ID   SPLA_STAAC              Reviewed;         238 AA.
AC   Q5HEW0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Serine protease SplA;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splA; OrderedLocusNames=SACOL1869;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX   PubMed=11681202;
RX   DOI=10.1002/1615-9861(200104)1:4<480::aid-prot480>3.0.co;2-o;
RA   Ziebandt A.-K., Weber H., Rudolph J., Schmid R., Hoeper D., Engelmann S.,
RA   Hecker M.;
RT   "Extracellular proteins of Staphylococcus aureus and the role of SarA and
RT   sigma B.";
RL   Proteomics 1:480-493(2001).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Negatively regulated by sigma-B factor.
CC       {ECO:0000269|PubMed:11681202}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; CP000046; AAW36884.1; -; Genomic_DNA.
DR   RefSeq; WP_001039423.1; NC_002951.2.
DR   AlphaFoldDB; Q5HEW0; -.
DR   SMR; Q5HEW0; -.
DR   MEROPS; S01.503; -.
DR   EnsemblBacteria; AAW36884; AAW36884; SACOL1869.
DR   KEGG; sac:SACOL1869; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; NAQFEVV; -.
DR   Proteomes; UP000000530; 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   1: Evidence at protein level;
KW   Hydrolase; Protease; Secreted; Serine protease; Signal.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000250"
FT   CHAIN           39..238
FT                   /note="Serine protease SplA"
FT                   /id="PRO_0000359527"
FT   ACT_SITE        77
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        116
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        192
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   238 AA;  25876 MW;  2447A1AE0AE88432 CRC64;
     MNKNVMVKGL TALTILTILT SLGFAENISN QPHSIAKAEK NVKEITDATK EPYNSVVAFV
     GGTGVVVGKN TIVTNKHIAK SNDIFKNRVS AHHSSKGKGG GNYDVKDIVE YPGKEDLAIV
     HVHETSTEGL NFNKNVSYTK FADGAKVKDR ISVIGYPKGA QTKYKMFEST GTINHISGTF
     MEFDAYAQPG NSGSPVLNSK HELIGILYAG SGKDESEKNF GVYFTPQLKE FIQNNIEK