ID   RSIW_ALKHC              Reviewed;         213 AA.
AC   Q9KG49;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Anti-sigma-W factor RsiW;
GN   Name=rsiW; OrderedLocusNames=BH0264;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: Is the anti-sigma factor for SigW. The presence of RsiW leads
CC       to the inactivation of SigW, and its proteolytic destruction to sigma-W
CC       activation (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC       Note=Site-2 clipped RsiW is released from the membrane to the
CC       cytoplasm. {ECO:0000250}.
CC   -!- PTM: Is processed by three successive proteolytic events. First, the
CC       extracellular region of RsiW is cleaved by PrsW (Site-1 cleavage) in
CC       response to cell envelope stresses. Next, it undergoes cleavage at an
CC       intramembrane site (Site-2 cleavage) mediated by RasP. This cleavage
CC       uncovers a cryptic proteolytic tag with conserved alanine residues in
CC       the transmembrane segment, that is recognized mainly by the ClpXP
CC       protease, which completely degrades the protein in the cytoplasm and
CC       leads to the induction of the sigma-W-controlled genes (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
CC       superfamily. Anti-sigma-W factor family. {ECO:0000305}.
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DR   EMBL; BA000004; BAB03983.1; -; Genomic_DNA.
DR   PIR; H83682; H83682.
DR   RefSeq; WP_010896446.1; NC_002570.2.
DR   AlphaFoldDB; Q9KG49; -.
DR   SMR; Q9KG49; -.
DR   STRING; 272558.10172876; -.
DR   EnsemblBacteria; BAB03983; BAB03983; BAB03983.
DR   KEGG; bha:BH0264; -.
DR   eggNOG; COG5662; Bacteria.
DR   HOGENOM; CLU_1347302_0_0_9; -.
DR   OMA; YMASAGQ; -.
DR   OrthoDB; 1494577at2; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1320; -; 1.
DR   InterPro; IPR041916; Anti_sigma_zinc_sf.
DR   InterPro; IPR027383; Znf_put.
DR   Pfam; PF13490; zf-HC2; 1.
PE   3: Inferred from homology;
KW   Membrane; Metal-binding; Reference proteome; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..213
FT                   /note="Anti-sigma-W factor RsiW"
FT                   /id="PRO_0000248140"
FT   TOPO_DOM        1..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..213
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  23947 MW;  DDFEF67BFC1EE911 CRC64;
     MSCEQHYRTL IDKYIDGEAT AEERQELNEH LETCDACFEY MLEVRKVVAF VQSASHVQAP
     EGFTENVMKN LPKRKQTNRF KVWMRRYPLA VAAAVFVLLM STSLFSMWSS DGEHVTVTGT
     GNVSIDQESG RVIVPEGEVI QGDLVVRNGE LIIEGEVQGN VLLVNSSQYL ASPGSVSGEI
     DEVNQILDWI WYHTKKFLTK VIDISDEKNS PSS