RPOC_RICPR
ID RPOC_RICPR Reviewed; 1372 AA.
AC Q9ZE20; Q9RH36;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {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=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=RP141;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RC STRAIN=ATCC VR-142 / Breinl;
RX PubMed=10508014; DOI=10.1128/aac.43.10.2400;
RA Drancourt M., Raoult D.;
RT "Characterization of mutations in the rpoB gene in naturally rifampin-
RT resistant Rickettsia species.";
RL Antimicrob. Agents Chemother. 43:2400-2403(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_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_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, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR EMBL; AJ235270; CAA14609.1; -; Genomic_DNA.
DR EMBL; AF076437; AAF22440.1; -; Genomic_DNA.
DR PIR; B71724; B71724.
DR RefSeq; NP_220532.1; NC_000963.1.
DR RefSeq; WP_004597190.1; NC_000963.1.
DR AlphaFoldDB; Q9ZE20; -.
DR SMR; Q9ZE20; -.
DR STRING; 272947.RP141; -.
DR EnsemblBacteria; CAA14609; CAA14609; CAA14609.
DR GeneID; 57569269; -.
DR KEGG; rpr:RP141; -.
DR PATRIC; fig|272947.5.peg.143; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000002480; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 2.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
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; 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; 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 SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 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..1372
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067786"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 808
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 882
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT VARIANT 33
FT /note="S -> G (in strain: Breinl)"
SQ SEQUENCE 1372 AA; 153382 MW; 7241DF46696F465C CRC64;
MSVVNFYGQL SNTQQFDQIR INIASPDQVR SWSFGEVTKP ETINYRTFKP EKDGLFCARI
FGPVKDYECL CGKYKRMKNR GITCEKCGVE VTVSRVRRER MGHIELAAPV AHIWFLKSLP
SRISTLLDMT MRDVEKILYF ENYVVVDPGL SILQKGELLT EEELQKAKDK YGEDAFTASI
GAEVIQQMLK ELDFSKLKQE LYDELHITSS EVKKKKLVKR LKLVEDFLES ENKPEWMIMD
VLPVIPPEIR PLVMLDGGRF ATSDLNELYR RVINRNNRLK KLIESKAPDI IVRNEKRMLQ
EAVDALFDNG RRGRAAKNAN KRPFKSLSDM LKGKQGRFRQ NLLGKRVDYS GRSVIVVGPE
LKLHQCGLPK KMALELFKPF IYSKLELYGI ATTIKAAKRM VEAEKPEVWD VLEEVIREHP
VLLNRAPTLH RLGIQAFEPL LIEGKAIQLH PLVCAAFNAD FDGDQMAVHI PLSIEAQLEA
RVFMMSTNNI LSPANGRPII VPDKDIVLGL YYLTIAFDNE VGEGMMFSDL AEMEHALYNK
FITIHTKIKY RRDQLNAEGK MVPVIIDTTY GRLMVGELLP SNPNIEFKFI NKQLTKKDIS
LVIDLVYRHC GQKATVIFAD QLMKLGFKYA CSSGISFGMD DMVVPESKST HINETQLEIK
EFEQQYSNGL ITYGEKYNKV VDAWSRCTDR VANDMMKEIA TPPVNDYPNH QKINAIYMMA
ISGARGSFQQ IKQLGGMRGL MTKSNGQIIQ TPIISNFKEG LTEFECFNSA NGMRKGQIDT
ALKTASSGYL TRKLVDVAQD CIITEKDCGT DKGIEVKSVI EGGEIIVPLA EKILGRTAAI
DIFHPVTNDL ILNKGELINE SKLEQIESAG LDRIMIKSVL TCESSTGICS ICYGRDLATG
TLVSEGEAIG VIAAQSIGEP GTQLTMRTFH IGGAATKGAE VSSVEASYDA KVKIISRNVV
INSEERKIVM SRNCELLLLD NNGNEKARHK IPYGARLLVD DGDMVIKTQK LAEWDPYTIP
IITEKSGKVL FKDMVEGISI RDVTDEATGI PSKVIIESKQ YSRGAELRPR IQLLDSKGEV
ITLSNGLEAR YYLPVGAVLS VEDGIQISVG DIIARIPKES TTTKDITGGL PRVAELVEAR
RPKDHAVIAE VDGRVEFGKD YKSKRRIIIH PIDGTMSIEY MVPKGKHVVV NEGDFVKKGD
LLIDGNPVLQ DILKVMGVEV LANYIVKEVQ AVYRLQGVKI DDKHIEVIIR QMLQKVEVTD
SGGTTLLVGE KIDRHEFDEI NAKAMKNGLK PAEAQLILQG ITKASLQTRS FISAASFQET
TRVLTEAAIA GKVDKLRGLK ENVIVGRLVP AGTGYFMDKM RKAAVKLDEE NV
