PEPE_SHESM
ID PEPE_SHESM Reviewed; 236 AA.
AC Q0HHP4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Shewmr4_2352;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
RG US DOE Joint Genome Institute;
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. MR-4.";
RL Submitted (AUG-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; CP000446; ABI39423.1; -; Genomic_DNA.
DR RefSeq; WP_011623113.1; NC_008321.1.
DR AlphaFoldDB; Q0HHP4; -.
DR SMR; Q0HHP4; -.
DR MEROPS; S51.001; -.
DR KEGG; she:Shewmr4_2352; -.
DR HOGENOM; CLU_071689_0_0_6; -.
DR OMA; RDHDKYT; -.
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_1000050619"
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; 25958 MW; DE1B2941BC093F8D CRC64;
MTVNALLLSS SRVGDTPYLS HAIPFIKPLT TNAQKWIFIP YAGVSMSYDT YLASVVAGLS
ELRLDISGIH QHPDPRQAIK DADGILIGGG NTFHLLHELY KYDLVHLIRE EVMNGKPYIG
WSAGSNVSGL SIRTTNDMPI IEPPSFTALN IVPFQLNPHY SNYRAPGHNG ETRAQRLLEF
TRVDPITPVV GIVEGSALWR QGETLSLLGD NPAYLFCGEQ QEIPIPVGSD LSHLLK
