLKDPQ GKIILLAGKK LTSRKIKELK ENHLEWVEYP MDILLNRHLA
EPVMVGKEVL LDMLTQLDKN RLEKIHDLGV QEFVIINDLA LGHDASIIHS FSADHESLKL
LKQTEKIDDE NALAAIRIHK VMKPGDPVTT EVAKQFVKKL FFDPERYDLT MVGRMKMNHK
LGLHVPDYIT TLTHEDIITT VKYLMKIKNN QGKIDDRDHL GNRRIRAVGE LLANELHSGL
VKMQKTIKDK LTTMSGAFDS LMPHDLVNSK MITSTIMEFF MGGQLSQFMD QTNPLSEVTH
KRRLSALGEG GLVKDRVGFE ARDVHPTYYG QFGPIETPEG QNIGLINTLS TFTRVNDLGF
IEAPYKKVVD GKVAGETIYL TAIQEDSHII APASTPIDEE GNILGDLIET RVEGEIVLNE
KSKVTLMDLS SSMLVGVAAS LIPFLEHDDA NRALMGTNMQ RQAVPLLRSD APIVGTGIEK
IIARDSWGAI KANRAGVVEK IDSKNIYILG EGKEEAYIDA YSLQKNLRTN QNTSFNQVPI
VKVGDKVEAG QIIADGPSMD RGELALGKNV RVAFMPWNGY NFEDAIVVSE RITKDDVFTS
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 EFGKQIASML EDKTKDFAKE LRAKMLEIAN AINEKDPLTI HVLENCSDEE
LLEYAKDWSK GVKMAIPVFE GISQEKFYKL FELAKIAMDG KMDLYDGRTG EKMRERVNVG
YMYMIKLHHL VDEKVHARST GPYSLVTHQP VGGKALFGGQ RFGEMEVWAL EAYGAAHTLK
EMLTIKSDDI RGRENAYRAI AKGEQVGESE IPETFYVLTK ELQSLALDIN IFGDDVDEDG
APRPIMIKED 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 GITATFLDHL KTLGFRYATK AGISISMEDI ITPKDKQKMV EKAKVEVKKI
QQQYDQGLLT DQERYNKIID TWTEVNDRMS KEMMSAIAKD 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 VKKGDIVSEK GLFAVVADDN GREAARHYIA RGSEILIDDN
SEVSANSVIS KPTTNTFKTI ATWDPYNTPI IADFKGKVNF VDVIAGVTVA EKEDENTGIT
SLVVNDYIPS GYKPSLFLEG ANGEEMRYFL EPKTSIAISD GSSVEQAEVL AKIPKATVKS
RDITGGLPRV SELFEARKPK PKDVAILSEV DGIVSFGKPI RNKEHIIVTS KDGRLTDYFV
DKGKQILVHA DEFVHAGEAM TDGVVSSHDI LRISGEKELY KYIVSEVQQV YRRQGVSIAD
KHIEIIVSQM LRQVRILDSG DSKFIEGDLV SKKLFKEENT RVIALKGEPA IAEPVLLGIT
RAAIGSDSII SAASFQETTK VLTEASIAMK KDFLEDLKEN VVLGRMIPVG TGMYKNKKIV
LRALEDNSKF
