ID   RSIW_OCEIH              Reviewed;         213 AA.
AC   Q8ETN0;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Anti-sigma-W factor RsiW;
GN   Name=rsiW; OrderedLocusNames=OB0229;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC12185.1; -; Genomic_DNA.
DR   RefSeq; WP_011064630.1; NC_004193.1.
DR   AlphaFoldDB; Q8ETN0; -.
DR   SMR; Q8ETN0; -.
DR   STRING; 221109.22775907; -.
DR   PRIDE; Q8ETN0; -.
DR   EnsemblBacteria; BAC12185; BAC12185; BAC12185.
DR   KEGG; oih:OB0229; -.
DR   eggNOG; COG5662; Bacteria.
DR   HOGENOM; CLU_1347302_0_0_9; -.
DR   OMA; YMASAGQ; -.
DR   OrthoDB; 1494577at2; -.
DR   Proteomes; UP000000822; 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_0000248143"
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..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;  23927 MW;  FECF775AF4916E4A CRC64;
     MSCSKDYLNL MHIYLDGDIT REDESKLSRH LEDCESCQKH FHELNRTITL MRSAERVEAP
     DGFTENVMAN LPSEKKTVKY RRWFKLHPMW TAAAIFLVLM AGGMISTWTH SSDQLVVSAQ
     NELIVDGDTV IVPAGVTVPG DVLVKNGDLL LLGTVDGDVT IFNGKILDND SEMNGEGLMA
     SVGGVNGELE TIDRMFEWIW YNIKNFFKGV FSF