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Anti-sigma-W factor RsiW (Regulator of SigW) (Sigma-W anti-sigma factor RsiW)

 RSIW_BACSU              Reviewed;         208 AA.
Q45588; O08075; Q45586; Q7DL99;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 2.
27-SEP-2017, entry version 93.
RecName: Full=Anti-sigma-W factor RsiW;
AltName: Full=Regulator of SigW;
AltName: Full=Sigma-W anti-sigma factor RsiW;
Name=rsiW; Synonyms=ybbM; OrderedLocusNames=BSU01740;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9274029; DOI=10.1099/00221287-143-8-2763;
Liu H., Haga K., Yasumoto K., Ohashi Y., Yoshikawa H., Takahashi H.;
"Sequence and analysis of a 31 kb segment of the Bacillus subtilis
chromosome in the area of the rrnH and rrnG operons.";
Microbiology 143:2763-2767(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
FUNCTION, AND INDUCTION.
PubMed=11544224; DOI=10.1128/JB.183.19.5617-5631.2001;
Petersohn A., Brigulla M., Haas S., Hoheisel J.D., Voelker U.,
Hecker M.;
"Global analysis of the general stress response of Bacillus
subtilis.";
J. Bacteriol. 183:5617-5631(2001).
[4]
INDUCTION.
STRAIN=168;
PubMed=11454200; DOI=10.1046/j.1365-2958.2001.02489.x;
Wiegert T., Homuth G., Versteeg S., Schumann W.;
"Alkaline shock induces the Bacillus subtilis sigma(W) regulon.";
Mol. Microbiol. 41:59-71(2001).
[5]
INDUCTION.
PubMed=12207695; DOI=10.1046/j.1365-2958.2002.03050.x;
Cao M., Wang T., Ye R., Helmann J.D.;
"Antibiotics that inhibit cell wall biosynthesis induce expression of
the Bacillus subtilis sigma(W) and sigma(M) regulons.";
Mol. Microbiol. 45:1267-1276(2002).
[6]
FUNCTION, CLEAVAGE BY RASP, DOMAIN, AND TOPOLOGY.
PubMed=15130127; DOI=10.1111/j.1365-2958.2004.04031.x;
Schoebel S., Zellmeier S., Schumann W., Wiegert T.;
"The Bacillus subtilis sigmaW anti-sigma factor RsiW is degraded by
intramembrane proteolysis through YluC.";
Mol. Microbiol. 52:1091-1105(2004).
[7]
INDUCTION.
PubMed=15870467; DOI=10.1099/mic.0.27761-0;
Pietiaeinen M., Gardemeister M., Mecklin M., Leskelae S., Sarvas M.,
Kontinen V.P.;
"Cationic antimicrobial peptides elicit a complex stress response in
Bacillus subtilis that involves ECF-type sigma factors and two-
component signal transduction systems.";
Microbiology 151:1577-1592(2005).
[8]
CLEAVAGE BY PRSW.
PubMed=16816000; DOI=10.1101/gad.1440606;
Ellermeier C.D., Losick R.;
"Evidence for a novel protease governing regulated intramembrane
proteolysis and resistance to antimicrobial peptides in Bacillus
subtilis.";
Genes Dev. 20:1911-1922(2006).
[9]
CLEAVAGE BY PRSW.
STRAIN=1012;
PubMed=17020587; DOI=10.1111/j.1365-2958.2006.05391.x;
Heinrich J., Wiegert T.;
"YpdC determines site-1 degradation in regulated intramembrane
proteolysis of the RsiW anti-sigma factor of Bacillus subtilis.";
Mol. Microbiol. 62:566-579(2006).
[10]
CLEAVAGE BY CPLXP, MUTAGENESIS OF ALA-91; 91-ALA-ALA-92;
91-ALA--ALA-93 AND 91-ALA--ALA-94, AND SUBCELLULAR LOCATION OF SITE-2
CLIPPED RSIW.
PubMed=16899079; DOI=10.1111/j.1365-2958.2006.05323.x;
Zellmeier S., Schumann W., Wiegert T.;
"Involvement of Clp protease activity in modulating the Bacillus
subtilis sigma-W stress response.";
Mol. Microbiol. 61:1569-1582(2006).
[11]
CLEAVAGE BY PRSW AND RASP, AND MUTAGENESIS OF SER-117; VAL-129;
GLY-146; ALA-168; SER-169; GLY-175; 188-TRP--GLU-208; 198-LEU--GLU-208
AND 204-PRO--GLU-208.
STRAIN=1012;
PubMed=19889088; DOI=10.1111/j.1365-2958.2009.06940.x;
Heinrich J., Hein K., Wiegert T.;
"Two proteolytic modules are involved in regulated intramembrane
proteolysis of Bacillus subtilis RsiW.";
Mol. Microbiol. 74:1412-1426(2009).
