(data stored in ACNUC7421 zone)

SWISSPROT: RSIW_BACSU

ID   RSIW_BACSU              Reviewed;         208 AA.
AC   Q45588; O08075; Q45586; Q7DL99;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   11-DEC-2019, entry version 100.
DE   RecName: Full=Anti-sigma-W factor RsiW;
DE   AltName: Full=Regulator of SigW;
DE   AltName: Full=Sigma-W anti-sigma factor RsiW;
GN   Name=rsiW; Synonyms=ybbM; OrderedLocusNames=BSU01740;
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   FUNCTION, AND 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   INDUCTION.
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   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   FUNCTION, CLEAVAGE BY RASP, DOMAIN, AND TOPOLOGY.
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   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   CLEAVAGE BY PRSW.
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   CLEAVAGE BY PRSW.
RC   STRAIN=1012;
RX   PubMed=17020587; DOI=10.1111/j.1365-2958.2006.05391.x;
RA   Heinrich J., Wiegert T.;
RT   "YpdC determines site-1 degradation in regulated intramembrane proteolysis
RT   of the RsiW anti-sigma factor of Bacillus subtilis.";
RL   Mol. Microbiol. 62:566-579(2006).
RN   [10]
RP   CLEAVAGE BY CPLXP, MUTAGENESIS OF ALA-91; 91-ALA-ALA-92; 91-ALA--ALA-93 AND
RP   91-ALA--ALA-94, AND SUBCELLULAR LOCATION OF SITE-2 CLIPPED RSIW.
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   [11]
RP   CLEAVAGE BY PRSW AND RASP, AND MUTAGENESIS OF SER-117; VAL-129; GLY-146;
RP   ALA-168; SER-169; GLY-175; 188-TRP--GLU-208; 198-LEU--GLU-208 AND
RP   204-PRO--GLU-208.
RC   STRAIN=1012;
RX   PubMed=19889088; DOI=10.1111/j.1365-2958.2009.06940.x;
RA   Heinrich J., Hein K., Wiegert T.;
RT   "Two proteolytic modules are involved in regulated intramembrane
RT   proteolysis of Bacillus subtilis RsiW.";
RL   Mol. Microbiol. 74:1412-1426(2009).
RN   [12]
RP   FUNCTION AS AN ANTI-SIGMA FACTOR, AND MUTAGENESIS OF 26-VAL--HIS-40.
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   [13] {ECO:0000244|PDB:5WUQ, ECO:0000244|PDB:5WUR}
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-80 IN COMPLEX WITH REDUCED AND
RP   OXIDIZED SIGW, COFACTOR, 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: The anti-sigma factor for extracytoplasmic function (ECF)
CC       sigma factor sigma-W (SigW). Holds SigW, its cognate ECF sigma factor,
CC       in an inactive form until released by regulated intramembrane
CC       proteolysis (RIP). SigW and RsiW mediate cell response to cell wall
CC       stress (PubMed:12207695). RIP occurs when an extracytoplasmic signal
CC       triggers a concerted proteolytic cascade to transmit information and
CC       elicit cellular responses. The membrane-spanning regulatory substrate
CC       protein is first cut periplasmically (site-1 protease, S1P, PrsW)
CC       (PubMed:16816000, PubMed:17020587), then within the membrane itself
CC       (site-2 protease, S2P, RasP) (PubMed:15130127), while cytoplasmic
CC       proteases finish degrading the anti-sigma factor, liberating sigma-W
CC       (PubMed:16899079). {ECO:0000269|PubMed:12207695,
CC       ECO:0000269|PubMed:15130127, ECO:0000269|PubMed:16816000,
CC       ECO:0000269|PubMed:16899079, ECO:0000269|PubMed:17020587,
CC       ECO:0000269|PubMed:21685450}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:28319136};
CC       Note=Binds 1 Zn(2+) ion per subunit. Absence of the Zn(2+) (in a
CC       residue 1-80 fragment) does not prevent interaction with SigW, nor does
CC       it change the overall conformation of RsiW, although a disulfide bond
CC       can form between Cys-3 and Cys-37 (PubMed:28319136).
