RPOC_RICM5
ID RPOC_RICM5 Reviewed; 1374 AA.
AC A8F0P8;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=RMA_0190;
OS Rickettsia massiliae (strain Mtu5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=416276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mtu5;
RX PubMed=17916642; DOI=10.1101/gr.6742107;
RA Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT "Lateral gene transfer between obligate intracellular bacteria: evidence
RT from the Rickettsia massiliae genome.";
RL Genome Res. 17:1657-1664(2007).
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; CP000683; ABV84484.1; -; Genomic_DNA.
DR AlphaFoldDB; A8F0P8; -.
DR SMR; A8F0P8; -.
DR EnsemblBacteria; ABV84484; ABV84484; RMA_0190.
DR KEGG; rms:RMA_0190; -.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000001311; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1374
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353422"
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 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 810
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1374 AA; 153461 MW; 0182C06EE1F44A4E CRC64;
MFMSVVNFCG QLSNTQQFDQ IRINIASPDQ VRSWSFGEVT KPETINYRTF KPEKDGLFCA
RIFGPVKDYE CLCGKYKRMK NRGITCEKCG VEVTVSRVRR ERMGHIELAA PVAHIWFLKS
LPSRISTLLD MTMRDIEKIL YFENYVVVDP GLSILQKGEL LTEEELQKAK DKYGEDAFTA
SIGAEVIQQM LKELDFSKLK QELYEELQTT SSEVKKKKLV KRLKLVEDFL ESENKPEWMI
MDVLPVIPPE IRPLVMLDGG RFATSDLNEL YRRVINRNNR LKKLIESKAP DIIVRNEKRM
LQEAVDALFD NGRRGRAAKN ANKRPFKSLS DMLKGKQGRF RQNLLGKRVD YSGRSVIVVG
PELKLHQCGL PKKMALELFK PFIYSKLELY GIATTIKAAK KMVEAEKSEV WDVLEEVIRE
HPVLLNRAPT LHRLGIQAFE PLLIEGKAIQ LHPLVCTAFN ADFDGDQMAV HIPLSIEAQL
EARVFMMSTN NILSPANGRP IIVPDKDIVL GLYYLTLAFD NEVGAGMMFS DLAEMEHALY
NKFITIHTKI KYRRNQLNAE GKMVPVIIDT TYGRLMVGEL LPSNPNIEFK FINKQLTKKD
ISLVIDLVYR HCGQKATVIF ADQLMKLGFK YACSSGISFG MDDMVVPESK STHINETQLE
IQEFEQQYSN GLITYGEKYN KVVDAWSRCT DRVANDMMKE IATPPVNDDP NHQRINAIYM
MAISGARGSF QQIKQLGGMR GLMTKSNGQI IQTPIISNFK EGLTEFECFN SANGMRKGQI
DTALKTASSG YLTRKLVDVA QDCIITEKDC GTDKGIEVKS VIEGGEVIVP LAEKILGRTA
AIDIFHPVTN DLILNKGELI SEAKLEQIES AGLDRIMIKS VLTCESTTGI CSICYGRDLA
TGTLVSEGEA IGVIAAQSIG EPGTQLTMRT FHIGGAATKG AEVSSVDASY DAKVKIISRN
VVINSEERKI VMSRNCELLL LDNNGNEKAR HKIPYGARLL VDDGDMVIKT QKLAEWDPYT
IPIITEKSGK VLFKDMVEGI TIRDVTDEAT GIPSKVIIES KQYSRGAELR PRIQLLGAKG
EVITLSNGLE ARYYLPVGAV LSVEDGVQIS VGDIIARIPK ESTTTKDITG GLPRVAELVE
ARRPKDHAVI AEIDGRVEFG KDYKSKRRII IHPIDETMSI EYMVPKGKHV VVNEGDFVKK
GDLLIDGNPV LQDILKVMGV EVLANYIVKE VQAVYRLQGV KIDDKHIEVI IRQMLQKVEV
TDSGGTTLLA GEKIDRHEFD EINAKAMKNG LKPAEAQLIL QGITKASLQT RSFISAASFQ
ETTRVLTEAA IAGKVDKLRG LKENVIVGRL VPAGTGYFMD KMRKAAIKLD EENV
