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   16-JUN-2009, entry version 18.
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; Bacillales; Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 67-85,
RP   FUNCTION, ENZYME REGULATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 14990 / DSM 20044 / CIP 81.55;
RX   MEDLINE=22126649; PubMed=12127798; DOI=10.1006/mpat.2002.0515;
RA   Ohara-Nemoto Y., Ikeda Y., Kobayashi M., Sasaki M., Tajika S.,
RA   Kimura S.;
RT   "Characterization and molecular cloning of a glutamyl endopeptidase
RT   from Staphylococcus epidermidis.";
RL   Microb. Pathog. 33:33-41(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-282, AND PROTEIN SEQUENCE OF
RP   67-96.
RC   STRAIN=6746;
RX   MEDLINE=21618051; 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
CC       carbonyl side of glutamic acid. Shows activity toward human
CC       fibronectin and type 1 collagen.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
CC   -!- ENZYME REGULATION: Inhibited by diisopropyl fluorophosphate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. Active from pH 6.0 to 9.0;
CC   -!- SUBUNIT: Monomer (Probable).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB096695; BAC24763.1; -; Genomic_DNA.
DR   EMBL; AJ305145; CAC27157.1; -; Genomic_DNA.
DR   HSSP; P09332; 1DT2.
DR   BRENDA; 3.4.21.19; 874.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000126; Pept_S1B_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR008256; Peptidase_S1B.
DR   InterPro; IPR008353; Peptidase_S1B_tx.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR01774; EXFOLTOXIN.
DR   PRINTS; PR00839; V8PROTEASE.
DR   PROSITE; PS00672; V8_HIS; FALSE_NEG.
DR   PROSITE; PS00673; V8_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Virulence; Zymogen.
FT   SIGNAL        1     27       Potential.
FT   PROPEP       28     66
FT                                /FTId=PRO_0000026896.
FT   CHAIN        67    282       Glutamyl endopeptidase.
FT                                /FTId=PRO_0000026897.
FT   ACT_SITE    117    117       Charge relay system (By similarity).
FT   ACT_SITE    159    159       Charge relay system (By similarity).
FT   ACT_SITE    235    235       Charge relay system (By similarity).
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
//