RPOZ_BACSU
ID RPOZ_BACSU Reviewed; 67 AA.
AC O35011;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=DNA-directed RNA polymerase subunit omega {ECO:0000303|PubMed:6802805};
DE Short=RNAP omega subunit;
DE EC=2.7.7.6 {ECO:0000269|PubMed:6802805};
DE AltName: Full=RNA polymerase omega 2 subunit {ECO:0000303|PubMed:6802805};
DE AltName: Full=Transcriptase subunit omega;
GN Name=rpoZ; Synonyms=yloH; OrderedLocusNames=BSU15690;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9534248; DOI=10.1099/00221287-144-3-801;
RA Foulger D., Errington J.;
RT "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT genome.";
RL Microbiology 144:801-805(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=6802805; DOI=10.1128/jb.150.2.977-980.1982;
RA Achberger E.C., Tahara M., Whiteley H.R.;
RT "Interchangeability of delta subunits of RNA polymerase from different
RT species of the genus Bacillus.";
RL J. Bacteriol. 150:977-980(1982).
RN [4]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=BS200;
RX PubMed=18289874; DOI=10.1016/j.pep.2008.01.006;
RA Yang X., Lewis P.J.;
RT "Overproduction and purification of recombinant Bacillus subtilis RNA
RT polymerase.";
RL Protein Expr. Purif. 59:86-93(2008).
RN [5]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=21710567; DOI=10.1002/pmic.201000790;
RA Delumeau O., Lecointe F., Muntel J., Guillot A., Guedon E., Monnet V.,
RA Hecker M., Becher D., Polard P., Noirot P.;
RT "The dynamic protein partnership of RNA polymerase in Bacillus subtilis.";
RL Proteomics 11:2992-3001(2011).
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). In vitro
CC reconstitution experiments this subunit is dispensible
CC (PubMed:18289874). {ECO:0000250, ECO:0000269|PubMed:18289874}.
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: RNAP is composed of a core of 2 alpha, a beta and a beta'
CC subunit. The core is associated with a delta subunit, and at least one
CC of epsilon or omega (PubMed:6802805, PubMed:18289874, PubMed:21710567).
CC When a sigma factor is associated with the core the holoenzyme is
CC formed, which can initiate transcription (PubMed:18289874).
CC {ECO:0000269|PubMed:18289874, ECO:0000269|PubMed:21710567,
CC ECO:0000269|PubMed:6802805}.
CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y13937; CAA74272.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13442.1; -; Genomic_DNA.
DR PIR; C69878; C69878.
DR RefSeq; NP_389451.1; NC_000964.3.
DR RefSeq; WP_003221520.1; NZ_JNCM01000035.1.
DR PDB; 6WVJ; EM; 3.36 A; F=1-67.
DR PDB; 6WVK; EM; 3.36 A; F=1-67.
DR PDB; 7CKQ; EM; 4.40 A; E=1-67.
DR PDB; 7F75; EM; 4.20 A; E=1-67.
DR PDBsum; 6WVJ; -.
DR PDBsum; 6WVK; -.
DR PDBsum; 7CKQ; -.
DR PDBsum; 7F75; -.
DR AlphaFoldDB; O35011; -.
DR SMR; O35011; -.
DR STRING; 224308.BSU15690; -.
DR PaxDb; O35011; -.
DR PRIDE; O35011; -.
DR EnsemblBacteria; CAB13442; CAB13442; BSU_15690.
DR GeneID; 50133576; -.
DR GeneID; 64303460; -.
DR GeneID; 936419; -.
DR KEGG; bsu:BSU15690; -.
DR PATRIC; fig|224308.179.peg.1709; -.
DR eggNOG; COG1758; Bacteria.
DR InParanoid; O35011; -.
DR OMA; KYTIVTV; -.
DR PhylomeDB; O35011; -.
DR BioCyc; BSUB:BSU15690-MON; -.
DR PRO; PR:O35011; -.
DR Proteomes; UP000001570; 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: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 Reference proteome; Transcription; Transferase.
FT CHAIN 1..67
FT /note="DNA-directed RNA polymerase subunit omega"
FT /id="PRO_0000128916"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 16..33
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:6WVJ"
SQ SEQUENCE 67 AA; 7754 MW; 022B8C8A5E371409 CRC64;
MLDPSIDSLM NKLDSKYTLV TVSARRAREM QIKKDQMIEH TISHKYVGKA LEEIDAGLLS
FEKEDRE
