ID   SPLF_STAAS              Reviewed;         239 AA.
AC   Q6G8C4;
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 SplF;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splF; OrderedLocusNames=SAS1733;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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; BX571857; CAG43537.1; -; Genomic_DNA.
DR   RefSeq; WP_001038709.1; NC_002953.3.
DR   AlphaFoldDB; Q6G8C4; -.
DR   SMR; Q6G8C4; -.
DR   MEROPS; S01.526; -.
DR   KEGG; sas:SAS1733; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; KYEAIGV; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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; IPR028301; V8_his_AS.
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:0000250"
FT   CHAIN           37..239
FT                   /note="Serine protease SplF"
FT                   /id="PRO_0000359580"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        114
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        192
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   239 AA;  25609 MW;  06B94756E8C9A950 CRC64;
     MNKNIIIKSI AALTILTSIT GVGTTVVDGI QQTAKAENTV KQITNTNVAP YSGVTWMGAG
     TGFVVGNHTI ITNKHVTYHM KVGDEIKAHP NGFYNNGGGL YKVTKIVDYP GKEDIAVVQV
     EEKSTQPKGR KFKDFTSKFN IASEAKENEP ISVIGYPNPN GNKLQMYEST GKVLSVNGNI
     VSSDAIIQPG SSGSPILNSK HEAIGVIYAG NKPSGESTRG FAVYFSPEIK KFIADNLDK