RPOC_RICB8
ID RPOC_RICB8 Reviewed; 1372 AA.
AC A8GV25;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 79.
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=A1I_01520;
OS Rickettsia bellii (strain OSU 85-389).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=391896;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSU 85-389;
RA Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.;
RT "Complete genome sequencing of Rickettsia bellii.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABV78696.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000849; ABV78696.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041808483.1; NC_009883.1.
DR AlphaFoldDB; A8GV25; -.
DR SMR; A8GV25; -.
DR PRIDE; A8GV25; -.
DR KEGG; rbo:A1I_01520; -.
DR HOGENOM; CLU_000524_3_1_5; -.
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..1372
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353420"
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 1372 AA; 153319 MW; 34291FFC687EDC93 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 IPIIANFKEG LTVFECFNSA NGMRKGQIDT
ALKTASSGYL TRKLVDVAQD CIITEKDCNT DKGIEVKSII EGGEVIAPLA 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 YKSKRRIIIN PVDGSMGLEY MVPKGKHVVV NEGDFVKKGD
LLIDGNPVLQ DILKVMGVEL LASYIVKEVQ AVYRLQGVKI DDKHIEVIIR QMLQKVEITD
SGGTTLLVGE KIDRREFDEI NEKAIKNGLR PADAQLILQG ITKSSLQTRS FISAASFQET
TRVLTEAAIA GKVDKLRGLK ENVIVGRLVP AGTGFFMDKM RKVAAKLDEE NA
