ID   SPLE_STAAT              Reviewed;         238 AA.
AC   A8Z4N5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Serine protease SplE;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splE; OrderedLocusNames=USA300HOU_1802;
OS   Staphylococcus aureus (strain USA300 / TCH1516).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=451516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300 / TCH1516;
RX   PubMed=17986343; DOI=10.1186/1471-2180-7-99;
RA   Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S.,
RA   Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O.,
RA   Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M.,
RA   Hemphill L., Ding Y., Dugan S., Blyth P.R., Buhay C.J., Dinh H.H.,
RA   Hawes A.C., Holder M., Kovar C.L., Lee S.L., Liu W., Nazareth L.V.,
RA   Wang Q., Zhou J., Kaplan S.L., Weinstock G.M.;
RT   "Subtle genetic changes enhance virulence of methicillin resistant and
RT   sensitive Staphylococcus aureus.";
RL   BMC Microbiol. 7:99-99(2007).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; CP000730; ABX29805.1; -; Genomic_DNA.
DR   RefSeq; WP_001038759.1; NC_010079.1.
DR   AlphaFoldDB; A8Z4N5; -.
DR   SMR; A8Z4N5; -.
DR   MEROPS; S01.312; -.
DR   KEGG; sax:USA300HOU_1802; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; MEIGEHI; -.
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_0000359577"
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;  25679 MW;  66CA24C37613EBA4 CRC64;
     MNKNIIIKSI AALTILTSVT GVGTTVVEGI QQTAKAEHNV KLIKNTNVAP YNGVVSIGSG
     TGFIVGKNTI VTNKHVVAGM EIGAHIIAHP NGEYNNGGFY KVKKIVRYSG QEDIAILHVE
     DKAVHPKNRN FKDYTGILKI ASEAKENERI SIVGYPEPYI NKFQMYESTG KVLSVKGNMI
     ITDAFVEPGN SGSAVFNSKY EVVGVHFGGN GPGNKSTKGY GVYFSPEIKK FIADNTDK