RPOY_STAAB
ID RPOY_STAAB Reviewed; 72 AA.
AC Q2YX59;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=DNA-directed RNA polymerase subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01553};
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}; OrderedLocusNames=SAB0956c;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
CC -!- FUNCTION: A non-essential component of RNA polymerase (RNAP).
CC {ECO:0000255|HAMAP-Rule:MF_01553}.
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: RNAP is composed of a core of 2 alpha, a beta and a beta'
CC subunit. The core is associated with a delta subunit, and at least one
CC of epsilon or omega. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01553}.
CC -!- SIMILARITY: Belongs to the RNA polymerase subunit epsilon family.
CC {ECO:0000255|HAMAP-Rule:MF_01553}.
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; AJ938182; CAI80644.1; -; Genomic_DNA.
DR RefSeq; WP_000257888.1; NC_007622.1.
DR AlphaFoldDB; Q2YX59; -.
DR SMR; Q2YX59; -.
DR GeneID; 66839285; -.
DR KEGG; sab:SAB0956c; -.
DR HOGENOM; CLU_187518_1_0_9; -.
DR OMA; TIYVEGE; -.
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 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT CHAIN 1..72
FT /note="DNA-directed RNA polymerase subunit epsilon"
FT /id="PRO_1000068878"
SQ SEQUENCE 72 AA; 8752 MW; CF72E1A6D2BAAB56 CRC64;
MAVFKVFYQH NRDEVIVREN TQSLYVEAQT EEQVRRYLKD RNFNIEFITK LEGAHLDYEK
ENSEHFNVEI AK