ID   SPLC_STAAW              Reviewed;         239 AA.
AC   Q8NVX7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Serine protease SplC;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splC; OrderedLocusNames=MW1753;
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; BA000033; BAB95618.1; -; Genomic_DNA.
DR   RefSeq; WP_001038865.1; NC_003923.1.
DR   AlphaFoldDB; Q8NVX7; -.
DR   SMR; Q8NVX7; -.
DR   MEROPS; S01.283; -.
DR   EnsemblBacteria; BAB95618; BAB95618; BAB95618.
DR   KEGG; sam:MW1753; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; DYPGNED; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR008256; Peptidase_S1B.
DR   InterPro; IPR008353; Peptidase_S1B_tx.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR028301; V8_his_AS.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR01774; EXFOLTOXIN.
DR   PRINTS; PR00839; V8PROTEASE.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS00672; V8_HIS; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Secreted; Serine protease; Signal.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000250"
FT   CHAIN           37..239
FT                   /note="Serine protease SplC"
FT                   /id="PRO_0000359558"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        113
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        193
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   239 AA;  26065 MW;  6A59F6BAD548E437 CRC64;
     MNKNIVIKSM AALAILTSVT GINAAVVEET QQIANAEKNV TQVKDTNIFP YNGVVSFKDA
     TGFVIGKNTI ITNKHVSKDY KVGDRITAHP DGDKGNGGIY KIKSISDYPG DEDISVMNIE
     EQAVERGPKG FNFNENVQAL NFAKDAKVDD KIKVIGYPLP AQNSFKQFES TGTIKRIKDN
     ILNFDAYIEP GNSGSPVLNS NNEVIGVVYG GIGKIGSEYN GAVYFTPQIK DFIQKHIEQ