RPOZ_TREPA
ID RPOZ_TREPA Reviewed; 67 AA.
AC O83699;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA-directed RNA polymerase subunit omega;
DE Short=RNAP omega subunit;
DE EC=2.7.7.6;
DE AltName: Full=RNA polymerase omega subunit;
DE AltName: Full=Transcriptase subunit omega;
GN Name=rpoZ; OrderedLocusNames=TP_0701;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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 (By similarity).
CC {ECO:0000250}.
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;
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC {ECO:0000305}.
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DR EMBL; AE000520; AAC65670.1; -; Genomic_DNA.
DR PIR; A71289; A71289.
DR RefSeq; WP_010882146.1; NC_021490.2.
DR AlphaFoldDB; O83699; -.
DR SMR; O83699; -.
DR IntAct; O83699; 3.
DR STRING; 243276.TPANIC_0701; -.
DR EnsemblBacteria; AAC65670; AAC65670; TP_0701.
DR GeneID; 57879226; -.
DR KEGG; tpa:TP_0701; -.
DR eggNOG; ENOG502ZVPX; Bacteria.
DR HOGENOM; CLU_187773_0_0_12; -.
DR OMA; SYQLSML; -.
DR OrthoDB; 2018659at2; -.
DR Proteomes; UP000000811; Chromosome.
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:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR InterPro; IPR036161; RPB6/omega-like_sf.
DR Pfam; PF01192; RNA_pol_Rpb6; 1.
DR SMART; SM01409; RNA_pol_Rpb6; 1.
DR SUPFAM; SSF63562; SSF63562; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..67
FT /note="DNA-directed RNA polymerase subunit omega"
FT /id="PRO_0000129006"
SQ SEQUENCE 67 AA; 7349 MW; 36D34AA347B48E10 CRC64;
MIFPMQQLIE FQGNIYEITC AATRRAFQLA AVCDPVLDEL GGKVVSAAAQ QVFSGTVDYR
IEPQELG