ID   SPLD_STAAM              Reviewed;         239 AA.
AC   Q7A2Q9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Serine protease SplD;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splD; OrderedLocusNames=SAV1810;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; BA000017; BAB57972.1; -; Genomic_DNA.
DR   RefSeq; WP_001038704.1; NC_002758.2.
DR   AlphaFoldDB; Q7A2Q9; -.
DR   SMR; Q7A2Q9; -.
DR   MEROPS; S01.526; -.
DR   KEGG; sav:SAV1810; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   PhylomeDB; Q7A2Q9; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR008256; Peptidase_S1B.
DR   InterPro; IPR028301; V8_his_AS.
DR   PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1.
DR   PANTHER; PTHR43019:SF62; SERINE ENDOPROTEASE DEGS; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00839; V8PROTEASE.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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..239
FT                   /note="Serine protease SplD"
FT                   /id="PRO_0000359566"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        114
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        192
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   239 AA;  25678 MW;  36B00B3C6108738A CRC64;
     MNKNIIIKSI AALTILTSIT GVGTTVVDGI QQTAKAENSV KLITNTNVAP YSGVTWMGAG
     TGFVVGNHTI ITNKHVTYHM KVGDEIKAHP NGFYNNGGGL YKVTKIVDYP GKEDIAVVQV
     EEKSTQPKGR KFKDFTSKFN IASEAKENEP ISVIGYPNPN GNKLQMYEST GKVLSVNGNI
     VTSDAVVQPG SSGSPILNSK REAIGVMYAS DKPTGESTRS FAVYFSPEIK KFIADNLDK
//