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SPLA_STAA1
ID   SPLA_STAA1              Reviewed;         235 AA.
AC   A7X3R0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Serine protease SplA;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splA; OrderedLocusNames=SAHV_1798;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; AP009324; BAF78681.1; -; Genomic_DNA.
DR   RefSeq; WP_001039427.1; NC_009782.1.
DR   AlphaFoldDB; A7X3R0; -.
DR   SMR; A7X3R0; -.
DR   MEROPS; S01.503; -.
DR   KEGG; saw:SAHV_1798; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; NAQFEVV; -.
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_0000359529"
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
 
 
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