(data stored in ACNUC7421 zone)

SWISSPROT: SIGW_BACSU

ID   SIGW_BACSU              Reviewed;         187 AA.
AC   Q45585; O08074;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   11-DEC-2019, entry version 135.
DE   RecName: Full=ECF RNA polymerase sigma factor SigW;
DE            Short=ECF sigma factor SigW;
DE   AltName: Full=Alternative RNA polymerase sigma factor SigW;
DE   AltName: Full=RNA polymerase sigma-W factor;
DE            Short=Sigma-W factor;
GN   Name=sigW; Synonyms=ybbL; OrderedLocusNames=BSU01730;
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=9274029; DOI=10.1099/00221287-143-8-2763;
RA   Liu H., Haga K., Yasumoto K., Ohashi Y., Yoshikawa H., Takahashi H.;
RT   "Sequence and analysis of a 31 kb segment of the Bacillus subtilis
RT   chromosome in the area of the rrnH and rrnG operons.";
RL   Microbiology 143:2763-2767(1997).
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   INDUCTION.
RX   PubMed=11544224; DOI=10.1128/jb.183.19.5617-5631.2001;
RA   Petersohn A., Brigulla M., Haas S., Hoheisel J.D., Voelker U., Hecker M.;
RT   "Global analysis of the general stress response of Bacillus subtilis.";
RL   J. Bacteriol. 183:5617-5631(2001).
RN   [4]
RP   FUNCTION, REGULON, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=11454200; DOI=10.1046/j.1365-2958.2001.02489.x;
RA   Wiegert T., Homuth G., Versteeg S., Schumann W.;
RT   "Alkaline shock induces the Bacillus subtilis sigma(W) regulon.";
RL   Mol. Microbiol. 41:59-71(2001).
RN   [5]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=12207695; DOI=10.1046/j.1365-2958.2002.03050.x;
RA   Cao M., Wang T., Ye R., Helmann J.D.;
RT   "Antibiotics that inhibit cell wall biosynthesis induce expression of the
RT   Bacillus subtilis sigma(W) and sigma(M) regulons.";
RL   Mol. Microbiol. 45:1267-1276(2002).
RN   [6]
RP   ACTIVITY REGULATION.
RX   PubMed=15130127; DOI=10.1111/j.1365-2958.2004.04031.x;
RA   Schoebel S., Zellmeier S., Schumann W., Wiegert T.;
RT   "The Bacillus subtilis sigmaW anti-sigma factor RsiW is degraded by
RT   intramembrane proteolysis through YluC.";
RL   Mol. Microbiol. 52:1091-1105(2004).
RN   [7]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=15870467; DOI=10.1099/mic.0.27761-0;
RA   Pietiaeinen M., Gardemeister M., Mecklin M., Leskelae S., Sarvas M.,
RA   Kontinen V.P.;
RT   "Cationic antimicrobial peptides elicit a complex stress response in
RT   Bacillus subtilis that involves ECF-type sigma factors and two-component
RT   signal transduction systems.";
RL   Microbiology 151:1577-1592(2005).
RN   [8]
RP   ACTIVITY REGULATION.
RX   PubMed=16816000; DOI=10.1101/gad.1440606;
RA   Ellermeier C.D., Losick R.;
RT   "Evidence for a novel protease governing regulated intramembrane
RT   proteolysis and resistance to antimicrobial peptides in Bacillus
RT   subtilis.";
RL   Genes Dev. 20:1911-1922(2006).
RN   [9]
RP   ACTIVITY REGULATION.
RX   PubMed=16899079; DOI=10.1111/j.1365-2958.2006.05323.x;
RA   Zellmeier S., Schumann W., Wiegert T.;
RT   "Involvement of Clp protease activity in modulating the Bacillus subtilis
RT   sigma-W stress response.";
RL   Mol. Microbiol. 61:1569-1582(2006).
RN   [10]
RP   FUNCTION AS A SIGMA FACTOR, AND INDUCTION.
