ID   SPLC_STAAR              Reviewed;         239 AA.
AC   Q6GFN8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Serine protease SplC;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splC; OrderedLocusNames=SAR1906;
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG40893.1; -; Genomic_DNA.
DR   RefSeq; WP_001039022.1; NC_002952.2.
DR   AlphaFoldDB; Q6GFN8; -.
DR   SMR; Q6GFN8; -.
DR   MEROPS; S01.283; -.
DR   KEGG; sar:SAR1906; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; DYPGNED; -.
DR   OrthoDB; 1468733at2; -.
DR   Proteomes; UP000000596; 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_0000359554"
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;  26062 MW;  4E37005D230140A8 CRC64;
     MNKNLVIKSM AALAILTSVT GISAAVVEET QQIAKAEKHV TQVKDTNVFP YHGVVAFKDA
     TGFVIGKNTI ITNKHVSKDY KVGDRITAHP NGDKGNGGIY KIKSISDYPG NEDISVMNIE
     EQAVERGSNG FNFNDNVQAF KFAKDAKVDD KIKVIGYPLP AQNSFKQFES TGTIKRIKDN
     ILNFDAYIEP GNSGSPVLNS NNEVIGVVYG GIGKVGSEYN GAVYFTPQIK DFIQKHIEQ