ID   RSIW_BACLD              Reviewed;         206 AA.
AC   Q65P50; Q62ZI9;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Anti-sigma-W factor RsiW;
GN   Name=rsiW; OrderedLocusNames=BLi00200, BL02700;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(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; AE017333; AAU39164.1; -; Genomic_DNA.
DR   EMBL; CP000002; AAU21819.1; -; Genomic_DNA.
DR   RefSeq; WP_003178441.1; NC_006322.1.
DR   AlphaFoldDB; Q65P50; -.
DR   SMR; Q65P50; -.
DR   STRING; 279010.BL02700; -.
DR   EnsemblBacteria; AAU21819; AAU21819; BL02700.
DR   GeneID; 66217654; -.
DR   KEGG; bld:BLi00200; -.
DR   KEGG; bli:BL02700; -.
DR   eggNOG; COG5662; Bacteria.
DR   HOGENOM; CLU_1347302_0_0_9; -.
DR   OMA; YMASAGQ; -.
DR   OrthoDB; 1494577at2; -.
DR   BioCyc; BLIC279010:BLI_RS01000-MON; -.
DR   Proteomes; UP000000606; Chromosome.
DR   Bgee; BL02700; Expressed in testis.
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..206
FT                   /note="Anti-sigma-W factor RsiW"
FT                   /id="PRO_0000248141"
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..206
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   206 AA;  22828 MW;  33D87246BC9DE224 CRC64;
     MSCPEHIVQL MHKYLDGDIL PEDETRLKEH LQSCEGCKKH LHEMEKSIAL VQSTSHLTAP
     ANFTANVLAN LPKEKRTASI NRWLKAHPFL VAAALFAILM GGSFFSSWKN DHDFSVSSQP
     NLVVKNNTVI VPEGEVVKGD VTVKNGKLII EGKVDGDVTI VNGEKYTASA GQVTGQIHEI
     NEVFDWIWYK IKSTGKSVFG VKESKE