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