ID   RSIW_ALKCK              Reviewed;         221 AA.
AC   Q5WLH2;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Anti-sigma-W factor RsiW;
GN   Name=rsiW; OrderedLocusNames=ABC0240;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD62783.1; -; Genomic_DNA.
DR   RefSeq; WP_011245103.1; NC_006582.1.
DR   AlphaFoldDB; Q5WLH2; -.
DR   SMR; Q5WLH2; -.
DR   STRING; 66692.ABC0240; -.
DR   EnsemblBacteria; BAD62783; BAD62783; ABC0240.
DR   KEGG; bcl:ABC0240; -.
DR   eggNOG; COG5662; Bacteria.
DR   HOGENOM; CLU_1347302_0_0_9; -.
DR   OMA; YMASAGQ; -.
DR   OrthoDB; 1494577at2; -.
DR   Proteomes; UP000001168; 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..221
FT                   /note="Anti-sigma-W factor RsiW"
FT                   /id="PRO_0000248139"
FT   TOPO_DOM        1..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..221
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   221 AA;  24429 MW;  C45EA8A5B38F70AE CRC64;
     MKTCHSHDEL IHIYLDGDAT KEQKEELYAH LQSCPSCREH LQELKKSIAF IQSSSHIEAP
     EGFTAGVMAK LPKTKKTAKW KLKAKRHPIL VAAAIFLIMM SAAFFSAWSH TTDGIAVSGN
     GPFVIDKEAG VVVVPEGEVI DGDLVVRNGT LVLEGEVRGN VLLINSRFNK DTLYASPNQV
     TGEIEEVDKA LSWAWYNMKE FFNEVVAVFD AGEDDPHSTD N