RPOC_RICAH
ID RPOC_RICAH Reviewed; 1372 AA.
AC A8GMA8;
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=A1C_01015;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
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; CP000847; ABV74533.1; -; Genomic_DNA.
DR RefSeq; WP_012013403.1; NC_009881.1.
DR AlphaFoldDB; A8GMA8; -.
DR SMR; A8GMA8; -.
DR STRING; 293614.A1C_01015; -.
DR PRIDE; A8GMA8; -.
DR EnsemblBacteria; ABV74533; ABV74533; A1C_01015.
DR KEGG; rak:A1C_01015; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000006830; 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_0000353419"
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; 153257 MW; F7D23376CAF82D9A CRC64;
MSVVNFYGQL SNTQQFDQIR INIASPDQVR SWSFGEVTKP ETINYRTFKP EKDGLFCARI
FGPVKDYECL CGKYKRMKNR GITCEKCGVE VTVSRVRRER MGHIELAAPV AHIWFLKSLP
SRISTLLDMT MRDVEKILYF ENYVVIDPGL SILQKGELLT EEELQKAKDK YGEDAFTASI
GAEVIQQMLK ELDFAKLKHE LYEELQTTSS EVKKKKIVKR 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 YYLTLAFDNE VGEGMMFSDL AEMEHALYNK
FITIHTKIKY RRNQLNAEGK MVHVIIDTTY GRLMVGELLP SNPNIEFKFI NKQLTKKDIS
LVIDLVYRHC GQKATVIFAD QLMKLGFKYA CSSGISFGMD DMVVPESKST HINETQLEIK
EFEQQYSNGL ITYGEKYNKV VDAWSRCTDR VANDMMKEIA TPRVSDEPNH QKINAIYMMA
ISGARGSFQQ IKQLGGMRGL MTKSNGQIIQ TPIISNFKEG LTEFECFNSA NGMRKGQIDT
ALKTASSGYL TRKLVDVAQD CIITEKDCGT DKGIEVKSVI EGGEVIVPSS EKILGRTAAI
DIFHPVTNAL ILNKGELINE AKLEQIESAG LDRIMIKSVL TCESTTGICS ICYGRDLATG
TLVSEGEAIG VIAAQSIGEP GTQLTMRTFH IGGAATKGAE VSSVEASYGA KVKIISRNVV
INSEERKIVM SRNCELLLLD NNGNEKARHK IPYGARLLVD DGDMVVKTQK LAEWDPYTIP
IITEKSGKVL FKDMVEGISI RDVTDEATGI PSKVIIESKQ YSRGAELRPR IQLLDAEGAV
ITLSNGLEAR YYLPVGAVLS VEDGVQISVG DIIARIPKES TTTKDITGGL PRVAELVEAR
RPKDHAVIAE VDGRVEFGKD YKSKRRIIIH PIDETMSIEY MVPKGKHVVV NEGDFVKKGD
LLIDGNPVLQ DILKVMGVEV LANYIVKEVQ AVYRLQGVKI DDKHIEVIIR QMLQKVEITD
SGGTTLLAGE KIDRHEFEEI NKKAIKNGLK PAAAQLILQG ITKASLQTRS FISAASFQET
TRVLTEAAIA GKVDKLRGLK ENVIVGRLVP AGTGYFMDKM RKAAVKLDEE NI
