ID   SPLF_STAAC              Reviewed;         239 AA.
AC   Q5HEW5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Serine protease SplF;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splF; OrderedLocusNames=SACOL1864;
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; AAW36879.1; -; Genomic_DNA.
DR   RefSeq; WP_001038688.1; NC_002951.2.
DR   AlphaFoldDB; Q5HEW5; -.
DR   SMR; Q5HEW5; -.
DR   MEROPS; S01.526; -.
DR   EnsemblBacteria; AAW36879; AAW36879; SACOL1864.
DR   KEGG; sac:SACOL1864; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; KYEAIGV; -.
DR   Proteomes; UP000000530; Chromosome.
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_0000359579"
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;  25655 MW;  5DF3595DD2C91990 CRC64;
     MNKNIIIKSI AALTILTSIT GVGTTMVEGI QQTAKAENTV KQITNTNVAP YSGVTWMGAG
     TGFVVGNHTI ITNKHVTYHM KVGDEIKAHP NGFYNNGGGL YKVTKIVDYP GKEDIAVVQV
     EEKSTQPKGR KFKDFTSKFN IASEAKENEP ISVIGYPNPN GNKLQMYEST GKVLSVNGNI
     VSSDAIIQPG SSGSPILNSK HEAIGVIYAG NKPSGESTRG FAVYFSPEIK KFIADNLDK