PEPE_SHESA
ID PEPE_SHESA Reviewed; 236 AA.
AC A0KY73;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Shewana3_2513;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000469; ABK48742.1; -; Genomic_DNA.
DR RefSeq; WP_011717430.1; NC_008577.1.
DR AlphaFoldDB; A0KY73; -.
DR SMR; A0KY73; -.
DR STRING; 94122.Shewana3_2513; -.
DR MEROPS; S51.001; -.
DR EnsemblBacteria; ABK48742; ABK48742; Shewana3_2513.
DR KEGG; shn:Shewana3_2513; -.
DR eggNOG; COG3340; Bacteria.
DR HOGENOM; CLU_071689_0_0_6; -.
DR OMA; RDHDKYT; -.
DR OrthoDB; 1485646at2; -.
DR Proteomes; UP000002589; 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..236
FT /note="Peptidase E"
FT /id="PRO_1000050618"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
SQ SEQUENCE 236 AA; 25925 MW; C4EA19EEB3C54FF1 CRC64;
MTINALLLSS SRVGDTPYLS HALPFIKPLT ANAQKWIFIP YAGVSMSYDT YLASVVAGLS
ELRLDISGIH QHPDPRQAIK DADGILIGGG NTFHLLHELY KYDLVHLIRE EVQNGKPYIG
WSAGSNVSGL SIRTTNDMPI IEPPSFTALN IVPFQLNPHY SNYRAPGHNG ETRAQRLLEF
TRVDPITPVV GIVEGSALWR QGDTLSLLGD NPAYLFCGEQ QEIPIPVGSD LSHLLK
