RPOC1_RIPO1
ID RPOC1_RIPO1 Reviewed; 625 AA.
AC B7JWQ8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=DNA-directed RNA polymerase subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
DE Short=RNAP subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=RNA polymerase subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=Transcriptase subunit gamma {ECO:0000255|HAMAP-Rule:MF_01323};
GN Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323};
GN OrderedLocusNames=PCC8801_0616;
OS Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX NCBI_TaxID=41431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 8801;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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_01323}.
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_01323};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC -!- SUBUNIT: In cyanobacteria the RNAP catalytic core is composed of 2
CC alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC factor is associated with the core the holoenzyme is formed, which can
CC initiate transcription. {ECO:0000255|HAMAP-Rule:MF_01323}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
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DR EMBL; CP001287; ACK64704.1; -; Genomic_DNA.
DR RefSeq; WP_012593981.1; NC_011726.1.
DR AlphaFoldDB; B7JWQ8; -.
DR SMR; B7JWQ8; -.
DR STRING; 41431.PCC8801_0616; -.
DR EnsemblBacteria; ACK64704; ACK64704; PCC8801_0616.
DR KEGG; cyp:PCC8801_0616; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_030022_2_0_3; -.
DR OMA; WGERTLP; -.
DR OrthoDB; 105573at2; -.
DR Proteomes; UP000008204; 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; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR InterPro; IPR012755; DNA-dir_RpoC1_gamma.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR034678; RNApol_RpoC1.
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 SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02387; rpoC1_cyan; 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..625
FT /note="DNA-directed RNA polymerase subunit gamma"
FT /id="PRO_1000141804"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ SEQUENCE 625 AA; 71113 MW; 3AE733D82BC652FF CRC64;
MKAQADSRFD YVKINLASPE RIRQWGERSL PNGVVVGEVT KPETINYRTL KPEMDGLFCE
RIFGPSKDWE CWCGKYKRVR HRGIVCERCG VEVTESRVRR HRMGFIKLAA PVTHVWYLKG
IPSYLSILLD MALRDVEQIV YFNSYVVLDP GNASNLSYKQ LLTEDQWIEI EEQIYAEDSE
LYGIEVGIGA EAIQRLLQEI NLEEVAEKLR EEILESKGQK RAKLIKRLRV IDNFVATNSR
PDWMVLSVIP VIPPDLRPMV QLDGGRFATS DLNDLYRRVI NRNNRLSRLQ EILAPEIIVR
NEKRMLQEAV DALIDNGRRG RTVVGANNRA LKSLSDIIEG KQGRFRQNLL GKRVDYSGRS
VIVVGPKLKI YQCGLPREMA IELFQPFVIH RLIRLGLVNN IKAAKKLIMR EDPSVWTVLE
EVITGHPVLL NRAPTLHRLG IQAFEPILVE GRAIQLHPLV CPAFNADFDG DQMAVHVPLS
LEAQSEARLL MLACHNILSP ATGKPIVAPS QDMVLGCYYL TAENPKAQKG ANRYFGSIPD
AIKAYEQGTV DLHAYVWLRY NGDVVTHKPD TEVLKTETLD DGSVIKHYRE RRVREKDGEV
ISQFIRTTPG RIIYNKTIED ALVAL
