ID F3Y8B2_MELPT Unreviewed; 102 AA.
AC F3Y8B2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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|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 OrderedLocusNames=MPTP_0242 {ECO:0000313|EMBL:BAK20740.1};
OS Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB
OS 702443).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Melissococcus.
OX NCBI_TaxID=940190 {ECO:0000313|EMBL:BAK20740.1, ECO:0000313|Proteomes:UP000008456};
RN [1] {ECO:0000313|EMBL:BAK20740.1, ECO:0000313|Proteomes:UP000008456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443
RC {ECO:0000313|Proteomes:UP000008456};
RX PubMed=21622755; DOI=10.1128/JB.05151-11;
RA Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M.,
RA Miyoshi-Akiyama T.;
RT "Complete genome sequence of Melissococcus plutonius ATCC 35311.";
RL J. Bacteriol. 193:4029-4030(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 35311;
RA Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D.,
RA Akiyama T.;
RT "Whole genome sequence of Melissococcus plutonius ATCC 35311.";
RL Submitted (APR-2011) 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.
CC {ECO:0000256|ARBA:ARBA00024694, ECO:0000256|HAMAP-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}.
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DR EMBL; AP012200; BAK20740.1; -; Genomic_DNA.
DR RefSeq; WP_013773178.1; NC_015516.1.
DR AlphaFoldDB; F3Y8B2; -.
DR STRING; 940190.MPTP_0242; -.
DR GeneID; 57042783; -.
DR KEGG; mps:MPTP_0242; -.
DR HOGENOM; CLU_125406_0_0_9; -.
DR OrthoDB; 9815459at2; -.
DR Proteomes; UP000008456; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000008456};
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}.
FT REGION 59..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 102 AA; 11802 MW; 9FCE5F6EDE5737FB CRC64;
MMLKPSIDSL LKKVPSKYSL VILASKRAHE LDEGMDPTLD SFESVKNVGR ALEEINTGKL
INDPHPEEKR ERIQLAREEK KKIHEQEQKD LEEKISHENT IK
//
