ID   SPLB_STAAT              Reviewed;         240 AA.
AC   A8Z4N8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Serine protease SplB;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splB; OrderedLocusNames=USA300HOU_1805;
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   -!- 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; CP000730; ABX29808.1; -; Genomic_DNA.
DR   RefSeq; WP_001039447.1; NC_010079.1.
DR   AlphaFoldDB; A8Z4N8; -.
DR   SMR; A8Z4N8; -.
DR   MEROPS; S01.282; -.
DR   KEGG; sax:USA300HOU_1805; -.
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_0000359549"
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