RPOC_CORGB
ID RPOC_CORGB Reviewed; 1333 AA.
AC A4QBG3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=cgR_0592;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
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; AP009044; BAF53560.1; -; Genomic_DNA.
DR RefSeq; WP_003854213.1; NC_009342.1.
DR AlphaFoldDB; A4QBG3; -.
DR SMR; A4QBG3; -.
DR PRIDE; A4QBG3; -.
DR EnsemblBacteria; BAF53560; BAF53560; cgR_0592.
DR GeneID; 58309599; -.
DR KEGG; cgt:cgR_0592; -.
DR HOGENOM; CLU_000524_3_1_11; -.
DR OMA; YRNIRVE; -.
DR PhylomeDB; A4QBG3; -.
DR Proteomes; UP000006698; 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; 1.
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; Transcription; Transferase; Zinc.
FT CHAIN 1..1333
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308830"
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 901
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 983
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 990
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 993
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1333 AA; 147309 MW; CC6FD6E7EAEB752D CRC64;
MLDVNVFDEL RIGLATADDI RRWSKGEVKK PETINYRTLK PEKDGLFCER IFGPTRDWEC
ACGKYKRVRY KGIICERCGV EVTKSKVRRE RMGHIELAAP VTHIWYFKGV PSRLGYLLDL
APKDLDLIIY FGANIITSVD EEARHSDQTT LEAEMLLEKK DVEADAESDI AERAEKLEED
LAELEAAGAK ADARRKVQAA ADKEMQHIRE RAQREIDRLD EVWQTFIKLA PKQMIRDEKL
YDELIDRYED YFTGGMGAES IEALIQNFDL DAEAEELRDI INNGKGQKKM RALKRLKVVA
AFQRSGNDPA GMVLNAIPVI PPELRPMVQL DGGRFATSDL NDLYRRVINR NNRLKRMIEL
GAPEIIVNNE KRMLQESVDA LFDNGRRGRP VTGPGNRPLK SLSDLLKGKQ GRFRQNLLGK
RVDYSGRSVI IVGPQLRLHE CGLPKLMALE LFKPFVMKRL VENEYAQNIK SAKRMVERQR
PEVWDVLEEA ISEHPVMLNR APTLHRLGIQ AFEPVLVEGK AIQLHPLACE AFNADFDGDQ
MAVHLPLSAE AQAEARVLML ASNNILSPAS GKPLAMPRLD MVTGLYYLTL EKSSEEFGGQ
GAYQPADENG PEKGVYSSLA EAIMAYDRGV LGLQAPVRIR LNHLRPPAEV EAEQFPDGWN
QGETWLAHTT LGRVMFNEIL PWNYPYLEGI MVRKGGGSDK IMLGDVVNDL AAKYPMITVA
QTMDKMKDAG FYWSTRSGVT IAMSDVLVLP NKEEMLDRYE ESARQIEVKY NRGKLTGRER
YDRLVELWKD ATDEVGQAVE DLYPDDNPIP MIVKSGAAGN MRQIWTLAGM KGMVVNSKGD
YITRPIKTSF REGLTVLEYF NNSHGSRKGL ADTALRTADS GYLTRRLVDV AQDVIVRVED
CGTRQGVRVP VAAEVLDATG AVTGYTRHDL IETSVSGRVL AGDATNAAGE VVLAAGTDLT
ELNIDLLVEA GIKDVKVRSV LTCQTPTGVC AKCYGKSMAS GQQVDIGEAV GIVAAQSIGE
PGTQLTMRTF HQGGVGGDIT GGLPRVQELF EARVPKNCAP IASVEGVIHL EDEGNFYTLT
IVPDDGSDNV VYEKLSKRQG LASTRVAMES NAGAFIERTL TEGDRVTVGQ RLLRGAADPH
DVLEILGRRG VEQHLIDEVQ AVYRAQGVAI HDKHIEIIIR QMLRRGTVIE SGSTEFLPGS
LVDLSEAKLA NSEAIGAGGQ PAELRSEIMG ITKASLATES WLSAASFQET TRVLTDAAIN
KRSDKLIGLK ENVIIGKLIP AGTGISRYRN ISIKPTEAAR NAAYSIPTYG ESIYGDDGFG
EFTGASVPLD EAF
