ID   GSEA_STAEQ              Reviewed;         282 AA.
AC   Q5HN75;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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; OrderedLocusNames=SERP1397;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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 (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.; EC=3.4.21.19;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10083};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; CP000029; AAW54738.1; -; Genomic_DNA.
DR   RefSeq; WP_010959202.1; NC_002976.3.
DR   AlphaFoldDB; Q5HN75; -.
DR   SMR; Q5HN75; -.
DR   STRING; 176279.SERP1397; -.
DR   MEROPS; S01.522; -.
DR   EnsemblBacteria; AAW54738; AAW54738; SERP1397.
DR   KEGG; ser:SERP1397; -.
DR   eggNOG; COG3591; Bacteria.
DR   HOGENOM; CLU_073589_1_0_9; -.
DR   OMA; NFANDDQ; -.
DR   OrthoDB; 1468733at2; -.
DR   Proteomes; UP000000531; 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; IPR000126; V8_ser_AS.
DR   PRINTS; PR01774; EXFOLTOXIN.
DR   PRINTS; PR00839; V8PROTEASE.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS00673; V8_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal;
KW   Virulence; Zymogen.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..66
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026898"
FT   CHAIN           67..282
FT                   /note="Glutamyl endopeptidase"
FT                   /id="PRO_0000026899"
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;  30831 MW;  5DA679C179F8A787 CRC64;
     MKKRFLSICT MTIAALATTT MVNTSYAKTD TESHNHSSLG TENKNVLDIN SSSHNIKPSQ
     NKSYPSVILP NNNRHQIFNT TQGHYDAVSF IYIPIHGGYM SGSGVVVGEN EILTNKHVVN
     GAKGNPRNIS VHPSAKNEND YPNGKFVGQE IIPYPGNSDL AILRVSPNEH NQHIGQVVKP
     ATISSNTDTR INENITVTGY PGDKPLATMW ESVGKVVYIG GEELRYDLST VGGNSGSPVF
     NGKNQVIGIH YGGVDNKYNS SVYINDFVQQ FLRNNIPDIN IQ