RPOC_CORU7
ID RPOC_CORU7 Reviewed; 1323 AA.
AC B1VES2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=cu0301;
OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=504474;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43042 / DSM 7109;
RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA Puehler A.;
RT "The lifestyle of Corynebacterium urealyticum derived from its complete
RT genome sequence established by pyrosequencing.";
RL J. Biotechnol. 136:11-21(2008).
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; AM942444; CAQ04261.1; -; Genomic_DNA.
DR RefSeq; WP_012359562.1; NC_010545.1.
DR AlphaFoldDB; B1VES2; -.
DR SMR; B1VES2; -.
DR STRING; 504474.cu0301; -.
DR PRIDE; B1VES2; -.
DR EnsemblBacteria; CAQ04261; CAQ04261; cu0301.
DR GeneID; 60605104; -.
DR KEGG; cur:cu0301; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_11; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001727; 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; 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; 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..1323
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141766"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 537
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 977
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 984
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 987
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1323 AA; 146472 MW; 9808A71EBF88B573 CRC64;
MLDVNFFDEL RIGLATADDI RRWSRGEVKK PETINYRTLK PEKDGLFCER IFGPTRDWEC
SCGKYKRVRY KGIICERCGV EVTKSKVRRE RMGHIELAAP VTHIWYFKGV PSRLGYLLDL
APKDLEKIIY FAANIITSVD EDARHSDQTT LEAEMLLEKK EVEQDRDADL ADRAKTLEED
LAELEAAGAK ADAKKKVQNA ADREMRHIRE RAEREVERLD EIWNTFVKLA PKQMIADETL
YEELLDRYED YFTGGMGAEA IQTLIRNFDL EAEAESLREV IRDGKGQRKL RALKRLKVVA
AFLRSGNDPA GMVLDCIPVI PPELRPMVQL DGGRFATSDL NDLYRRVINR NNRLKRMLDL
GAPEIIVNNE KRMLQESVDA LFDNGRRGRP VTGPGNRPLK SLSDLLKGKQ GRFRQNLLGK
RVDYSGRSVI IVGPQLKLHQ CGLPKLMALE LFKPFVMKRL VEKSYAQNIK SAKRMVERQR
PEVWDVLEEA IAEHPVMLNR APTLHRLGIQ AFEPVLIEGK AIQLHPLACE AFNADFDGDQ
MAVHLPLSDE AQAEARILML ASNNILSPAS GKPLAMPRLD MVTGLYYLTL IKGKEEFGGQ
GAFTEATEQG PATGVYTSLA EAIMAYDRGV LGLQAPIHVR IDHLRPPAEV EAEQFPDGWQ
KGQTWTAETT LGRVQFNELL PWNYPYVEGV MDKKNQAVVI NDLAAKYPMI TVAQTVDKLK
DAGFYWATRS GVTITMHDVL VLPNKQEILD EYEAKAQRIE KKLARGKINE SERYQSLVDL
WKEATDFVGE SVEKLYPDDN PIPMIVKSGA AGNMRQIWTL AGMKGMVTNS RGDYITRPVK
TSFREGLSVL EYFNNSHGSR KGLADTALRT ADSGYLTRRL VDVAQDVIVR EDDCGTKQGV
VLDVCTPVLD ANGEKTGEFA RADFVETSVL GRFLAADAIG ANGEVVCEAG TVIGELELAE
LVKAGVETIK ARSVMTCGTA TGVCSTCYGK SMATGKKVEI GEAVGIVAAQ SIGEPGTQLT
MRTFHLGGVG GDITGGLPRV QELFEARVPK AKSPIASVDG KIKIEDDDAF FTLTIIPDDG
SEEVVYEKLS KRQGLATLGT GGVERPLRDG DHVKMGQQLL KGAADPHEVL RVMGRRGVQQ
HLINEVQKVY RDQGVAIHDK HIEIIVRQML RRVTVIDSGS TEYLPGSLVD HSDAVAASKE
AVKTGGRPVE VRAEIMGITK ASLATESWLS AASFQETTRV LTDAAINKRS DKLIGLKENV
IIGKLIPAGT GIARYRNIQV QPTEEARAAA FTLPSTFGDG FYGDEGYGEF TGASVPLDDL
GLH
