ID A0A1Y4G833_9ACTN Unreviewed; 86 AA.
AC A0A1Y4G833;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA-directed RNA polymerase subunit omega {ECO:0000256|ARBA:ARBA00013725};
DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418};
DE AltName: Full=Transcriptase subunit omega {ECO:0000256|ARBA:ARBA00029924};
GN ORFNames=DMP12_13750 {ECO:0000313|EMBL:ROT88022.1}, GKG38_11510
GN {ECO:0000313|EMBL:MSA95668.1}, GO738_12030
GN {ECO:0000313|EMBL:MVN16056.1};
OS Gordonibacter urolithinfaciens.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=1335613 {ECO:0000313|EMBL:MVN16056.1, ECO:0000313|Proteomes:UP000468327};
RN [1] {ECO:0000313|Proteomes:UP000285258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27213 {ECO:0000313|Proteomes:UP000285258};
RA Danylec N., Stoll D.A., Doetsch A., Huch M.;
RT "Genome Sequencing of selected type strains of the family
RT Eggerthellaceae.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT88022.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 27213 {ECO:0000313|EMBL:ROT88022.1};
RX PubMed=31210629; DOI=.1099/ijsem.0.003537;
RA Danylec N., Stoll D.A., Huch M.;
RT "Gordonibacter faecihominis is a later heterotypic synonym of Gordonibacter
RT urolithinfaciens.";
RL Int. J. Syst. Evol. Microbiol. 69:2527-2532(2019).
RN [3] {ECO:0000313|EMBL:ROT88022.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 27213 {ECO:0000313|EMBL:ROT88022.1};
RX PubMed=30643901;
RA Danylec N., Stoll D.A., Dotsch A., Huch M.;
RT "Draft Genome Sequences of Type Strains of Gordonibacter faecihominis,
RT Paraeggerthella hongkongensis, Parvibacter caecicola,Slackia equolifaciens,
RT Slackia faecicanis, and Slackia isoflavoniconvertens.";
RL Microbiol. Resour. Announc. 8:e01532-18(2019).
RN [4] {ECO:0000313|EMBL:MSA95668.1, ECO:0000313|Proteomes:UP000462865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A1 {ECO:0000313|EMBL:MSA95668.1,
RC ECO:0000313|Proteomes:UP000462865};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
RN [5] {ECO:0000313|EMBL:MVN16056.1, ECO:0000313|Proteomes:UP000468327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ResAG-59 {ECO:0000313|EMBL:MVN16056.1,
RC ECO:0000313|Proteomes:UP000468327};
RA Stoll D.A., Danylec N., Franz C.M.A.P., Huch M.;
RT "Whole genome shotgun sequencing (WGS) data from Adlercreutzia
RT equolifaciens ResAG-91, Eggerthella lenta MRI-F36, MRI-F37, MRI-F40, ResAG-
RT 49, ResAG-88, ResAG-121, ResAG-145, and Gordonibacter sp. ResAG-5, ResAG-
RT 26, ResAG-43, ResAG-50, ResAG-59.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00024550};
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:0000256|ARBA:ARBA00025935}.
CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC {ECO:0000256|ARBA:ARBA00006711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MVN16056.1}.
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; WKZA01000064; MSA95668.1; -; Genomic_DNA.
DR EMBL; WPOC01000022; MVN16056.1; -; Genomic_DNA.
DR EMBL; QIBW01000026; ROT88022.1; -; Genomic_DNA.
DR RefSeq; WP_015540438.1; NZ_WPOG01000035.1.
DR GeneID; 78359410; -.
DR Proteomes; UP000285258; Unassembled WGS sequence.
DR Proteomes; UP000462865; Unassembled WGS sequence.
DR Proteomes; UP000468327; Unassembled WGS sequence.
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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.90.940.10; -; 1.
DR InterPro; IPR003716; DNA-dir_RNA_pol_omega.
DR InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR InterPro; IPR036161; RPB6/omega-like_sf.
DR NCBIfam; TIGR00690; rpoZ; 1.
DR Pfam; PF01192; RNA_pol_Rpb6; 1.
DR SMART; SM01409; RNA_pol_Rpb6; 1.
DR SUPFAM; SSF63562; RPB6/omega subunit-like; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000313|EMBL:MVN16056.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:MVN16056.1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:MVN16056.1}.
SQ SEQUENCE 86 AA; 9734 MW; 7F034F77C1F35D69 CRC64;
MSIIEPKIDV LLDRTDNDRF LLCALASKRA HDINDMMRGQ RDRAIQLQTA VEIARAADKK
PLSLAFNEIA RGEVSYDPNS IDIKNH
//
