RPOY_GEOS3
ID RPOY_GEOS3 Reviewed; 71 AA.
AC A0A0K2H5X8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=DNA-directed RNA polymerase subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01553, ECO:0000303|PubMed:25092033};
DE Short=RNAP epsilon subunit {ECO:0000255|HAMAP-Rule:MF_01553};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01553};
DE AltName: Full=RNA polymerase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_01553};
DE AltName: Full=Transcriptase subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01553};
GN Name=rpoY {ECO:0000255|HAMAP-Rule:MF_01553, ECO:0000303|PubMed:25092033};
GN ORFNames=GT50_03365;
OS Geobacillus stearothermophilus (strain DSM 13240 / CIP 106956 / 10).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=272567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13240 / CIP 106956 / 10;
RA Lewis S.A., Clifton S.W., Najar F.Z., Roe B.A.;
RT "Complete genome Sequence of Geobacillus stearothermophilus strain 10, a
RT Yellowstone hot spring isolate.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-58, AND SUBUNIT.
RX PubMed=25092033; DOI=10.1128/jb.02020-14;
RA Keller A.N., Yang X., Wiedermannova J., Delumeau O., Krasny L., Lewis P.J.;
RT "epsilon, a new subunit of RNA polymerase found in gram-positive
RT bacteria.";
RL J. Bacteriol. 196:3622-3632(2014).
CC -!- FUNCTION: A non-essential component of RNA polymerase (RNAP)
CC (Probable). Has a similar structure to bacteriophage T7 protein Gp2 (AC
CC P03704), which is known to bind to RNAP in the DNA binding-cleft.
CC Unlike Gp2 however, this protein does not inhibit transcription
CC inititation (PubMed:25092033). {ECO:0000269|PubMed:25092033,
CC ECO:0000305}.
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_01553};
CC -!- SUBUNIT: Monomer (PubMed:25092033). RNAP is composed of a core of 2
CC alpha, a beta and a beta' subunit. The core is associated with a delta
CC subunit, and at least one of epsilon or omega. When a sigma factor is
CC associated with the core the holoenzyme is formed, which can initiate
CC transcription (By similarity). {ECO:0000250|UniProtKB:O31718,
CC ECO:0000269|PubMed:25092033}.
CC -!- SIMILARITY: Belongs to the RNA polymerase subunit epsilon family.
CC {ECO:0000255|HAMAP-Rule:MF_01553}.
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DR EMBL; CP008934; ALA69333.1; -; Genomic_DNA.
DR RefSeq; WP_013145900.1; NZ_CP008934.1.
DR PDB; 4NJC; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-58.
DR PDBsum; 4NJC; -.
DR AlphaFoldDB; A0A0K2H5X8; -.
DR SMR; A0A0K2H5X8; -.
DR EnsemblBacteria; ALA69333; ALA69333; GT50_03365.
DR KEGG; gse:GT50_03365; -.
DR PATRIC; fig|272567.8.peg.680; -.
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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01553; RNApol_bact_RpoY; 1.
DR InterPro; IPR009907; RpoY.
DR Pfam; PF07288; RpoY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Transcription; Transferase.
FT CHAIN 1..71
FT /note="DNA-directed RNA polymerase subunit epsilon"
FT /id="PRO_0000451559"
FT STRAND 1..9
FT /evidence="ECO:0007829|PDB:4NJC"
FT STRAND 20..29
FT /evidence="ECO:0007829|PDB:4NJC"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:4NJC"
FT STRAND 40..50
FT /evidence="ECO:0007829|PDB:4NJC"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:4NJC"
SQ SEQUENCE 71 AA; 8444 MW; BCA811D6D703E51D CRC64;
MIFKVFYQEN ADEVPVREKT KTLYIEAESE RDVRRKLEGR PINIEYIQPL EGAHLEYEKK
SPNFQVLEIS S