ID   SPLD_STAAC              Reviewed;         239 AA.
AC   Q5HEW3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Serine protease SplD;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splD; OrderedLocusNames=SACOL1866;
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; AAW36881.1; -; Genomic_DNA.
DR   RefSeq; WP_001038708.1; NC_002951.2.
DR   AlphaFoldDB; Q5HEW3; -.
DR   SMR; Q5HEW3; -.
DR   MEROPS; S01.526; -.
DR   EnsemblBacteria; AAW36881; AAW36881; SACOL1866.
DR   KEGG; sac:SACOL1866; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; AQNENTM; -.
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:0000255"
FT   CHAIN           37..239
FT                   /note="Serine protease SplD"
FT                   /id="PRO_0000359564"
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;  25669 MW;  BE539687FB6C9946 CRC64;
     MNKNIIIKSI AALTILTSIT GVGTTVVDGI QQTAKAENSV KLITNTNVAP YSGVTWMGAG
     TGFVVGNQTI ITNKHVTYHM KVGDEIKAHP NGFYNNGGGL YKVTKIVDYP GKEDIAVVQV
     EEKSTQPKGR KFKDFTSKFN IASEAKENEP ISVIGYPNPN GNKLQMYEST GKVLSVNGNI
     VTSDAVVQPG SSGSPILNSK REAIGVMYAS DKPTGESTRS FAVYFSPEIK KFIADNLDK