ID   RPOC_RICBR              Reviewed;        1361 AA.
AC   Q1RHD1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=RBE_1152;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05233.1; -; Genomic_DNA.
DR   RefSeq; WP_011477811.1; NC_007940.1.
DR   AlphaFoldDB; Q1RHD1; -.
DR   SMR; Q1RHD1; -.
DR   STRING; 336407.RBE_1152; -.
DR   PRIDE; Q1RHD1; -.
DR   EnsemblBacteria; ABE05233; ABE05233; RBE_1152.
DR   KEGG; rbe:RBE_1152; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_5; -.
DR   OMA; YRNIRVE; -.
DR   Proteomes; UP000001951; 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; -; 1.
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..1361
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000240821"
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"
SQ   SEQUENCE   1361 AA;  152026 MW;  8158940BE7C96B08 CRC64;
     MSVVNFYGQL SNTQQFDQIR INIASPEQVR SWSFGEVIKP ETINYRTFKP EKDGLFCARI
     FGPVKDYECL CGKYKRMKNR GITCEKCGVE VTVSRVRRER MGHIELAAPV AHIWFLKSLP
     SRISTLLDMT MRDIEKILYF ENYVVVDPGL SILQKGELLT EEELQKAKDK YGEDAFTASI
     GAEVVQQMLK ELDFPTLKQE LYEELQNTTS EVKKKKLVKR LKLVEDFLES ENKPEWMIMN
     VLPVMPPELR 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 YYLTLAFDHE VGEGMMFSDL TEMEHALYNK
     FITIHTKIKY RRNQLNAEGK IVPVIVDTTY GRLMVGELLP SNPNIEYKFI NKPLTKKDIS
     LVIDLVYRHC GQKATVIFAD QLMKLGFKYA CSSGISFGMD DMVVPKSKIV HIDETQLEIK
     EFEQQYSNGL ITYGEKYNKV IDAWSRCTDR VANDMMKEIA KPPVSDDSNQ QKINSIYMMA
     ISGARGSFQQ IKQLGGMRGL MTKSNGQIIP TPIIANFKEG LTVFECFNSA NGMRKGQIDT
     ALKTASSGYL TRKLVDVAQD CIITEKDCNT DKGIEVKSII EGGEVIVPLA EMILGRTAAI
     NIYHPVTNDL ILTKGELINE SKLEQIESAG LDRIMIKSVL TCESSTGICA ICYGRDLATG
     SLVSEGEAIG VIAAQSIGEP GTQLTMRTFH IGGAATKGAE VSSVEASYDA KVKILSRNVV
     INSEERKIVM SRNCELLLLD NNGNEKAHSK IPYGARLLVD EGDMVTKTQK LAEWDPYTIP
     IITEKSGKVL FKDMVEGISV RDVTDEATGI PSKVIIESKQ YSRGAELRPR IQLLDAKGEI
     IMLSNGLEAR YYLPVGAVLS VEDGVQISVG DIIARIPKES TTTKDITGGL PRVAELFEAR
     RPKDHAVIAE IDGRVEFGKD YKSKRRIIIH PVDGSMGLEY MVPKGKHVVV NEGDFVKKGD
     LLIDGNPVLQ DILKVMGVEL LASYIVKEVQ AVYRLQGVKI DDKHIEVIIR QMLQKVEITD
     SGGTTLLVGE KIDRREFDEI NEKAIKNGLR PADAQLILQG ITKSSLQTRS FISAASFQET
     TRVLTEAAIA GKVDKLRGLK ENVIVGRLVP AGTGFLYGQN A