CC       {ECO:0000269|PubMed:28319136};
CC   -!- SUBUNIT: Forms a heterodimer with cognate sigma factor SigW, which
CC       probably prevents SigW from binding to DNA (PubMed:28319136).
CC       {ECO:0000269|PubMed:28319136}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16899079};
CC       Single-pass membrane protein {ECO:0000269|PubMed:16899079}. Note=Site-2
CC       clipped RsiW is released from the membrane to the cytoplasm
CC       (PubMed:16899079). {ECO:0000269|PubMed:16899079}.
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).
CC       {ECO:0000269|PubMed:11454200, ECO:0000269|PubMed:11544224,
CC       ECO:0000269|PubMed:12207695, ECO:0000269|PubMed:15870467}.
CC   -!- DOMAIN: The cytoplasmic domain is able to inactivate SigW and the
CC       extracellular and transmembrane domains are crucial for sensing and
CC       transducing the signal that triggers SigW activation (PubMed:15130127).
CC       The N-terminus binds the zinc ion and is followed by a long helix
CC       (about residues 40-80) that fits into a hydrophobic surface groove on
CC       SigW, probably blocking its ability to interact with the -10 and -35
CC       promoter elements (PubMed:28319136). {ECO:0000269|PubMed:15130127,
CC       ECO:0000269|PubMed:28319136}.
CC   -!- PTM: Is processed by successive proteolytic events. First, the
CC       extracellular region of RsiW is cleaved by PrsW (site-1 cleavage) in
CC       response to cell envelope stresses (PubMed:16816000, PubMed:17020587).
CC       In a reconstituted E.coli system PrsW cuts between Ala-168 and Ser-169
CC       followed by trimming by E.coli Tsp; the endogenous extracellular
CC       exopeptidase responsible for the event in B.subtilis has not been
CC       identified (PubMed:19889088). Next, it undergoes cleavage at an
CC       intramembrane site (site-2 cleavage) mediated by RasP
CC       (PubMed:15130127). This cleavage uncovers a cryptic proteolytic tag
CC       with conserved alanine residues in the transmembrane segment, that is
CC       recognized mainly by the ClpXP protease, which completely degrades the
CC       protein in the cytoplasm and leads to the induction of the sigma-W-
CC       controlled genes (PubMed:16899079). {ECO:0000269|PubMed:15130127,
CC       ECO:0000269|PubMed:16816000, ECO:0000269|PubMed:16899079,
CC       ECO:0000269|PubMed:17020587, ECO:0000269|PubMed:19889088}.
CC   -!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
CC       superfamily. Anti-sigma-W factor family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA19508.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; AB002150; BAA19508.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB11950.1; -; Genomic_DNA.
DR   PIR; G69744; G69744.
DR   RefSeq; NP_388055.1; NC_000964.3.
DR   RefSeq; WP_003234951.1; NZ_JNCM01000030.1.
DR   PDB; 5WUQ; X-ray; 2.80 A; C/D=1-80.
DR   PDB; 5WUR; X-ray; 2.60 A; C/D=1-80.
DR   PDBsum; 5WUQ; -.
DR   PDBsum; 5WUR; -.
DR   SMR; Q45588; -.
DR   IntAct; Q45588; 1.
DR   STRING; 224308.BSU01740; -.
DR   PaxDb; Q45588; -.
DR   PRIDE; Q45588; -.
DR   EnsemblBacteria; CAB11950; CAB11950; BSU01740.
DR   GeneID; 938876; -.
DR   KEGG; bsu:BSU01740; -.
DR   PATRIC; fig|224308.179.peg.180; -.
DR   eggNOG; COG5662; LUCA.
DR   HOGENOM; HOG000261706; -.
DR   InParanoid; Q45588; -.
DR   OMA; YMASAGQ; -.
DR   BioCyc; BSUB:BSU01740-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR027383; Znf_put.
DR   Pfam; PF13490; zf-HC2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q45588.
DR   SWISS-2DPAGE; Q45588.
