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SPLB_STAAE
ID   SPLB_STAAE              Reviewed;         240 AA.
AC   A6QHZ5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Serine protease SplB;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splB; OrderedLocusNames=NWMN_1705;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
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; AP009351; BAF67977.1; -; Genomic_DNA.
DR   RefSeq; WP_001039447.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QHZ5; -.
DR   SMR; A6QHZ5; -.
DR   MEROPS; S01.282; -.
DR   EnsemblBacteria; BAF67977; BAF67977; NWMN_1705.
DR   KEGG; sae:NWMN_1705; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; NKYVLHE; -.
DR   Proteomes; UP000006386; 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_0000359548"
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
 
 
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