ID   SPLC_STAAM              Reviewed;         239 AA.
AC   Q7A2Q8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Serine protease SplC;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splC; OrderedLocusNames=SAV1811;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; BA000017; BAB57973.1; -; Genomic_DNA.
DR   RefSeq; WP_001038872.1; NC_002758.2.
DR   AlphaFoldDB; Q7A2Q8; -.
DR   SMR; Q7A2Q8; -.
DR   MEROPS; S01.283; -.
DR   PaxDb; Q7A2Q8; -.
DR   DNASU; 1121785; -.
DR   EnsemblBacteria; BAB57973; BAB57973; SAV1811.
DR   KEGG; sav:SAV1811; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; DYPGNED; -.
DR   PhylomeDB; Q7A2Q8; -.
DR   BioCyc; SAUR158878:SAV_RS09725-MON; -.
DR   Proteomes; UP000002481; 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_0000359557"
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;  26099 MW;  A56BB3CDB77B29A9 CRC64;
     MNKNIVIKSM AALAILTSVT GINAAVVEET QQIANAEKNV TQVKDTNNFP YNGVVSFKDA
     TGFVIGKNTI ITNKHVSKDY KVGDRITAHP NGDKGNGGIY KIKSISDYPG DEDISVMNIE
     EQAVERGPKG FNFNENVQAF NFAKDAKVDD KIKVIGYPLP AQNSFKQFES TGTIKRIKDN
     ILNFDAYIEP GNSGSPVLNS NNEVIGVVYG GIGKIGSEYN GAVYFTPQIK DFIQKHIEQ