PEPE_ECOLI
ID PEPE_ECOLI Reviewed; 229 AA.
AC P0A7C6; P32666; Q2M6T3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=b4021, JW3981;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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 -!- INTERACTION:
CC P0A7C6; P37095: pepB; NbExp=2; IntAct=EBI-555623, EBI-549539;
CC P0A7C6; P29745: pepT; NbExp=4; IntAct=EBI-555623, EBI-555639;
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; U00006; AAC43115.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76991.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78023.1; -; Genomic_DNA.
DR PIR; D65209; D65209.
DR RefSeq; NP_418445.1; NC_000913.3.
DR RefSeq; WP_000421763.1; NZ_STEB01000022.1.
DR AlphaFoldDB; P0A7C6; -.
DR SMR; P0A7C6; -.
DR BioGRID; 4262655; 24.
DR DIP; DIP-48072N; -.
DR IntAct; P0A7C6; 4.
DR STRING; 511145.b4021; -.
DR MEROPS; S51.001; -.
DR jPOST; P0A7C6; -.
DR PaxDb; P0A7C6; -.
DR PRIDE; P0A7C6; -.
DR EnsemblBacteria; AAC76991; AAC76991; b4021.
DR EnsemblBacteria; BAE78023; BAE78023; BAE78023.
DR GeneID; 66672068; -.
DR GeneID; 948520; -.
DR KEGG; ecj:JW3981; -.
DR KEGG; eco:b4021; -.
DR PATRIC; fig|1411691.4.peg.2692; -.
DR EchoBASE; EB1864; -.
DR eggNOG; COG3340; Bacteria.
DR HOGENOM; CLU_071689_0_0_6; -.
DR InParanoid; P0A7C6; -.
DR OMA; RDHDKYT; -.
DR PhylomeDB; P0A7C6; -.
DR BioCyc; EcoCyc:EG11920-MON; -.
DR BioCyc; MetaCyc:EG11920-MON; -.
DR PRO; PR:P0A7C6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008233; F:peptidase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Cytoplasm; Dipeptidase; Hydrolase; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..229
FT /note="Peptidase E"
FT /id="PRO_0000209955"
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
