ID   SPLF_STAA8              Reviewed;         239 AA.
AC   Q2FXC8; Q9KH46;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Serine protease SplF;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splF; OrderedLocusNames=SAOUHSC_01935;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 37-53, SUBCELLULAR
RP   LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=11179322; DOI=10.1128/iai.69.3.1521-1527.2001;
RA   Reed S.B., Wesson C.A., Liou L.E., Trumble W.R., Schlievert P.M.,
RA   Bohach G.A., Bayles K.W.;
RT   "Molecular characterization of a novel Staphylococcus aureus serine
RT   protease operon.";
RL   Infect. Immun. 69:1521-1527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11179322}.
CC   -!- DEVELOPMENTAL STAGE: Maximally expressed during early stationary phase.
CC       {ECO:0000269|PubMed:11179322}.
CC   -!- INDUCTION: Positively regulated by agr (accessory gene regulator).
CC       {ECO:0000269|PubMed:11179322}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; AF271715; AAF97930.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD30998.1; -; Genomic_DNA.
DR   RefSeq; WP_001038688.1; NZ_LS483365.1.
DR   RefSeq; YP_500436.1; NC_007795.1.
DR   PDB; 6SF7; X-ray; 1.70 A; A/B/C/D=37-239.
DR   PDBsum; 6SF7; -.
DR   AlphaFoldDB; Q2FXC8; -.
DR   SMR; Q2FXC8; -.
DR   STRING; 1280.SAXN108_1841; -.
DR   MEROPS; S01.526; -.
DR   EnsemblBacteria; ABD30998; ABD30998; SAOUHSC_01935.
DR   GeneID; 3921019; -.
DR   KEGG; sao:SAOUHSC_01935; -.
DR   PATRIC; fig|93061.5.peg.1762; -.
DR   eggNOG; COG3591; Bacteria.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; KYEAIGV; -.
DR   PRO; PR:Q2FXC8; -.
DR   Proteomes; UP000008816; 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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000269|PubMed:11179322"
FT   CHAIN           37..239
FT                   /note="Serine protease SplF"
FT                   /id="PRO_0000359585"
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