KW   3D-structure; Cell membrane; Membrane; Metal-binding; Reference proteome;
KW   Stress response; Transcription; Transcription regulation; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..208
FT                   /note="Anti-sigma-W factor RsiW"
FT                   /id="PRO_0000097485"
FT   TOPO_DOM        1..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:28319136"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..208
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   METAL           3
FT                   /note="Zinc"
FT                   /evidence="ECO:0000269|PubMed:28319136"
FT   METAL           30
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000269|PubMed:28319136"
FT   METAL           34
FT                   /note="Zinc"
FT                   /evidence="ECO:0000269|PubMed:28319136"
FT   METAL           37
FT                   /note="Zinc"
FT                   /evidence="ECO:0000269|PubMed:28319136"
FT   MUTAGEN         26..40
FT                   /note="VLNEHLETCEKCRKH->KFEHHFEECSPCLEK: Partially inhibits
FT                   SigW, confers low diamide induction. A swap mutant with
FT                   RsrA of S.coelicolor."
FT                   /evidence="ECO:0000269|PubMed:21685450"
FT   MUTAGEN         91..94
FT                   /note="AAAA->LLLL: Abolishes induction of sigma-W-
FT                   controlled genes."
FT                   /evidence="ECO:0000269|PubMed:16899079"
FT   MUTAGEN         91..93
FT                   /note="AAA->LLL: Abolishes induction of sigma-W-controlled
FT                   genes."
FT                   /evidence="ECO:0000269|PubMed:16899079"
FT   MUTAGEN         91..92
FT                   /note="AA->LL: Abolishes induction of sigma-W-controlled
FT                   genes."
FT                   /evidence="ECO:0000269|PubMed:16899079"
FT   MUTAGEN         91
FT                   /note="A->L: No effect."
FT                   /evidence="ECO:0000269|PubMed:16899079"
FT   MUTAGEN         117
FT                   /note="S->F: No longer requires PrsW for degradation."
FT                   /evidence="ECO:0000269|PubMed:19889088"
FT   MUTAGEN         129
FT                   /note="V->M: No longer requires PrsW for degradation."
FT                   /evidence="ECO:0000269|PubMed:19889088"
FT   MUTAGEN         146
FT                   /note="G->S: No longer requires PrsW for degradation."
FT                   /evidence="ECO:0000269|PubMed:19889088"
FT   MUTAGEN         168
FT                   /note="A->Q: Retains anti-sigma-W activity, not degraded by
FT                   PrsW."
FT                   /evidence="ECO:0000269|PubMed:19889088"
FT   MUTAGEN         169
FT                   /note="S->Q: Wild-type; retains anti-sigma-W activity,
FT                   degraded by PrsW."
FT                   /evidence="ECO:0000269|PubMed:19889088"
FT   MUTAGEN         175
FT                   /note="G->D: No longer requires PrsW for degradation."
FT                   /evidence="ECO:0000269|PubMed:19889088"
FT   MUTAGEN         188..208
FT                   /note="Missing: No longer requires PrsW for degradation."
FT                   /evidence="ECO:0000269|PubMed:19889088"
FT   MUTAGEN         199..208
FT                   /note="Missing: No longer requires PrsW for degradation."
FT                   /evidence="ECO:0000269|PubMed:19889088"
FT   MUTAGEN         204..208
FT                   /note="Missing: Requires PrsW for degradation."
FT                   /evidence="ECO:0000269|PubMed:19889088"
FT   HELIX           5..16
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           21..33
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           35..52
FT                   /evidence="ECO:0000244|PDB:5WUR"
FT   HELIX           63..69
FT                   /evidence="ECO:0000244|PDB:5WUR"
SQ   SEQUENCE   208 AA;  23341 MW;  6CDC7814FD744465 CRC64;
     MSCPEQIVQL MHMHLDGDIL PKDEHVLNEH LETCEKCRKH FYEMEKSIAL VRSTSHVEAP
     ADFTANVMAK LPKEKKRASV KRWFRTHPVI AAAAVFIILM GGGFFNSWHN DHNFSVSKQP
     NLVVHNHTVT VPEGETVKGD VTVKNGKLII KGKIDGDVTV VNGEKYMASA GQVTGQIEEI
     NQLFDWTWYK MKSAGKSVLD AFNPNGEE
//

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