RPOZ_FRATH
ID RPOZ_FRATH Reviewed; 72 AA.
AC Q2A273;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=DNA-directed RNA polymerase subunit omega {ECO:0000255|HAMAP-Rule:MF_00366};
DE Short=RNAP omega subunit {ECO:0000255|HAMAP-Rule:MF_00366};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00366};
DE AltName: Full=RNA polymerase omega subunit {ECO:0000255|HAMAP-Rule:MF_00366};
DE AltName: Full=Transcriptase subunit omega {ECO:0000255|HAMAP-Rule:MF_00366};
GN Name=rpoZ {ECO:0000255|HAMAP-Rule:MF_00366}; OrderedLocusNames=FTL_1533;
OS Francisella tularensis subsp. holarctica (strain LVS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=376619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVS;
RA Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S.,
RA Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R.,
RA Garcia E.;
RT "Complete genome sequence of Francisella tularensis LVS (Live Vaccine
RT Strain).";
RL Submitted (MAR-2006) 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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00366}.
CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC {ECO:0000255|HAMAP-Rule:MF_00366}.
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DR EMBL; AM233362; CAJ79972.1; -; Genomic_DNA.
DR RefSeq; WP_003016869.1; NZ_CP009694.1.
DR PDB; 6WMP; EM; 2.98 A; E=1-72.
DR PDB; 6WMR; EM; 3.46 A; E=1-72.
DR PDB; 6WMT; EM; 4.43 A; E=1-72.
DR PDBsum; 6WMP; -.
DR PDBsum; 6WMR; -.
DR PDBsum; 6WMT; -.
DR AlphaFoldDB; Q2A273; -.
DR SMR; Q2A273; -.
DR KEGG; ftl:FTL_1533; -.
DR OMA; NVDNRFQ; -.
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 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 PANTHER; PTHR34476; PTHR34476; 1.
DR Pfam; PF01192; RNA_pol_Rpb6; 1.
DR SMART; SM01409; RNA_pol_Rpb6; 1.
DR SUPFAM; SSF63562; SSF63562; 1.
DR TIGRFAMs; TIGR00690; rpoZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Transcription; Transferase.
FT CHAIN 1..72
FT /note="DNA-directed RNA polymerase subunit omega"
FT /id="PRO_1000005930"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:6WMP"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:6WMP"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:6WMP"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:6WMP"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6WMP"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6WMP"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:6WMP"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:6WMP"
FT TURN 67..71
FT /evidence="ECO:0007829|PDB:6WMR"
SQ SEQUENCE 72 AA; 8173 MW; BF42DFFBCF1F1BAB CRC64;
MARVTVEDCL DKVETRFDLV VLASMRANKI LKNGYSESME NEKKEKATVV ALREIAESEI
TSEQILRNEI EG