RPOC_CORDI
ID RPOC_CORDI Reviewed; 1336 AA.
AC Q6NJF6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=DIP0447;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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; BX248355; CAE48952.1; -; Genomic_DNA.
DR RefSeq; WP_010934310.1; NC_002935.2.
DR AlphaFoldDB; Q6NJF6; -.
DR SMR; Q6NJF6; -.
DR STRING; 257309.DIP0447; -.
DR PRIDE; Q6NJF6; -.
DR EnsemblBacteria; CAE48952; CAE48952; DIP0447.
DR KEGG; cdi:DIP0447; -.
DR HOGENOM; CLU_000524_3_0_11; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000002198; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1336
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067735"
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 902
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 991
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 994
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1336 AA; 147984 MW; 9C219FE19670866A CRC64;
MIDVNFFDEL RIGLATADDI RRWSKGEVKK PETINYRTLK PEKDGLFCER IFGPTRDWEC
ACGKYKRVRY KGIICERCGV EVTKSKVRRE RMGHIELAAP VTHIWYFKGV PSRLGYLLDL
APKDLERIIY FAANIITSVD DEARHADQTT LEAEMLLEKK DVEADMESEI AERAAKLEED
LAELEAAGAK ADARNKVKKA AEKEMQHIRE RAEREIDRLE EIWQTFIKLA PKQMIIDETI
YEELVDRYED YFTGGMGAEA IQTLIRNFDL DSEAEELREI INNGKGQKKM RALKRLKVVA
AFQRSGNDPA GMVLDCIPVI PPELRPMVQL DGGRFATSDL NDLYRRVINR NNRLKRMIEL
GAPEIIVNNE KRMLQESVDA LFDNGRRGRP VTGPGNRPLK SLSDLLKGKQ GRFRQNLLGK
RVDYSGRSVI IVGPQLKLHE CGLPKLMALE LFKPFVMKRL VENDYAQNIK SAKRMVERQR
PEVWDVLEEA ISEHPVMLNR APTLHRLGIQ AFEPKLVEGK AIQLHPLACE AFNADFDGDQ
MAVHLPLSAE AQAEARILML ASNNILSPAS GKPLAMPRLD MVTGLYYLTM DKNENEIGGQ
GAYASATEEG PAQGVYSSYA EAIMARDRGV LGLQAKIKVR ISHLRPPVDI EAEQFPEGWN
KGDVWLADTT LGRIMFNELL PWNYPYLEGV MVRKGGGTGK IMLGDVINDL AATYPMITVA
QTMDKMKDAG FYWATRSGVT ITMSDVLVLP NKEEILDRYE AEARKIERKY WEQGALTERE
RYDRLVELWK DATDEVGNAV EKLYPDDNPI PMIVKSGAAG NMRQIWTLAG MKGMVVNSKG
DYITRPIKTS FREGLSVLEY FNNSHGSRKG LADTALRTAD SGYLTRRLVD VAQDVIVRED
DCGTKQGIRV PVAVEVKDAE GNVTGYTGHS LIETSVAGRV AATAVKDAEG NVMVEPGENL
TDQLIDELIA AGVKEVKVRS VLTCQTPTGV CAKCYGKSMA TGKLVDIGEA VGIVAAQSIG
EPGTQLTMRT FHQGGVGGDI TGGLPRVQEL FEARVPKNRA PIASVAGTVH LDDEGNFYTL
TINPDDGSDV VVYEKLSKRQ GLATVRVPME SNPGAMIERT LAEGDHVEVG DRLLRGPADP
HDVLEVLGRR GVEQHLVDEV QDVYRAQGVA IHDKHIEIII RQMLRRGTVI ESGSTEFLPG
TLVDLSEAKA ANAEALANGG QPAELRSEIM GITKASLATE SWLSAASFQE TTRVLTDAAI
NKRSDKLIGL KENVIIGKLI PAGTGISRYR NISVKPTEAA RNAAYSIPTY GDSIYGDDGY
GEFTGASVPL DEAYDL
