ID   SPLE_STAAC              Reviewed;         238 AA.
AC   Q5HEW4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Serine protease SplE;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splE; OrderedLocusNames=SACOL1865;
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).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; CP000046; AAW36880.1; -; Genomic_DNA.
DR   RefSeq; WP_001038759.1; NC_002951.2.
DR   AlphaFoldDB; Q5HEW4; -.
DR   SMR; Q5HEW4; -.
DR   MEROPS; S01.312; -.
DR   EnsemblBacteria; AAW36880; AAW36880; SACOL1865.
DR   KEGG; sac:SACOL1865; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; MEIGEHI; -.
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   3: Inferred from homology;
KW   Hydrolase; Protease; Secreted; Serine protease; Signal.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..238
FT                   /note="Serine protease SplE"
FT                   /id="PRO_0000359573"
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        191
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   238 AA;  25679 MW;  66CA24C37613EBA4 CRC64;
     MNKNIIIKSI AALTILTSVT GVGTTVVEGI QQTAKAEHNV KLIKNTNVAP YNGVVSIGSG
     TGFIVGKNTI VTNKHVVAGM EIGAHIIAHP NGEYNNGGFY KVKKIVRYSG QEDIAILHVE
     DKAVHPKNRN FKDYTGILKI ASEAKENERI SIVGYPEPYI NKFQMYESTG KVLSVKGNMI
     ITDAFVEPGN SGSAVFNSKY EVVGVHFGGN GPGNKSTKGY GVYFSPEIKK FIADNTDK