ID   SPLB_STAAB              Reviewed;         240 AA.
AC   Q2YTM3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Serine protease SplB;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splB; OrderedLocusNames=SAB1672c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI81361.1; -; Genomic_DNA.
DR   RefSeq; WP_001039452.1; NC_007622.1.
DR   AlphaFoldDB; Q2YTM3; -.
DR   SMR; Q2YTM3; -.
DR   MEROPS; S01.282; -.
DR   KEGG; sab:SAB1672c; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; NKYVLHE; -.
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_0000359538"
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;  26095 MW;  B83017FEBE0F2B67 CRC64;
     MNKNVVIKSL ATLTILTSVA GIGTTLVEEV QQTAKAENNV TKIKDTNIFP YTGVVAFNSA
     TGFVVGKNTI LTNKHVSKNY KVGDRITAHP NSDKSNGGIY SIKKIINYPG KEDVSVIKVE
     EHAIERGPKG FNFNDNVTPF KYAAGAKAGD RIKVIGYPHP YKNKYVLHES TGPVMSVEGS
     SIVYSAHTES GNSGSPVLNS NNELVGIHFA SDVKNDDNRN AYGVYFTPEI KRFIAENIDK