RPOC_WEIPA
ID RPOC_WEIPA Reviewed; 1054 AA.
AC P96178;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Weissella paramesenteroides (Leuconostoc paramesenteroides).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Weissella.
OX NCBI_TaxID=1249;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33313 / DSM 20288 / JCM 9890 / CCUG 30068 / LMG 9852 / NBRC
RC 109620 / NCDO 803 / NCIMB 13092 / NRRL B-3471 / R80;
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+) ion1 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, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X95813; CAA65080.1; -; Genomic_DNA.
DR AlphaFoldDB; P96178; -.
DR SMR; P96178; -.
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; 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; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN <1..>1054
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067832"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 387
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 752
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 826
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 833
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 836
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 1054
SQ SEQUENCE 1054 AA; 118067 MW; 1B3E81C060154EEA CRC64;
RIRYKGIVCD RCGVEVTSAK VRRERMGHIE LAAPVSHIWY FKGIPSRMGL VLDMSPRSLE
EIIYFASYVV TKGGDTPLTE KQLLSEREYR ELKAEYGNAF EAGMGAEAVQ TLLANVDLEE
EVTELKAELR EATGQKRVRA VRRLDIIEAF VKSGNKPEWM VMDVIPIIPP DLRPMVQLEG
GRFATSDLND LYRRVINRNN RLKRLLELNA PGIIVQNEKR MLQEAADALV DNGRRGRPVT
GPGNRPLKSL SHMLKGKQGR FRQNLLGKRV DYSGRSVIDV GPFLKMNQMG LPRQMAMELF
RPFIMKELVK RDLAGNIRAA KRKIDRRDDD VMDVLEDVIK EHPVLLNRAP TLHRLGIQAF
EPVLVSGKAM RLHPLVTEAY NADFDGDQMA IHVPLSDEAQ AEARLLMLAA GHILAPKDGK
PIVAPSQDMV IGNYYLTTEE AGREGEGMIF KDVNEVRTAY QNKYVHLHTR IGIQTSSLPA
AKPFTAEQRS RIMLTSVGKL FFNDILPEDF PFLNEPTEAN LHEIDNRFFL EPGEDIKAHY
AETPILPPFK KGYLSDIIAE VYKIYKVTET SLLLDRMKDL GYDESTKSGL TVGVSDVTDL
KEKPEIIADA HKQVATVTKQ FRRGLITDSE RYERVIAIWN KAKDDITEKL IEHFEPDNNI
FMMSDSGARG NISNFTQLAG MRGLMAAPNG RIMELPIIAN FREGLSVLEM FFSTHGARKG
MTDTALKTAD SGYMTRRLVD VAQDVIIREL DCHSDRGLDV TAIMNGNEVI EPLYERILGR
YAQKSVFDPE TGETLVNHNE MITEDIAKRI IEAGITTVTI RSAFTCNTEH GVCVRCYGRN
MATGDVVEVG EAVGTVAAQS IGEPGTQLTM RTFHTGGVAG NDITQGLPRV QEIFEARNPK
GRAMITEVTG EVTSIEENPA DRTKEVTIQG ETDTRTYTLP MTARMRVGEG DRIHRGETLN
EGSADPKEII QVRDTLATEN YIVHEVQKVY RMQGVEISDK HIEVMARQML RKVRVMDPGE
TDLLPGTLMD IAQFRDANED TLLKGGLPAT GRPV
