ID   PEPE_ECOLC              Reviewed;         229 AA.
AC   B1IUN1;
DT   20-MAY-2008, 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}; OrderedLocusNames=EcolC_4009;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA79608.1; -; Genomic_DNA.
DR   RefSeq; WP_000421763.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IUN1; -.
DR   SMR; B1IUN1; -.
DR   MEROPS; S51.001; -.
DR   GeneID; 66672068; -.
DR   KEGG; ecl:EcolC_4009; -.
DR   HOGENOM; CLU_071689_0_0_6; -.
DR   OMA; RDHDKYT; -.
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_1000081585"
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