SPLC_STAAU
ID SPLC_STAAU Reviewed; 239 AA.
AC Q53782;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Serine protease SplC;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=splC;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FDA 485;
RX PubMed=9048880; DOI=10.1016/s0167-4781(96)00216-3;
RA Rieneck K., Renneberg J., Diamant M., Gutschik E., Bendtzen K.;
RT "Molecular cloning and expression of a novel Staphylococcus aureus
RT antigen.";
RL Biochim. Biophys. Acta 1350:128-132(1997).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U63529; AAC12901.1; -; Genomic_DNA.
DR RefSeq; WP_001038872.1; NZ_WYDB01000002.1.
DR PDB; 2AS9; X-ray; 1.70 A; A/B=37-239.
DR PDBsum; 2AS9; -.
DR AlphaFoldDB; Q53782; -.
DR SMR; Q53782; -.
DR MEROPS; S01.283; -.
DR OMA; DYPGNED; -.
DR EvolutionaryTrace; Q53782; -.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Protease; Secreted; Serine protease; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000250"
FT CHAIN 37..239
FT /note="Serine protease SplC"
FT /id="PRO_0000359551"
FT ACT_SITE 75
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 113
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 239 AA; 26099 MW; A56BB3CDB77B29A9 CRC64;
MNKNIVIKSM AALAILTSVT GINAAVVEET QQIANAEKNV TQVKDTNNFP YNGVVSFKDA
TGFVIGKNTI ITNKHVSKDY KVGDRITAHP NGDKGNGGIY KIKSISDYPG DEDISVMNIE
EQAVERGPKG FNFNENVQAF NFAKDAKVDD KIKVIGYPLP AQNSFKQFES TGTIKRIKDN
ILNFDAYIEP GNSGSPVLNS NNEVIGVVYG GIGKIGSEYN GAVYFTPQIK DFIQKHIEQ