RX   PubMed=21685450; DOI=10.1093/nar/gkr477;
RA   Jung Y.G., Cho Y.B., Kim M.S., Yoo J.S., Hong S.H., Roe J.H.;
RT   "Determinants of redox sensitivity in RsrA, a zinc-containing anti-sigma
RT   factor for regulating thiol oxidative stress response.";
RL   Nucleic Acids Res. 39:7586-7597(2011).
RN   [11] {ECO:0000244|PDB:5WUQ, ECO:0000244|PDB:5WUR}
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH REDUCED AND OXIDZED
RP   SIGW, SUBUNIT, AND DOMAIN.
RC   STRAIN=168;
RX   PubMed=28319136; DOI=10.1371/journal.pone.0174284;
RA   Devkota S.R., Kwon E., Ha S.C., Chang H.W., Kim D.Y.;
RT   "Structural insights into the regulation of Bacillus subtilis SigW activity
RT   by anti-sigma RsiW.";
RL   PLoS ONE 12:E0174284-E0174284(2017).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released. Sigma-W controls genes involved in response to cell envelope
CC       stress such as antimicrobial peptides (PubMed:12207695,
CC       PubMed:15870467), alkaline pH (PubMed:11454200), transport processes
CC       and detoxification. {ECO:0000269|PubMed:11454200,
CC       ECO:0000269|PubMed:12207695, ECO:0000269|PubMed:15870467,
CC       ECO:0000269|PubMed:21685450}.
CC   -!- ACTIVITY REGULATION: Extracytoplasmic function (ECF) sigma factors are
CC       held in an inactive form by a cognate anti-sigma factor (RsiW for this
CC       protein) until released by regulated membrane proteolysis (RIP). RIP
CC       occurs when an extracytoplasmic signal (envelope stress) triggers a
CC       concerted proteolytic cascade to transmit information and elicit
CC       cellular responses. The anti-sigma factor RsiW is a membrane protein,
CC       binding sigma-W in the cytoplasm. RsiW is first cut
CC       extracytoplasmically (site-1 protease, S1P, by PrsW) (PubMed:16816000),
CC       then within the membrane itself (site-2 protease, S2P, by RasP)
CC       (PubMed:15130127), while cytoplasmic proteases (predominantly ClpX-
CC       ClpP) finish degrading the regulatory protein, liberating sigma-W
CC       (PubMed:16899079). {ECO:0000269|PubMed:15130127,
CC       ECO:0000269|PubMed:16816000, ECO:0000269|PubMed:16899079}.
CC   -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core
CC       formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1
CC       omega subunit) to form the RNA polymerase holoenzyme that can initiate
CC       transcription. Forms a heterodimer with cognate anti-sigma factor RsiW,
CC       which prevents it binding to the -10 and -35 promoter elements
CC       (PubMed:28319136). {ECO:0000269|PubMed:28319136}.
CC   -!- INDUCTION: By different stresses causing damage to the cell envelope,
CC       such as alkaline shock (PubMed:11454200), salt shock (PubMed:11544224),
CC       phage infection and certain antibiotics that affect cell wall
CC       biosynthesis (PubMed:12207695, PubMed:15870467). Does not respond to
CC       oxidative stress caused by diamide (PubMed:21685450).
CC       {ECO:0000269|PubMed:11454200, ECO:0000269|PubMed:11544224,
CC       ECO:0000269|PubMed:12207695, ECO:0000269|PubMed:15870467,
CC       ECO:0000269|PubMed:21685450}.
CC   -!- DOMAIN: The sigma-70 factor domain-2 mediates sequence-specific
CC       interaction with the -10 element in promoter DNA (PubMed:28319136), and
CC       plays an important role in melting the double-stranded DNA and the
CC       formation of the transcription bubble. Also mediates interaction with
CC       the RNA polymerase subunits RpoB and RpoC (By similarity).
CC       {ECO:0000250|UniProtKB:P0AGB6, ECO:0000269|PubMed:28319136}.
CC   -!- DOMAIN: The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-
CC       H) motif that mediates interaction with the -35 element in promoter DNA
CC       (PubMed:28319136). The domain also mediates interaction with the RNA
CC       polymerase subunit RpoA (By similarity). {ECO:0000250|UniProtKB:P0AGB6,
CC       ECO:0000269|PubMed:28319136}.
