ID   PEPE_SALG2              Reviewed;         234 AA.
AC   B5R7Q9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=SG4050;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(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; AM933173; CAR39820.1; -; Genomic_DNA.
DR   RefSeq; WP_000421784.1; NC_011274.1.
DR   AlphaFoldDB; B5R7Q9; -.
DR   SMR; B5R7Q9; -.
DR   MEROPS; S51.001; -.
DR   EnsemblBacteria; CAR39820; CAR39820; SG4050.
DR   KEGG; seg:SG4050; -.
DR   HOGENOM; CLU_071689_0_0_6; -.
DR   OMA; RDHDKYT; -.
DR   Proteomes; UP000008321; 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..234
FT                   /note="Peptidase E"
FT                   /id="PRO_1000127249"
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   234 AA;  25350 MW;  B793085221607B54 CRC64;
     MELLLLSNST LPGKAWLEHA LPLIANQLNG RRSAVFIPFA GVTQTWDEYT DKTAEVLAPL
     GINVTGIHRV ADPLAAIEKA EIIIVGGGNT FQLMKESRER GLLAPMADRV KRGALYIGWS
     AGANLACPTI RTTNDMPIVD PNGFDALDLF PLQINPHFTN ALPEGHKGET REQRIRELLV
     VAPELTVIGL PEGNWIQVSN GQAVPGGPNT TWVFKAGEEA VALEAVIAFN PWPH