ID   SSPC_STAAR              Reviewed;         109 AA.
AC   Q6GI36;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Staphostatin B;
DE   AltName: Full=Staphylococcal cysteine protease B inhibitor;
GN   Name=sspC; OrderedLocusNames=SAR1020;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Specifically inhibits the cysteine protease staphopain B
CC       (SspB) by blocking the active site of the enzyme. Probably required to
CC       protect cytoplasmic proteins from being degraded by prematurely
CC       activated/folded prostaphopain B. Also involved in growth capacity,
CC       viability and bacterial morphology (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a stable non-covalent complex with prematurely
CC       activated/folded SspB. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: Inactivated by staphylococcal serine protease (SspA).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I57 (SspC) family.
CC       {ECO:0000305}.
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DR   EMBL; BX571856; CAG40024.1; -; Genomic_DNA.
DR   RefSeq; WP_000284455.1; NC_002952.2.
DR   AlphaFoldDB; Q6GI36; -.
DR   SMR; Q6GI36; -.
DR   MEROPS; I57.001; -.
DR   KEGG; sar:SAR1020; -.
DR   HOGENOM; CLU_174854_0_0_9; -.
DR   OMA; NTSHNQY; -.
DR   OrthoDB; 1783741at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.310.10; -; 1.
DR   InterPro; IPR016085; Protease_inh_b-brl_dom.
DR   InterPro; IPR037296; Staphostatin_A/B.
DR   InterPro; IPR015113; Staphostatin_B.
DR   Pfam; PF09023; Staphostatin_B; 1.
DR   SUPFAM; SSF50882; SSF50882; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Protease inhibitor; Thiol protease inhibitor; Virulence.
FT   CHAIN           1..109
FT                   /note="Staphostatin B"
FT                   /id="PRO_0000220557"
FT   REGION          97..101
FT                   /note="Binds to staphopain B"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   109 AA;  12916 MW;  A823C1333A61436B CRC64;
     MYQLQFINLV YDTTKLTHLE QTNINLFIGN WSNHQLQKSI CIRHGDDTSH NQYHILFIDT
     AHQRIKFSSF DNEEIIYILD YDDTQHILMQ TSSKQGIGTS RPIVYERLV