GSEA_STAES
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 03-AUG-2022, entry version 88.
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 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; 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., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA 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 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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR EMBL; AE015929; AAO05142.1; -; Genomic_DNA.
DR RefSeq; NP_765098.1; NC_004461.1.
DR RefSeq; WP_001829860.1; NZ_WBME01000083.1.
DR PDB; 4JCN; X-ray; 1.80 A; A=67-282.
DR PDB; 6PYM; X-ray; 1.20 A; A=67-282.
DR PDB; 6Q12; X-ray; 2.20 A; A/B=56-282.
DR PDB; 6Q24; X-ray; 1.85 A; A=56-282.
DR PDB; 6TYA; X-ray; 2.07 A; A=66-282.
DR PDB; 6U1B; X-ray; 2.08 A; A=59-282.
DR PDBsum; 4JCN; -.
DR PDBsum; 6PYM; -.
DR PDBsum; 6Q12; -.
DR PDBsum; 6Q24; -.
DR PDBsum; 6TYA; -.
DR PDBsum; 6U1B; -.
DR AlphaFoldDB; P0C0Q2; -.
DR SMR; P0C0Q2; -.
DR STRING; 176280.SE_1543; -.
DR MEROPS; S01.522; -.
DR EnsemblBacteria; AAO05142; AAO05142; SE_1543.
DR GeneID; 50018384; -.
DR KEGG; sep:SE_1543; -.
DR PATRIC; fig|176280.10.peg.1509; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_073589_1_0_9; -.
DR OMA; NFANDDQ; -.
DR Proteomes; UP000001411; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Protease; 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_0000042921"
FT CHAIN 67..282
FT /note="Glutamyl endopeptidase"
FT /id="PRO_0000042922"
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"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:6PYM"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6PYM"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:6PYM"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:6PYM"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:6PYM"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 209..220
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:6PYM"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:6PYM"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:6PYM"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:6PYM"
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
