RPOC_GEOSM
ID RPOC_GEOSM Reviewed; 1382 AA.
AC C6E4R3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=GM21_3334;
OS Geobacter sp. (strain M21).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter; unclassified Geobacter.
OX NCBI_TaxID=443144;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-2009) 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; CP001661; ACT19359.1; -; Genomic_DNA.
DR RefSeq; WP_015838553.1; NC_012918.1.
DR AlphaFoldDB; C6E4R3; -.
DR SMR; C6E4R3; -.
DR STRING; 443144.GM21_3334; -.
DR EnsemblBacteria; ACT19359; ACT19359; GM21_3334.
DR KEGG; gem:GM21_3334; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
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..1382
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000214494"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
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 1382 AA; 153915 MW; 7A6B624944A70943 CRC64;
MEDIFNFFDK PKDPLHFSSI KISISSPDKI RERSFGEVKK PETINYRTFK PERDGLFCAK
IFGPTKDYEC NCGKYKRMKH RGIVCEKCGV EVIPSKVRRE RLGHIDLATP VAHIWFLKSL
PSRIGNLMDI TLKDLEKVLY FEAYVVTDPK ETGLAFGTVF SEDQYQKALE EYSYGFEAGM
GAAAIRTCLT SMDLDQLSEQ LRIEMQEATS EAKRKKTAKR LKVMEAFKNS GNKPEWMILE
CIPVLPPELR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLMELQAPEV IIRNEKRMLQ
EAVDALFDNG RRGRAIAGPN KRPLKSLSDM LKGKSGRFRQ NLLGKRVDYS GRSVIVVGPE
LRLHQCGLPK KMALELFKPF IYNKLEERGF VTTIKSAKKM VEKEKPEVWD VLEEVIKEHP
VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCTAFNAD FDGDQMAVHL PLSVESQVEA
RVLMMSTNNI LSPAHGKPII VPSQDMVLGI YYMTREKHFA LGEGKIFASA DEVNIAWDAG
EIHLQARIKV RMKNLVSDEK PTLIETTTGR VLLRDILPDA VPYATINKVM TKKELSNLVD
VCYRLAGNKE TVILADKLKA IGFRYAAKAG ISISINDMVI PEGKPAIITR ATEEVQEIQN
QYTEGLITDG ERYNKVIDIW AKSTEDIAKE MLDNLSRDTI LDPEGKEVKV PSFNAIHMMA
DSGARGSAQQ IRQLAGMRGL MAKPSGEIIE TPITANFREG LTVLQYFIST HGARKGLADT
ALKTANSGYL TRRLVDVAQD AIITEADCGT IDGLTVSSLT EGGEVIEHIG DRILGRVALD
DILDPVTGDV LVPANEEIDE NLVARIEAAG LEKVKIRSVL TCESRRGICA KCYGRDLARG
HLVNRGEAVG VIAAQSIGEP GTQLTMRTFH IGGTASRRAE QTALEARNEG FAKFININYV
TNSEGHHIVM NRNGELAIVD ETGREREKYG VVYGAKIKVS PQEKVTQGQS VAEWDPYTMP
ILTEIAGRVK FGDVIEGVTM EEQVDEVTGL SRKVIIETRD ADKRPRITIK DESGKTAKIG
DSLLARYYLP VGSNINVLED TEVNAGDVIA KIPRETTKTK DITGGLPRVA ELFEARKPKD
FAVITEIDGV VAFGKDAKGK RKVLVTPELG EPKEYLIPKG KHISVHEGDH VRAGEALMDG
SSNPHDILRV LGQKELAKYL VDEVQEVYRL QGVKINDKHI ETIVRQMLRR VRVKDVGDTN
LLIDDQIERW VFEEENEKAM DKGGRPATAE SLLLGITKAS LSTESFISAA SFQETTKVLT
QASIEGKIDS LRGLKENVIM GRLIPAGTGL ALYRNLRMVA EEPVIIPEPV EPEDEEIYEE
EA
