ID   SPLE_STAAR              Reviewed;         238 AA.
AC   Q6GFP0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Serine protease SplE;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splE; OrderedLocusNames=SAR1902;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG40890.1; -; Genomic_DNA.
DR   RefSeq; WP_001038734.1; NC_002952.2.
DR   AlphaFoldDB; Q6GFP0; -.
DR   SMR; Q6GFP0; -.
DR   MEROPS; S01.312; -.
DR   KEGG; sar:SAR1902; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; MEIGEHI; -.
DR   OrthoDB; 1682439at2; -.
DR   Proteomes; UP000000596; 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_0000359574"
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;  25722 MW;  B5E11E593683BA16 CRC64;
     MNKNIIIKSI AALTILTSVT GVGTTMVEGI QQTAKAEHNV KLIKNTNVAP YNGIVSIGSG
     TGFIVGKNTI VTNKHVVAGM EIGAHIIAHP NGEYNNGGFY KVKKIVRYAG KEDIAILHVE
     DKAVHPKNRN FKDYTGILKI ASEAKENERI SIVGYPEPYI NKFQMYESTG KVLSVKGNMI
     ISDAFVEPGN SGSAVFNSKY EVVGVHFGGN GPANKSTKGY GVYFSPEIKK FIADNLDK