ID PEPE_ACTP2 Reviewed; 234 AA.
AC A3N0N1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=APL_0871;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(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; CP000569; ABN73967.1; -; Genomic_DNA.
DR RefSeq; WP_005612204.1; NC_009053.1.
DR AlphaFoldDB; A3N0N1; -.
DR SMR; A3N0N1; -.
DR STRING; 416269.APL_0871; -.
DR MEROPS; S51.001; -.
DR EnsemblBacteria; ABN73967; ABN73967; APL_0871.
DR KEGG; apl:APL_0871; -.
DR eggNOG; COG3340; Bacteria.
DR HOGENOM; CLU_071689_0_0_6; -.
DR Proteomes; UP000001432; 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 PANTHER; PTHR20842:SF0; ALPHA-ASPARTYL DIPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR20842; PROTEASE S51 ALPHA-ASPARTYL DIPEPTIDASE; 1.
DR Pfam; PF03575; Peptidase_S51; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Dipeptidase; Hydrolase; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..234
FT /note="Peptidase E"
FT /id="PRO_1000050609"
FT ACT_SITE 123
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
FT ACT_SITE 138
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
SQ SEQUENCE 234 AA; 26125 MW; F12FE257720FBB4A CRC64;
MKNMLLMSGS KYKDTAYLVH TLPWLAQFLA DYKGKKVAFV PYAGVRRSFD EYETTVKNAL
QSLELEIVSV HRGKQHRDII EQADVIAIGG GNTFCLLKQM YEHDLLDAIR AKVNSGTPYF
GWSAGANVAG SSIMTTNDMP ITYPPSFNAL NLFPHQINPH FISGKMQGHN GESREERLEE
FLIVNPQSLV YAMPEGTALH IQGEQATVLG AQDILCFSEK MQLDTKAVNS TFNY
//