CC   -!- DISRUPTION PHENOTYPE: Alteration (reduction or loss for the most part)
CC       of expression of about 60 genes that are high-pH-inducible, including
CC       sigW and its anti-sigma factor rsiW (PubMed:11454200).
CC       {ECO:0000269|PubMed:11454200}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC       {ECO:0000305}.
DR   EMBL; AB002150; BAA19507.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11949.1; -; Genomic_DNA.
DR   PIR; H69706; H69706.
DR   RefSeq; NP_388054.1; NC_000964.3.
DR   RefSeq; WP_003234958.1; NZ_JNCM01000030.1.
DR   PDB; 5WUQ; X-ray; 2.80 A; A/B=1-187.
DR   PDB; 5WUR; X-ray; 2.60 A; A/B=1-187.
DR   PDBsum; 5WUQ; -.
DR   PDBsum; 5WUR; -.
DR   SMR; Q45585; -.
DR   IntAct; Q45585; 2.
DR   STRING; 224308.BSU01730; -.
DR   PaxDb; Q45585; -.
DR   PRIDE; Q45585; -.
DR   EnsemblBacteria; CAB11949; CAB11949; BSU01730.
DR   GeneID; 938868; -.
DR   KEGG; bsu:BSU01730; -.
DR   PATRIC; fig|224308.179.peg.179; -.
DR   eggNOG; ENOG4105EMN; Bacteria.
DR   eggNOG; COG1595; LUCA.
DR   HOGENOM; HOG000094755; -.
DR   InParanoid; Q45585; -.
DR   KO; K03088; -.
DR   OMA; RYQRKVY; -.
DR   PhylomeDB; Q45585; -.
DR   BioCyc; BSUB:BSU01730-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR039425; RNA_pol_sigma-70-like.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR   InterPro; IPR014294; RNA_pol_sigma-W_bacilli.
DR   InterPro; IPR000838; RNA_pol_sigma70_ECF_CS.
DR   InterPro; IPR007627; RNA_pol_sigma70_r2.
DR   InterPro; IPR013249; RNA_pol_sigma70_r4_t2.
DR   InterPro; IPR013325; RNA_pol_sigma_r2.
DR   InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR43133; PTHR43133; 1.
DR   Pfam; PF04542; Sigma70_r2; 1.
DR   Pfam; PF08281; Sigma70_r4_2; 1.
DR   SUPFAM; SSF88659; SSF88659; 1.
DR   SUPFAM; SSF88946; SSF88946; 1.
DR   TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR   TIGRFAMs; TIGR02948; SigW_bacill; 1.
DR   PROSITE; PS01063; SIGMA70_ECF; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q45585.
DR   SWISS-2DPAGE; Q45585.
KW   3D-structure; DNA-binding; Reference proteome; Sigma factor;
KW   Stress response; Transcription; Transcription regulation.
FT   CHAIN           1..187
FT                   /note="ECF RNA polymerase sigma factor SigW"
FT                   /id="PRO_0000094016"
FT   DNA_BIND        166..184
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000305|PubMed:28319136"
FT   REGION          3..95
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000305|PubMed:28319136"
FT   REGION          125..187
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000305|PubMed:28319136"
FT   MOTIF           47..50
FT                   /note="Polymerase core binding"
FT   HELIX           3..13
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           17..39
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           42..58
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           60..62
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           69..88
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           92..94
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           126..135
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           139..149
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           155..162
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           166..184
FT                   /evidence="ECO:0000244|PDB:5WUR"
SQ   SEQUENCE   187 AA;  21713 MW;  5F532568D462181A CRC64;
     MEMMIKKRIK QVKKGDQDAF ADIVDIYKDK IYQLCYRMLG NVHEAEDIAQ EAFIRAYVNI
     DSFDINRKFS TWLYRIATNL TIDRIRKKKP DYYLDAEVAG TEGLTMYSQI VADGVLPEDA
     VVSLELSNTI QQKILKLPDK YRTVIVLKYI DELSLIEIGE ILNIPVGTVK TRIHRGREAL
     RKQLRDL
//

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