ID   SPLA_STAAM              Reviewed;         235 AA.
AC   Q99T60;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Serine protease SplA;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splA; OrderedLocusNames=SAV1813;
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; BAB57975.1; -; Genomic_DNA.
DR   RefSeq; WP_001039427.1; NC_002758.2.
DR   AlphaFoldDB; Q99T60; -.
DR   SMR; Q99T60; -.
DR   MEROPS; S01.503; -.
DR   PaxDb; Q99T60; -.
DR   EnsemblBacteria; BAB57975; BAB57975; SAV1813.
DR   KEGG; sav:SAV1813; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; NAQFEVV; -.
DR   PhylomeDB; Q99T60; -.
DR   BioCyc; SAUR158878:SAV_RS09735-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..35
FT                   /evidence="ECO:0000250"
FT   CHAIN           36..235
FT                   /note="Serine protease SplA"
FT                   /id="PRO_0000359530"
FT   ACT_SITE        74
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        189
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   235 AA;  25441 MW;  DE576B839B4A8682 CRC64;
     MNKNVMVKGL TALTILTSLG FAENISNQPH SIAKAEKNVK EITDATKAPY NSVVAFAGGT
     GVVVGKNTIV TNKHIAKSND IFKNRVAAHY SSKGKGGGNY DVKDIVEYPG KEDLAIVHVH
     ETSTEGLNFN KNVSYTKFAE GAKAKDRISV IGYPKGAQTK YKMFESTGTI NHISGTFIEF
     DAYAQPGNSG SPVLNSKHEL IGILYAGSGK DESEKNFGVY FTPQLKEFIQ NNIEK