RPOC_GEODF
ID RPOC_GEODF Reviewed; 1377 AA.
AC B9M6V1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Geob_3631;
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32;
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 Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-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; CP001390; ACM21972.1; -; Genomic_DNA.
DR RefSeq; WP_012648699.1; NC_011979.1.
DR AlphaFoldDB; B9M6V1; -.
DR SMR; B9M6V1; -.
DR STRING; 316067.Geob_3631; -.
DR PRIDE; B9M6V1; -.
DR EnsemblBacteria; ACM21972; ACM21972; Geob_3631.
DR KEGG; geo:Geob_3631; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000007721; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1377
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000165842"
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 1377 AA; 153202 MW; F21741519188AA18 CRC64;
MEDIFNFFDK PKDPLHFSAI RISVSSPEKI RERSFGEVKK PETINYRTFK PERDGLFCAK
IFGPTKDYEC NCGKYKRMKH RGIVCEKCGV EVIPSKVRRE RLGHIDLATP VAHIWFLKSL
PSRIGNLMDI TLKDLEKVLY FEAYVVTDPK NTGMPFAQVF SEDQYLKAME EYNGQFEAGM
GAAAIRECLM SMDLDVLAEQ LRVEMLEATS EAKRKKTAKR LKVVEAFKSS GNKPEWMILE
CIPVLPPELR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLMELQAPEV IIRNEKRMLQ
EAVDALFDNG RRGRAIAGPN KRPLKSLSDM LKGKSGRFRQ NLLGKRVDYS GRSVIVVGPE
LRLHQCGLPK KMALELFKPF IYNKLEEKGF VTTIKSAKKM VEKERPEVWD VLEEVIKEHP
VMLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCTAFNAD FDGDQMAVHL PLSVESQVET
RVLMMSTNNI LSPAHGKPII VPSQDMVLGI YYMTREKFFA KGDGKIFASQ DEVRIALDAD
EVDLQARVKV RLKNLATDEK PQLVDTTPGR VVLREILPDE VPFATINKVM TKKELSNLVD
VCYRLAGNKE TVILADKLKS IGFRYSTIAG ISISINDMVI PEGKTAIINR ASEDVKEIQN
QYTEGLITDG ERYNKVIDIW AKSTEEIAKE MLDNLSRDIV HAPDGKEVKV PSFNAIHMMA
DSGARGSAQQ IRQLAGMRGL MAKPSGEIIE TPITANFREG LTVLQYFIST HGARKGLADT
ALKTANSGYL TRRLVDVAQD AIITEPDCGT LDGLVVSSLT EGGEIIEHIG DRILGRVALD
DILDPVTGDV LVASNEEIDE TLVQKIESAG LEKVKIRSVL TCQSRRGICA KCYGRDLARG
HLVNMGEAVG VIAAQSIGEP GTQLTMRTFH IGGTASRRAE QTSLEARTEG SVKFININYV
TNTDGHHIVM NRNGELAIVD ETGREREKYS ILYGAKIKVN VGQVIKQGEA IAEWDPYTMP
ILTEIAGKVK FGDIIEGVSM EEQVDEVTGL SRKVVVESRD ADKRPRITIK DEAGKTAKIN
ETTMGRYYLP VGANITVQED AVVNAGDVIA KIPRETTKTK DITGGLPRVA ELFEARKPKD
FAVITEIDGI VTFGKDAKGK RKVIVTPEMG EPKEYLIPKG KHISVHEGDH VRAGEALMDG
SSNPHDILRV LGQKELAKYL VDEVQEVYRL QGVKINDKHI ETIVRQMLRR VRIKDVGDTT
LLIDDQLERY IFEDENERVL DKGGKPAIAE PLLLGITKAS LSTESFISAA SFQETTKVLT
QASIEGKIDG LRGLKENVIM GRLIPAGTGL ARYRNLKLVA EEPVVTPSEQ VEEVAAG