[12]
FUNCTION AS AN ANTI-SIGMA FACTOR, AND MUTAGENESIS OF 26-VAL--HIS-40.
PubMed=21685450; DOI=10.1093/nar/gkr477;
Jung Y.G., Cho Y.B., Kim M.S., Yoo J.S., Hong S.H., Roe J.H.;
"Determinants of redox sensitivity in RsrA, a zinc-containing anti-
sigma factor for regulating thiol oxidative stress response.";
Nucleic Acids Res. 39:7586-7597(2011).
[13] {ECO:0000244|PDB:5WUQ, ECO:0000244|PDB:5WUR}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-80 IN COMPLEX WITH REDUCED
AND OXIDIZED SIGW, COFACTOR, SUBUNIT, AND DOMAIN.
STRAIN=168;
PubMed=28319136; DOI=10.1371/journal.pone.0174284;
Devkota S.R., Kwon E., Ha S.C., Chang H.W., Kim D.Y.;
"Structural insights into the regulation of Bacillus subtilis SigW
activity by anti-sigma RsiW.";
PLoS ONE 12:E0174284-E0174284(2017).
-!- FUNCTION: The anti-sigma factor for extracytoplasmic function
(ECF) sigma factor sigma-W (SigW). Holds SigW, its cognate ECF
sigma factor, in an inactive form until released by regulated
intramembrane proteolysis (RIP). SigW and RsiW mediate cell
response to cell wall stress (PubMed:12207695). RIP occurs when an
extracytoplasmic signal triggers a concerted proteolytic cascade
to transmit information and elicit cellular responses. The
membrane-spanning regulatory substrate protein is first cut
periplasmically (site-1 protease, S1P, PrsW) (PubMed:16816000,
PubMed:17020587), then within the membrane itself (site-2
protease, S2P, RasP) (PubMed:15130127), while cytoplasmic
proteases finish degrading the anti-sigma factor, liberating
sigma-W (PubMed:16899079). {ECO:0000269|PubMed:12207695,
ECO:0000269|PubMed:15130127, ECO:0000269|PubMed:16816000,
ECO:0000269|PubMed:16899079, ECO:0000269|PubMed:17020587,
ECO:0000269|PubMed:21685450}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:28319136};
Note=Binds 1 Zn(2+) ion per subunit. Absence of the Zn(2+) (in a
residue 1-80 fragment) does not prevent interaction with SigW, nor
does it change the overall conformation of RsiW, although a
disulfide bond can form between Cys-3 and Cys-37
(PubMed:28319136). {ECO:0000269|PubMed:28319136};
-!- SUBUNIT: Forms a heterodimer with cognate sigma factor SigW, which
probably prevents SigW from binding to DNA (PubMed:28319136).
{ECO:0000269|PubMed:28319136}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16899079};
Single-pass membrane protein {ECO:0000269|PubMed:16899079}.
Note=Site-2 clipped RsiW is released from the membrane to the
cytoplasm (PubMed:16899079). {ECO:0000269|PubMed:16899079}.
-!- INDUCTION: By different stresses causing damage to the cell
envelope, such as alkaline shock (PubMed:11454200), salt shock
(PubMed:11544224), phage infection and certain antibiotics that
affect cell wall biosynthesis (PubMed:12207695, PubMed:15870467).
{ECO:0000269|PubMed:11454200, ECO:0000269|PubMed:11544224,
ECO:0000269|PubMed:12207695, ECO:0000269|PubMed:15870467}.
-!- DOMAIN: The cytoplasmic domain is able to inactivate SigW and the
extracellular and transmembrane domains are crucial for sensing
and transducing the signal that triggers SigW activation
(PubMed:15130127). The N-terminus binds the zinc ion and is
followed by a long helix (about residues 40-80) that fits into a
hydrophobic surface groove on SigW, probably blocking its ability
to interact with the -10 and -35 promoter elements
(PubMed:28319136). {ECO:0000269|PubMed:15130127,
ECO:0000269|PubMed:28319136}.
-!- PTM: Is processed by successive proteolytic events. First, the
extracellular region of RsiW is cleaved by PrsW (site-1 cleavage)
in response to cell envelope stresses (PubMed:16816000,
PubMed:17020587). In a reconstituted E.coli system PrsW cuts
between Ala-168 and Ser-169 followed by trimming by E.coli Tsp;
the endogenous extracellular exopeptidase responsible for the
event in B.subtilis has not been identified (PubMed:19889088).
Next, it undergoes cleavage at an intramembrane site (site-2
cleavage) mediated by RasP (PubMed:15130127). This cleavage
uncovers a cryptic proteolytic tag with conserved alanine residues
in the transmembrane segment, that is recognized mainly by the
ClpXP protease, which completely degrades the protein in the
cytoplasm and leads to the induction of the sigma-W-controlled
genes (PubMed:16899079). {ECO:0000269|PubMed:15130127,
ECO:0000269|PubMed:16816000, ECO:0000269|PubMed:16899079,
ECO:0000269|PubMed:17020587, ECO:0000269|PubMed:19889088}.
