ID   PEPE_ECOL6              Reviewed;         229 AA.
AC   Q8FB55;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=c4980;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014075; AAN83406.1; -; Genomic_DNA.
DR   RefSeq; WP_000421769.1; NC_004431.1.
DR   AlphaFoldDB; Q8FB55; -.
DR   SMR; Q8FB55; -.
DR   STRING; 199310.c4980; -.
DR   MEROPS; S51.001; -.
DR   EnsemblBacteria; AAN83406; AAN83406; c4980.
DR   KEGG; ecc:c4980; -.
DR   eggNOG; COG3340; Bacteria.
DR   HOGENOM; CLU_071689_0_0_6; -.
DR   OMA; RDHDKYT; -.
DR   BioCyc; ECOL199310:C4980-MON; -.
DR   Proteomes; UP000001410; 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_0000209957"
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;  24560 MW;  519FB4356C843CC2 CRC64;
     MELLLLSNST LPGKAWLEHA LPLIAEQLQG RRSAVFIPFA GVTQTWDDYT AKTAAVLASL
     GVSVTGIHSV VDPVAAIENA EIVIVGGGNT FQLLKQCRER GLLAPITDVV KRGALYIGWS
     AGANLACPTI RTTNDMPIVD PQGFDALNLF PLQINPHFTN ALPEGHKGET REQRIRELLV
     VAPELTIIGL PEGNWITVSK GHATLGGPNT TYVFKAGEEA VPLEAGHRF