ID A0A0Q0NWG8_9GAMM Unreviewed; 236 AA.
AC A0A0Q0NWG8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Peptidase E {ECO:0000256|HAMAP-Rule:MF_00510};
DE EC=3.4.13.21 {ECO:0000256|HAMAP-Rule:MF_00510};
DE AltName: Full=Alpha-aspartyl dipeptidase {ECO:0000256|HAMAP-Rule:MF_00510};
DE AltName: Full=Asp-specific dipeptidase {ECO:0000256|HAMAP-Rule:MF_00510};
DE AltName: Full=Dipeptidase E {ECO:0000256|HAMAP-Rule:MF_00510};
GN Name=pepE {ECO:0000256|HAMAP-Rule:MF_00510,
GN ECO:0000313|EMBL:KPZ67747.1};
GN ORFNames=AN944_03930 {ECO:0000313|EMBL:KPZ67747.1};
OS Shewanella sp. P1-14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ67747.1, ECO:0000313|Proteomes:UP000050414};
RN [1] {ECO:0000313|EMBL:KPZ67747.1, ECO:0000313|Proteomes:UP000050414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ67747.1,
RC ECO:0000313|Proteomes:UP000050414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:0000256|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:0000256|HAMAP-Rule:MF_00510};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00510}.
CC -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534, ECO:0000256|HAMAP-Rule:MF_00510}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPZ67747.1}.
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DR EMBL; LKTL01000036; KPZ67747.1; -; Genomic_DNA.
DR RefSeq; WP_055026314.1; NZ_LKTL01000036.1.
DR AlphaFoldDB; A0A0Q0NWG8; -.
DR PATRIC; fig|1723761.3.peg.4030; -.
DR Proteomes; UP000050414; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_00510};
KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997, ECO:0000256|HAMAP-
KW Rule:MF_00510};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00510};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00510};
KW Reference proteome {ECO:0000313|Proteomes:UP000050414};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_00510}.
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00510"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00510"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00510"
SQ SEQUENCE 236 AA; 26043 MW; 9C7AAED9AE29715A CRC64;
MAVNALMLSS SREGNTPYLA HAIEFIKPLT THAKKWVFIP YAGVSVEYDK YLAMVTEGLA
PLNIEVSSIH QYSDPKQAIK DADGILVGGG NTFQLLNELY RYDLVHLLNE QVSNGKPYIG
WSAGSNITGL SIRTTNDMPI VEPASFTGLK LLPFQLNPHY TNYQAPGHNG ETRAQRLLEF
TIVDPITPVI GIQEGTALWR QGDTLSLVGE KDAYLFHGKE QEVVIPVGSD LSHYLD
//