-!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
superfamily. Anti-sigma-W factor family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA19508.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB002150; BAA19508.1; ALT_FRAME; Genomic_DNA.
EMBL; AL009126; CAB11950.1; -; Genomic_DNA.
PIR; G69744; G69744.
RefSeq; NP_388055.1; NC_000964.3.
RefSeq; WP_003234951.1; NZ_JNCM01000030.1.
PDB; 5WUQ; X-ray; 2.80 A; C/D=1-80.
PDB; 5WUR; X-ray; 2.60 A; C/D=1-80.
PDBsum; 5WUQ; -.
PDBsum; 5WUR; -.
ProteinModelPortal; Q45588; -.
SMR; Q45588; -.
IntAct; Q45588; 1.
STRING; 224308.Bsubs1_010100000993; -.
PaxDb; Q45588; -.
EnsemblBacteria; CAB11950; CAB11950; BSU01740.
GeneID; 938876; -.
KEGG; bsu:BSU01740; -.
PATRIC; fig|224308.179.peg.180; -.
eggNOG; COG5662; LUCA.
HOGENOM; HOG000261706; -.
InParanoid; Q45588; -.
OMA; YMASAGQ; -.
BioCyc; BSUB:BSU01740-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR027383; Znf_put.
Pfam; PF13490; zf-HC2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Membrane;
Metal-binding; Reference proteome; Stress response; Transcription;
Transcription regulation; Transmembrane; Transmembrane helix; Zinc.
CHAIN 1 208 Anti-sigma-W factor RsiW.
/FTId=PRO_0000097485.
TOPO_DOM 1 87 Cytoplasmic.
{ECO:0000305|PubMed:28319136}.
TRANSMEM 88 108 Helical. {ECO:0000255}.
TOPO_DOM 109 208 Extracellular. {ECO:0000255}.
METAL 3 3 Zinc. {ECO:0000269|PubMed:28319136}.
METAL 30 30 Zinc; via tele nitrogen.
{ECO:0000269|PubMed:28319136}.
METAL 34 34 Zinc. {ECO:0000269|PubMed:28319136}.
METAL 37 37 Zinc. {ECO:0000269|PubMed:28319136}.
MUTAGEN 26 40 VLNEHLETCEKCRKH->KFEHHFEECSPCLEK:
Partially inhibits SigW, confers low
diamide induction. A swap mutant with
RsrA of S.coelicolor.
{ECO:0000269|PubMed:21685450}.
MUTAGEN 91 94 AAAA->LLLL: Abolishes induction of sigma-
W-controlled genes.
{ECO:0000269|PubMed:16899079}.
MUTAGEN 91 93 AAA->LLL: Abolishes induction of sigma-W-
controlled genes.
{ECO:0000269|PubMed:16899079}.
MUTAGEN 91 92 AA->LL: Abolishes induction of sigma-W-
controlled genes.
{ECO:0000269|PubMed:16899079}.
MUTAGEN 91 91 A->L: No effect.
{ECO:0000269|PubMed:16899079}.
MUTAGEN 117 117 S->F: No longer requires PrsW for
degradation.
{ECO:0000269|PubMed:19889088}.
MUTAGEN 129 129 V->M: No longer requires PrsW for
degradation.
{ECO:0000269|PubMed:19889088}.
MUTAGEN 146 146 G->S: No longer requires PrsW for
degradation.
{ECO:0000269|PubMed:19889088}.
MUTAGEN 168 168 A->Q: Retains anti-sigma-W activity, not
degraded by PrsW.
{ECO:0000269|PubMed:19889088}.
MUTAGEN 169 169 S->Q: Wild-type; retains anti-sigma-W
activity, degraded by PrsW.
{ECO:0000269|PubMed:19889088}.
MUTAGEN 175 175 G->D: No longer requires PrsW for
degradation.
{ECO:0000269|PubMed:19889088}.
MUTAGEN 188 208 Missing: No longer requires PrsW for
degradation.
{ECO:0000269|PubMed:19889088}.
MUTAGEN 199 208 Missing: No longer requires PrsW for
degradation.
{ECO:0000269|PubMed:19889088}.
MUTAGEN 204 208 Missing: Requires PrsW for degradation.
{ECO:0000269|PubMed:19889088}.
HELIX 5 16 {ECO:0000244|PDB:5WUR}.
HELIX 21 33 {ECO:0000244|PDB:5WUR}.
HELIX 35 52 {ECO:0000244|PDB:5WUR}.
HELIX 63 69 {ECO:0000244|PDB:5WUR}.
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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