ID   RSIW_GEOKA              Reviewed;         203 AA.
AC   Q5L3P4;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Anti-sigma-W factor RsiW;
GN   Name=rsiW; OrderedLocusNames=GK0151;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD74436.1; -; Genomic_DNA.
DR   RefSeq; WP_011229663.1; NC_006510.1.
DR   AlphaFoldDB; Q5L3P4; -.
DR   SMR; Q5L3P4; -.
DR   STRING; 235909.GK0151; -.
DR   EnsemblBacteria; BAD74436; BAD74436; GK0151.
DR   KEGG; gka:GK0151; -.
DR   eggNOG; COG5662; Bacteria.
DR   HOGENOM; CLU_1347302_0_0_9; -.
DR   OMA; YMASAGQ; -.
DR   Proteomes; UP000001172; 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..203
FT                   /note="Anti-sigma-W factor RsiW"
FT                   /id="PRO_0000248142"
FT   TOPO_DOM        1..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..203
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   203 AA;  22693 MW;  F610D6C9D43339AE CRC64;
     MECPKEIVLL MHSYFDGDLQ PEGEQQLKEH LRSCAACAAH FHELKKTVAF LQYAAHVAAP
     PSFAAKVMEA MPKERKTARL RRFLHRHPLL TAASLFLALT LGSLASSWGE RGAFSVSADE
     HVIIRDHTVI VPKGETVKGD IVVRNGSIRI EGTVDGDVTV IHGKKYMASA GQVTGEVEEI
     NQVFEWIWYN IKERFNRALQ SIE