ID   SSPB_STAAW              Reviewed;         393 AA.
AC   Q8NX99;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Staphopain B;
DE            EC=3.4.22.-;
DE   AltName: Full=Staphylococcal cysteine proteinase B;
DE   AltName: Full=Staphylopain B;
DE   Flags: Precursor;
GN   Name=sspB; OrderedLocusNames=MW0931;
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).
CC   -!- FUNCTION: Cysteine protease that plays an important role in the
CC       inhibition of host innate immune response. Degrades host elastin,
CC       fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised
CC       S. aureus by neutrophils and monocytes by inducing their death in a
CC       proteolytic activity-dependent manner. Decreases surface expression of
CC       the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-
CC       3/LGALS3, thereby inhibiting the neutrophil-activating ability of the
CC       lectin. {ECO:0000250|UniProtKB:P0C1S6}.
CC   -!- ACTIVITY REGULATION: Prematurely activated/folded staphopain B is
CC       inhibited by staphostatin B (SspC), which is probably required to
CC       protect staphylococcal cytoplasmic proteins from degradation by SspB.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: In the cytoplasm, prematurely activated/folded SspB forms a
CC       stable non-covalent complex with SspC. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: Proteolytically cleaved by staphylococcal serine protease (SspA).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: The cascade of activation of extracellular proteases
CC       proceeds from the metalloprotease aureolysin (aur), through SspA to
CC       SspB. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C47 family. {ECO:0000305}.
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DR   EMBL; BA000033; BAB94796.1; -; Genomic_DNA.
DR   RefSeq; WP_001089097.1; NC_003923.1.
DR   AlphaFoldDB; Q8NX99; -.
DR   SMR; Q8NX99; -.
DR   MEROPS; C47.002; -.
DR   EnsemblBacteria; BAB94796; BAB94796; BAB94796.
DR   KEGG; sam:MW0931; -.
DR   HOGENOM; CLU_069043_0_0_9; -.
DR   OMA; SCKTRVF; -.
DR   PRO; PR:Q8NX99; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.500.10; -; 1.
DR   InterPro; IPR046350; Cystatin_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR008750; Peptidase_C47.
DR   InterPro; IPR028076; Staphopain_pro.
DR   InterPro; IPR037155; Staphopain_pro_sf.
DR   Pfam; PF05543; Peptidase_C47; 1.
DR   Pfam; PF14731; Staphopain_pro; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54403; SSF54403; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Secreted; Signal; Thiol protease; Virulence; Zymogen.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000250"
FT   PROPEP          37..219
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026571"
FT   CHAIN           220..393
FT                   /note="Staphopain B"
FT                   /id="PRO_0000026572"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        340
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        360
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   SITE            219..220
FT                   /note="Cleavage; by SspA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   393 AA;  44611 MW;  8BF34645BC810746 CRC64;
     MNSSYKSRVF NIISIIMVSM LILSLGAFAN NNKAKADSHS KQLEINVKSD KVPQKVKDLA
     QQQFAGYAKA LDKQSNAKTG KYELGEAFKI YKFNGEEDNS YYYPVIKDGK IVYTLTLSPK
     NKDDLNKSKE DMNYSVKISN FIAKDLDQIK DKNSNITVLT DEKGFYFEED GKVRLVKATP
     LPGNVKEKES AKTVSSKLKQ ELKNTVTPTK VEENEAIQED QVQYENTLKN FKIREQQFDN
     SWCAGFSMAA LLNATKNTDT YNAHDIMRTL YPEVSEQDLP NCSTFPNQMI EYGKSQGRDI
     HYQEGVPSYE QVDQLTKDNV GIMILAQSVS QNPNDPHLGH ALAVVGNAKI NDQEKLIYWN
     PWDTELSIQD ADSSLLHLSF NRDYNWYGSM IGY