ID   GSEA_STAEP              Reviewed;         282 AA.
AC   P0C0Q1; Q7DG19; Q8CMC1; Q9AJX0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Glutamyl endopeptidase;
DE            EC=3.4.21.19;
DE   AltName: Full=Glutamic acid-specific protease;
DE            Short=GluSE;
DE   Flags: Precursor;
GN   Name=gseA; Synonyms=esp;
OS   Staphylococcus epidermidis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 67-85, FUNCTION,
RP   ACTIVITY REGULATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 14990 / DSM 20044 / CIP 81.55 / NCTC 11047;
RX   PubMed=12127798; DOI=10.1006/mpat.2002.0515;
RA   Ohara-Nemoto Y., Ikeda Y., Kobayashi M., Sasaki M., Tajika S., Kimura S.;
RT   "Characterization and molecular cloning of a glutamyl endopeptidase from
RT   Staphylococcus epidermidis.";
RL   Microb. Pathog. 33:33-41(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-282, AND PROTEIN SEQUENCE OF 67-96.
RC   STRAIN=6746;
RX   PubMed=11767947; DOI=10.1515/bc.2001.192;
RA   Dubin G., Chmiel D., Mak P., Rakwalska M., Rzychon M., Dubin A.;
RT   "Molecular cloning and biochemical characterisation of proteases from
RT   Staphylcoccus epidermidis.";
RL   Biol. Chem. 382:1575-1582(2001).
CC   -!- FUNCTION: Exhibits a significant hydrolytic activity for the carbonyl
CC       side of glutamic acid. Shows activity toward human fibronectin and type
CC       1 collagen. {ECO:0000269|PubMed:12127798}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.; EC=3.4.21.19;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10083};
CC   -!- ACTIVITY REGULATION: Inhibited by diisopropyl fluorophosphate.
CC       {ECO:0000269|PubMed:12127798}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. Active from pH 6.0 to 9.0.;
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:12127798}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12127798}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; AB096695; BAC24763.1; -; Genomic_DNA.
DR   EMBL; AJ305145; CAC27157.1; -; Genomic_DNA.
DR   RefSeq; WP_001829860.1; NZ_WLVA01000001.1.
DR   AlphaFoldDB; P0C0Q1; -.
DR   SMR; P0C0Q1; -.
DR   MEROPS; S01.522; -.
DR   GeneID; 50018384; -.
DR   BRENDA; 3.4.21.19; 5875.
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; IPR000126; V8_ser_AS.
DR   PRINTS; PR01774; EXFOLTOXIN.
DR   PRINTS; PR00839; V8PROTEASE.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS00673; V8_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease;
KW   Signal; Virulence; Zymogen.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..66
FT                   /evidence="ECO:0000269|PubMed:11767947,
FT                   ECO:0000269|PubMed:12127798"
FT                   /id="PRO_0000026896"
FT   CHAIN           67..282
FT                   /note="Glutamyl endopeptidase"
FT                   /id="PRO_0000026897"
FT   ACT_SITE        117
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT   ACT_SITE        159
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT   ACT_SITE        235
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
SQ   SEQUENCE   282 AA;  30809 MW;  5DAD3E8D7EB3E0CB CRC64;
     MKKRFLSICT MTIAALATTT MVNTSYAKTD TESHNHSSLG TENKNVLDIN SSSHNIKPSQ
     NKSYPSVILP NNNRHQIFNT TQGHYDAVSF IYIPIDGGYM SGSGVVVGEN EILTNKHVVN
     GAKGNPRNIS VHPSAKNEND YPNGKFVGQE IIPYPGNSDL AILRVSPNEH NQHIGQVVKP
     ATISSNTDTR INENITVTGY PGDKPLATMW ESVGKVVYIG GEELRYDLST VGGNSGSPVF
     NGKNQVIGIH YGGVDNKYNS SVYINDFVQQ FLRNNIPDIN IQ