ID   SSPC_STAAW              Reviewed;         109 AA.
AC   Q7A189;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Staphostatin B;
DE   AltName: Full=Staphylococcal cysteine protease B inhibitor;
GN   Name=sspC; OrderedLocusNames=MW0930;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX   PubMed=14500882; DOI=10.1110/ps.03247703;
RA   Rzychon M., Filipek R., Sabat A., Kosowska K., Dubin A., Potempa J.,
RA   Bochtler M.;
RT   "Staphostatins resemble lipocalins, not cystatins in fold.";
RL   Protein Sci. 12:2252-2256(2003).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RA   Brown C.K., Gu Z.-Y., Nickerson N., McGavin M.J., Ohlendorf D.H.,
RA   Earhart C.A.;
RT   "Crystal structure of a staphylococcal inhibitor/chaperone.";
RL   Submitted (FEB-2004) to the PDB data bank.
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   -!- DOMAIN: N-terminal residues are not required for inhibitory activity.
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; BA000033; BAB94795.1; -; Genomic_DNA.
DR   RefSeq; WP_000284457.1; NC_003923.1.
DR   PDB; 1NYC; X-ray; 1.40 A; A/B=1-109.
DR   PDB; 1QWX; X-ray; 1.50 A; A/B=1-109.
DR   PDBsum; 1NYC; -.
DR   PDBsum; 1QWX; -.
DR   AlphaFoldDB; Q7A189; -.
DR   SMR; Q7A189; -.
DR   MEROPS; I57.001; -.
DR   EnsemblBacteria; BAB94795; BAB94795; BAB94795.
DR   KEGG; sam:MW0930; -.
DR   HOGENOM; CLU_174854_0_0_9; -.
DR   OMA; NTSHNQY; -.
DR   EvolutionaryTrace; Q7A189; -.
DR   Proteomes; UP000000418; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Protease inhibitor; Thiol protease inhibitor;
KW   Virulence.
FT   CHAIN           1..109
FT                   /note="Staphostatin B"
FT                   /id="PRO_0000220559"
FT   REGION          97..101
FT                   /note="Binds to staphopain B"
FT                   /evidence="ECO:0000250"
FT   STRAND          2..10
FT                   /evidence="ECO:0007829|PDB:1NYC"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:1NYC"
FT   HELIX           18..25
FT                   /evidence="ECO:0007829|PDB:1NYC"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:1NYC"
FT   TURN            34..37
FT                   /evidence="ECO:0007829|PDB:1NYC"
FT   STRAND          38..45
FT                   /evidence="ECO:0007829|PDB:1NYC"
FT   STRAND          50..59
FT                   /evidence="ECO:0007829|PDB:1NYC"
FT   TURN            60..63
FT                   /evidence="ECO:0007829|PDB:1NYC"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:1NYC"
FT   STRAND          72..83
FT                   /evidence="ECO:0007829|PDB:1NYC"
FT   STRAND          86..97
FT                   /evidence="ECO:0007829|PDB:1NYC"
FT   STRAND          103..107
FT                   /evidence="ECO:0007829|PDB:1NYC"
SQ   SEQUENCE   109 AA;  12882 MW;  A4D002333A614362 CRC64;
     MYQLQFINLV YDTTKLTHLE QTNINLFIGN WSNHQLQKSI CIRHGDDTSH NQYHILFIDT
     AHQRIKFSSI DNEEIIYILD YDDTQHILMQ TSSKQGIGTS RPIVYERLV