RPOC_RICRS
ID RPOC_RICRS Reviewed; 1372 AA.
AC A8GQW5;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=A1G_01040;
OS Rickettsia rickettsii (strain Sheila Smith).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=392021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheila Smith;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia rickettsii.";
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}.
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DR EMBL; CP000848; ABV75790.1; -; Genomic_DNA.
DR RefSeq; WP_012150398.1; NC_009882.1.
DR AlphaFoldDB; A8GQW5; -.
DR SMR; A8GQW5; -.
DR EnsemblBacteria; ABV75790; ABV75790; A1G_01040.
DR GeneID; 45538778; -.
DR KEGG; rri:A1G_01040; -.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000006832; 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..1372
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353424"
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; 153275 MW; 126E945D7D724AB0 CRC64;
MSVVNFYGQL SNTQQFDQIR INIASPDQVR SWSFGEVTKP ETINYRTFKP EKDGLFCARI
FGPVKDYECL CGKYKRMKNR GITCEKCGVE VTVSRVRRER MGHIELAAPV AHIWFLKSLP
SRISTLLDMT MRDVEKILYF ENYVVVDPGL SILQKGELLT EEELQKAKDK YGEDAFTASI
GAEVIQQMLK ELDFSKLKQE LYEELQTTSS EVKKKKLVKR LKLVENFLES ENKPEWMIMD
VLPVIPPEIR PLVMLDGGRF ATSDLNELYR RVINRNNRLK KLIESKAPDI IVRNEKRMLQ
EAVDALFDNG RRGRAAKNAN KRPFKSLSDM LKGKQGRFRQ NLLGKRVDYS GRSVIVVGPE
LKLHQCGLPK KMALELFKPF IYSKLELYGI ATTIKAAKRM VEAEKSEVWD VLEEVIREHP
VLLNRAPTLH RLGIQAFEPL LIEGKAIQLH PLVCAAFNAD FDGDQMAVHI PLSIEAQLEA
RVFMMSTNNI LSPANGRPII VPDKDIVLGL YYLTLAFDNE VGAGMMFSDL AEMEHALYNK
FITIHTKIKY RRNQLNAEGK MVPVIIDTTY GRLMVGELLP SNPNIEFKFI NKQLTKKDIS
LVIDLVYRHC GQKATVIFAD QLMKLGFKYA CSSGISFGMD DMVVPESKST HINKTQLEIK
EFEQQYSNGL ITYGEKYNKV VDAWSRCTDR VANDMMKEIA TLPVNDAPNH QKINAIYMMA
ISGARGSFQQ IKQLGGMRGL MTKSNGQIIQ TPIISNFKEG LTEFECFNSA NGMRKGQIDT
ALKTASSGYL TRKLVDVAQD CIITEKDCGT DKGIEVKSVI EGGEVIVPLA EKILGRTAAI
DIFHPVTNDL ILNKGELINE AKLEQIESAG LDRIMIKSVL TCESTTGICS ICYGRDLATG
TLVSEGEAIG VIAAQSIGEP GTQLTMRTFH IGGAATKGAE VSSVDASYDA KVKIISRNVV
INSEERKIVM SRNCELLLLD NHGNEKARHK IPYGARLLVD DGDMVIKTQK LAEWDPYTIP
IITEKSGKVL FKDMVEGISI RDVTDEATGI PSKVIIESKQ YSRGAELRPR IQLLDAKGEV
ITLSNGLEAR YYLPVGAVLS VEDGVQISVG DIIARIPKES TTTKDITGGL PRVAELVEAR
RPKDHAVIAE IDGRVEFGKD YKSKRRIIIH PIDETMSIEY MVPKGKHVVV NEGDFVKKGD
LLIDGNPVLQ DILKVMGVEV LANYIVNEVQ AVYRLQGVKI DDKHIEVIIR QMLQKVEVTD
SGGTTLLAGE KIDRHEFDEI NEKAIKNGLK PAEAQLILQG ITKASLQTRS FISAASFQET
TRVLTEAAIA GKVDKLRGLK ENVIVGRLVP AGTGYFMDKM RKAAVKLDEE NV
