RPOC_OENOE
ID RPOC_OENOE Reviewed; 1004 AA.
AC P95405;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
DE Flags: Fragment;
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322};
OS Oenococcus oeni (Leuconostoc oenos).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=1247;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23279 / DSM 20252 / BCRC 14062 / CIP 106144 / JCM 6125 / NBRC
RC 100497 / NCDO 1674 / NCIMB 11648 / NRRL B-3472;
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: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 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-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, ECO:0000305}.
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DR EMBL; X96384; CAA65248.1; -; Genomic_DNA.
DR AlphaFoldDB; P95405; -.
DR SMR; P95405; -.
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 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; 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; 1.
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; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN <1..>1004
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067771"
FT BINDING 388
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 390
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 392
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 757
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 831
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 838
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 841
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT NON_TER 1
FT NON_TER 1004
SQ SEQUENCE 1004 AA; 111965 MW; 73750DF47F3A2C36 CRC64;
RIRYKGIVCD RCGVEVTSSK VRRERMGHIE LAAPVTHIWY FKGIPSRMGL ILDMSPRSLE
EIIYFASYVV INPGNTPLEK KQLITEAEYR QYQDQYGTDT FDAKMGAEAI KELLAEVDLE
KHAKELKNEL KDATGQKRTR AVRRLDIVEA FIQSGNKPEW MVMDVVPVIP PDLRPMVQLE
GGRFATSDLN DLYRRVINRN NRLKRLLDLN APGIIVQNEK RMLQEAVDAL IDNGRRGRPV
SGPGNRPLKS LSHLLKGKQG RFRQNLLGKR VDYSGRSVID VGPFLKMNQM GLPRQMAVEL
FKPFIYNRLI ELGTENGGAN NLRSARRLVE RHEDVVQDVL EEVVKEHPVL LNRAPTLHRL
GIQAFEPVLV SGKAMRLHPL VTTAYNADFD GDQMAIHVPL SDEAQAEARL LMLAASHILA
PKDGKPIVAP SQDMTIGNYY LTTEEAGIKG EGMIFSSADE VKMALQNHEV ELHTRIGIAA
SSFDKAKPFT DHQRARIMVT TVGKVIFNEI LPDDFPYINE PKSENFNGID GRFFLDPGTD
IVGWFKNESL NGPFKSGFLS DIIAQIYARY QVTRTSVLLD DMKDLGYNIS TRSGLTVRMS
DVTELPEKGE VLKEAHEKVA KITKQFRRGL LTDDERYIQV TQTWSDAQDK IKSMLIASFD
SKNPIFMMSD SGARGNISNS FQLAGMRGLM AAPNGKVIEL PVTANFREGL CVLEMFISTH
GARKGMTDTA LKTANSGYLT RRLVDVAQEV IVREEDCGTD RGLDVSAIMD GNEVIEPLYD
RILGRYAMKP VIDPKTGEVI AKKNQMIDEH VADQIIDAGI QTVTIRSIFT CRTEHGVCVK
CYGRNMATGD IVEVGEAVGT VAAQSIGEPG TQLTMRTFHT GGVALSEDIT QGLPRVQEIF
EARNPKGRAE ISEVTGKVTS IEENPADRTK TVTIEGETDT REYVLPISAR LRVAEGDEIH
RSEAINEGPL DPKELIKVSS TLKTENYMLA EVRKVYRMQG VGIA
