RPOC_STRPY
ID RPOC_STRPY Reviewed; 989 AA.
AC P0C0D9; P95816;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000305};
DE Short=RNAP subunit beta';
DE EC=2.7.7.6;
DE AltName: Full=RNA polymerase subunit beta';
DE AltName: Full=Transcriptase subunit beta';
DE Flags: Fragment;
GN Name=rpoC;
OS Streptococcus pyogenes.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 923;
RX PubMed=8863429; DOI=10.1099/00207713-46-4-1004;
RA Morse R., Collins M.D., O'Hanlon K., Wallbanks S., Richardson P.T.;
RT "Analysis of the beta' subunit of DNA-dependent RNA polymerase does not
RT support the hypothesis inferred from 16S rRNA analysis that Oenococcus oeni
RT (formerly Leuconostoc oenos) is a tachytelic (fast-evolving) bacterium.";
RL Int. J. Syst. Bacteriol. 46:1004-1009(1996).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000250}.
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:0000250|UniProtKB:P0A8T7};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; X96385; CAA65249.1; -; Genomic_DNA.
DR AlphaFoldDB; P0C0D9; -.
DR SMR; P0C0D9; -.
DR PRIDE; P0C0D9; -.
DR eggNOG; COG0086; Bacteria.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 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; Metal-binding; Nucleotidyltransferase;
KW Transcription; Transferase; Zinc.
FT CHAIN <1..>989
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067810"
FT BINDING 752
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 826
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 833
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 836
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT NON_TER 1
FT NON_TER 989
SQ SEQUENCE 989 AA; 110463 MW; DD1E7EC1684E610B CRC64;
RIRYKGIVCD RCGVEVTRAK VRRERMGHIE LKAPVSHIWY FKGIPSRMGL TLDMSPRALE
EVIYFAAYVV IDPKDTPLEP KSLLTEREYR EKLQEYGHGS FVAKMGAEAI QDLLKRVDLA
AEIAELKEEL KSASGQKRIK AVRRLDVLDA FNKSGNKPEW MVLNILPVIP PDLRPMVQLD
GGRFAASDLN DLYRRVINRN NRLARLLELN APGIIVQNEK RMLQEAVDAL IDNGRRGRPI
TGPGSRPLKS LSHMLKGKQG RFRQNLLGKR VDFSGRSVIA VGPTLKMYQC GVPREMAIEL
FKPFVMREIV AKEYAGNVKA AKRMVERGDE RIWDILEEVI KEHPVLLNRA PTLHRLGIQA
FEPVLIDGNL LRLHPLVCEA GNADFDGQMA IHVPLSEEAQ AEARLLMLAA EHILNPKDGK
PVVTPSQDMV LGNYYLTMED AGREGEGMIF KDKDEAVMAY RNGYAHLHSR VGIAVDSMPN
KPWKDSQRHK IMVTTVGKIL FNDIMPEDLP YLQEPNNANL TEGTPDKYFL EPGQDIQEVI
DGLDINVPFK KKNLGNIIAE TFKRFRTTET SAFLDRLKDL GYYHSTLAGL TVGIADIPVI
DNKAEIIDAA HHRVEEINKA FRRGLMTDDD RYVAVTTTWR EAKEALEKRL IETQDPKNPF
VMMMDSGARG NISNFSQLAG MRGLMAAPNG RIMELPILSN FREGLSVLEM FFSTHSARKG
MTDTALKTAD SGYLTRRLVD VAQDVIIRED DCGTDRGLLI RAITDGKEVT ETLEVRLQGR
YTRKSVKHPE TGEVLIGADQ LITEDMARKI VDAGVEEVTI RSVFTCATRH GVCRHCYGIN
LATGDAVEVG EAVGTIAAQS IGEPGTQLTM RTFHTGGVAS NTDITQGLPR IQEIFEARNP
KGEAVITEVK GNVVEIEEDA STRTKKVYVQ GKTGMGEYVV PFTARMKVEV GDEVNRGAAL
TEGSIQPKRL LEVRDTLSVE TYLLAEVQK
