ID PEPE_HAEI8 Reviewed; 234 AA.
AC Q4QMU5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 87.
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=NTHI0738;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87652.1; -; Genomic_DNA.
DR RefSeq; WP_011272125.1; NC_007146.2.
DR AlphaFoldDB; Q4QMU5; -.
DR SMR; Q4QMU5; -.
DR MEROPS; S51.001; -.
DR KEGG; hit:NTHI0738; -.
DR HOGENOM; CLU_071689_0_0_6; -.
DR Proteomes; UP000002525; 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; Serine protease.
FT CHAIN 1..234
FT /note="Peptidase E"
FT /id="PRO_0000258594"
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; 26153 MW; A7599B1697291B8D CRC64;
MKNMLLLSSS KYKNTGYLEH TLPWLQNFLA DYRGKTIAFV PYAGVSRTFD EYEKTVQNAL
SDLGMNIVSV HHGKQHRDII EQADVISIGG GNTFCLLKQL YEHNLIDIIR EKVNNGTPYF
GWSAGANVAG ASIMTTNDMP ITYPPSFQAL QLFPHQINPH FISGKMQGHN GESREERLAE
FLLVNPTALV YALPEGSALH IQNEMATVLG ENPILCFSEN MECGTFDINT TFSY
//
