ID R9AJQ3_9GAMM Unreviewed; 93 AA.
AC R9AJQ3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=DNA-directed RNA polymerase subunit omega {ECO:0000256|ARBA:ARBA00013725, ECO:0000256|HAMAP-Rule:MF_00366};
DE Short=RNAP omega subunit {ECO:0000256|HAMAP-Rule:MF_00366};
DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418, ECO:0000256|HAMAP-Rule:MF_00366};
DE AltName: Full=RNA polymerase omega subunit {ECO:0000256|ARBA:ARBA00030998, ECO:0000256|HAMAP-Rule:MF_00366};
DE AltName: Full=Transcriptase subunit omega {ECO:0000256|ARBA:ARBA00029924, ECO:0000256|HAMAP-Rule:MF_00366};
GN Name=rpoZ {ECO:0000256|HAMAP-Rule:MF_00366};
GN ORFNames=I593_03710 {ECO:0000313|EMBL:EOR02442.1};
OS Acinetobacter tandoii DSM 14970 = CIP 107469.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120927 {ECO:0000313|EMBL:EOR02442.1, ECO:0000313|Proteomes:UP000016201};
RN [1] {ECO:0000313|EMBL:EOR02442.1, ECO:0000313|Proteomes:UP000016201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107469 {ECO:0000313|EMBL:EOR02442.1,
RC ECO:0000313|Proteomes:UP000016201};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter tandoii CIP 107469.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C-
CC terminal regions of the beta' subunit thereby facilitating its
CC interaction with the beta and alpha subunits. {ECO:0000256|HAMAP-
CC Rule:MF_00366}.
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 ECO:0000256|HAMAP-Rule:MF_00366};
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|HAMAP-Rule:MF_00366}.
CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC {ECO:0000256|ARBA:ARBA00006711, ECO:0000256|HAMAP-Rule:MF_00366}.
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:EOR02442.1}.
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DR EMBL; AQFM01000048; EOR02442.1; -; Genomic_DNA.
DR RefSeq; WP_004978050.1; NZ_KE007371.1.
DR AlphaFoldDB; R9AJQ3; -.
DR GeneID; 56337437; -.
DR PATRIC; fig|1120927.3.peg.3610; -.
DR eggNOG; COG1758; Bacteria.
DR OrthoDB; 9796300at2; -.
DR Proteomes; UP000016201; Unassembled WGS sequence.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.940.10; -; 1.
DR HAMAP; MF_00366; RNApol_bact_RpoZ; 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 PANTHER; PTHR34476; DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA; 1.
DR PANTHER; PTHR34476:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA; 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:0000256|HAMAP-Rule:MF_00366};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00366};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00366};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00366}.
SQ SEQUENCE 93 AA; 10524 MW; 8BCDF14AAF2ACA8D CRC64;
MARVTVEDCL DHVDNRFELV LVASKRARQL ARQGIEPTVE WDNDKPTVVA LREIAIGHVS
KDILKQREQD YQTSSLDLAL SANNLNLDGF SFQ
//
