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 03-AUG-2022, entry version 144.
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]
RP FUNCTION, SUBUNIT, AND INDUCTION.
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).
RN [12] {ECO:0007744|PDB:5WUQ, ECO:0007744|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 (RNAP) to specific initiation sites and
CC are then released. Sigma-W controls genes involved in response to cell
CC envelope 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, ECO:0000305|PubMed:21710567}.
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 ECO:0000305|PubMed:21710567}.
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). Association with
CC RNAP core increases during most stresses but not during sporulation (at
CC protein level) (PubMed:21710567). {ECO:0000269|PubMed:11454200,
CC ECO:0000269|PubMed:11544224, ECO:0000269|PubMed:12207695,
CC ECO:0000269|PubMed:15870467, ECO:0000269|PubMed:21685450,
CC ECO:0000269|PubMed:21710567}.
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}.
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; 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; 5OR5; NMR; -; A=64-69.
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 PDB; 6JHE; X-ray; 3.10 A; A=126-187.
DR PDBsum; 5OR5; -.
DR PDBsum; 5WUQ; -.
DR PDBsum; 5WUR; -.
DR PDBsum; 6JHE; -.
DR AlphaFoldDB; Q45585; -.
DR SMR; Q45585; -.
DR IntAct; Q45585; 2.
DR STRING; 224308.BSU01730; -.
DR PaxDb; Q45585; -.
DR PRIDE; Q45585; -.
DR EnsemblBacteria; CAB11949; CAB11949; BSU_01730.
DR GeneID; 938868; -.
DR KEGG; bsu:BSU01730; -.
DR PATRIC; fig|224308.179.peg.179; -.
DR eggNOG; COG1595; Bacteria.
DR InParanoid; Q45585; -.
DR OMA; LVDMQGY; -.
DR PhylomeDB; Q45585; -.
DR BioCyc; BSUB:BSU01730-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
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;
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:0007829|PDB:5WUR"
FT HELIX 17..39
FT /evidence="ECO:0007829|PDB:5WUR"
FT HELIX 42..58
FT /evidence="ECO:0007829|PDB:5WUR"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5WUR"
FT HELIX 69..88
FT /evidence="ECO:0007829|PDB:5WUR"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:5WUR"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:5WUR"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:5WUR"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:5WUR"
FT HELIX 166..184
FT /evidence="ECO:0007829|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
