ID   GSEA_STAES              Reviewed;         282 AA.
AC   P0C0Q2; 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 25.
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; OrderedLocusNames=SE_1543;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22832016; PubMed=12950922;
RX   DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S1B family.
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DR   EMBL; AE015929; AAO05142.1; -; Genomic_DNA.
DR   RefSeq; NP_765098.1; -.
DR   HSSP; P09332; 1DT2.
DR   MEROPS; S01.269; -.
DR   GeneID; 1055780; -.
DR   GenomeReviews; AE015929_GR; SE_1543.
DR   KEGG; sep:SE1543; -.
DR   HOGENOM; P0C0Q2; -.
DR   OMA; P0C0Q2; EDINFAN.
DR   BioCyc; SEPI176280:SE_1543-MON; -.
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   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Protease; Secreted; Serine protease;
KW   Signal; Virulence; Zymogen.
FT   SIGNAL        1     27       Potential.
FT   PROPEP       28     66       By similarity.
FT                                /FTId=PRO_0000042921.
FT   CHAIN        67    282       Glutamyl endopeptidase.
FT                                /FTId=PRO_0000042922.
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
//