ID   SPLB_STAA3              Reviewed;         240 AA.
AC   Q2FFT0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Serine protease SplB;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splB; OrderedLocusNames=SAUSA300_1757;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
CC   -!- FUNCTION: Serine protease that cleaves specifically after the sequence
CC       Trp-Glu-Leu-Gln. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; CP000255; ABD22137.1; -; Genomic_DNA.
DR   RefSeq; WP_001039447.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FFT0; -.
DR   SMR; Q2FFT0; -.
DR   MEROPS; S01.282; -.
DR   PRIDE; Q2FFT0; -.
DR   EnsemblBacteria; ABD22137; ABD22137; SAUSA300_1757.
DR   KEGG; saa:SAUSA300_1757; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; NKYVLHE; -.
DR   Proteomes; UP000001939; Chromosome.
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:0000250"
FT   CHAIN           37..240
FT                   /note="Serine protease SplB"
FT                   /id="PRO_0000359550"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FXC3"
FT   ACT_SITE        113
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FXC3"
FT   ACT_SITE        193
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FXC3"
SQ   SEQUENCE   240 AA;  26097 MW;  00A3349F1FE5D52E CRC64;
     MNKNVVIKSL AALTILTSVT GIGTTLVEEV QQTAKAENNV TKVKDTNIFP YTGVVAFKSA
     TGFVVGKNTI LTNKHVSKNY KVGDRITAHP NSDKGNGGIY SIKKIINYPG KEDVSVIQVE
     ERAIERGPKG FNFNDNVTPF KYAAGAKAGE RIKVIGYPHP YKNKYVLYES TGPVMSVEGS
     SIVYSAHTES GNSGSPVLNS NNELVGIHFA SDVKNDDNRN AYGVYFTPEI KKFIAENIDK