PEPE_ECOSM
ID PEPE_ECOSM Reviewed; 229 AA.
AC B1LPH7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Peptidase E {ECO:0000255|HAMAP-Rule:MF_00510};
DE EC=3.4.13.21 {ECO:0000255|HAMAP-Rule:MF_00510};
DE AltName: Full=Alpha-aspartyl dipeptidase {ECO:0000255|HAMAP-Rule:MF_00510};
DE AltName: Full=Asp-specific dipeptidase {ECO:0000255|HAMAP-Rule:MF_00510};
DE AltName: Full=Dipeptidase E {ECO:0000255|HAMAP-Rule:MF_00510};
GN Name=pepE {ECO:0000255|HAMAP-Rule:MF_00510};
GN OrderedLocusNames=EcSMS35_4474;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
CC -!- FUNCTION: Hydrolyzes dipeptides containing N-terminal aspartate
CC residues. May play a role in allowing the cell to use peptide aspartate
CC to spare carbon otherwise required for the synthesis of the aspartate
CC family of amino acids. {ECO:0000255|HAMAP-Rule:MF_00510}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-
CC Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor
CC does it cleave isoaspartyl peptides.; EC=3.4.13.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00510};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00510}.
CC -!- SIMILARITY: Belongs to the peptidase S51 family. {ECO:0000255|HAMAP-
CC Rule:MF_00510}.
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DR EMBL; CP000970; ACB17783.1; -; Genomic_DNA.
DR RefSeq; WP_000421763.1; NC_010498.1.
DR AlphaFoldDB; B1LPH7; -.
DR SMR; B1LPH7; -.
DR MEROPS; S51.001; -.
DR EnsemblBacteria; ACB17783; ACB17783; EcSMS35_4474.
DR GeneID; 66672068; -.
DR KEGG; ecm:EcSMS35_4474; -.
DR HOGENOM; CLU_071689_0_0_6; -.
DR OMA; RDHDKYT; -.
DR Proteomes; UP000007011; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd03146; GAT1_Peptidase_E; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00510; Peptidase_E; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005320; Peptidase_S51.
DR InterPro; IPR023172; Peptidase_S51_dipeptidase-E.
DR Pfam; PF03575; Peptidase_S51; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Dipeptidase; Hydrolase; Protease; Serine protease.
FT CHAIN 1..229
FT /note="Peptidase E"
FT /id="PRO_1000127247"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
FT ACT_SITE 135
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
SQ SEQUENCE 229 AA; 24570 MW; 53D4D8395DFC63FD CRC64;
MELLLLSNST LPGKAWLEHA LPLIAEQLQG RRSAVFIPFA GVTQTWDDYT AKTAAVLAPL
GVSVTGIHSV VDPVAAIENA EIVIVGGGNT FQLLKQCRER GLLAPITDVV KRGALYIGWS
AGANLACPTI RTTNDMPIVD PQGFDALNLF PLQINPHFTN ALPEGHKGET REQRIRELLV
VAPELTIIGL PEGNWITVSK GHATLGGPNT TYVFKAGEEA VPLEAGHRF
