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Database: UniProt
Entry: B4VLV7_9CYAN
LinkDB: B4VLV7_9CYAN
Original site: B4VLV7_9CYAN 
ID   B4VLV7_9CYAN            Unreviewed;        76 AA.
AC   B4VLV7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 53.
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   ORFNames=MC7420_484 {ECO:0000313|EMBL:EDX77347.1};
OS   Coleofasciculus chthonoplastes PCC 7420.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Coleofasciculus.
OX   NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX77347.1, ECO:0000313|Proteomes:UP000003835};
RN   [1] {ECO:0000313|EMBL:EDX77347.1, ECO:0000313|Proteomes:UP000003835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX77347.1,
RC   ECO:0000313|Proteomes:UP000003835};
RA   Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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: In cyanobacteria the RNAP catalytic core is composed of 2
CC       alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC       factor is associated with the core the holoenzyme is formed, which can
CC       initiate transcription. {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; DS989844; EDX77347.1; -; Genomic_DNA.
DR   RefSeq; WP_006099459.1; NZ_DS989844.1.
DR   AlphaFoldDB; B4VLV7; -.
DR   STRING; 118168.MC7420_484; -.
DR   eggNOG; ENOG5032RMS; Bacteria.
DR   HOGENOM; CLU_175526_0_0_3; -.
DR   OrthoDB; 463386at2; -.
DR   Proteomes; UP000003835; 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   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   Pfam; PF01192; 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:UP000003835};
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   76 AA;  9067 MW;  1827A6825381D80F CRC64;
     MLHRRYQFDS SQIMHRAEEL VTAASNRYRI TVQVANRAKR RRYEDFENLD DPMMKPVLRA
     IIEMSDELTQ PEIIGD
//
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