ID   SSPC_STAAC              Reviewed;         109 AA.
AC   Q5HH37;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, 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=SACOL1055;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW36520.1; -; Genomic_DNA.
DR   RefSeq; WP_000284457.1; NC_002951.2.
DR   AlphaFoldDB; Q5HH37; -.
DR   SMR; Q5HH37; -.
DR   MEROPS; I57.001; -.
DR   EnsemblBacteria; AAW36520; AAW36520; SACOL1055.
DR   KEGG; sac:SACOL1055; -.
DR   HOGENOM; CLU_174854_0_0_9; -.
DR   OMA; NTSHNQY; -.
DR   Proteomes; UP000000530; 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_0000220554"
FT   REGION          97..101
FT                   /note="Binds to staphopain B"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   109 AA;  12882 MW;  A4D002333A614362 CRC64;
     MYQLQFINLV YDTTKLTHLE QTNINLFIGN WSNHQLQKSI CIRHGDDTSH NQYHILFIDT
     AHQRIKFSSI DNEEIIYILD YDDTQHILMQ TSSKQGIGTS RPIVYERLV