PEPE_SALTY
ID PEPE_SALTY Reviewed; 229 AA.
AC P36936;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Peptidase E;
DE EC=3.4.13.21;
DE AltName: Full=Alpha-aspartyl dipeptidase;
DE AltName: Full=Asp-specific dipeptidase;
DE AltName: Full=Dipeptidase E;
GN Name=pepE; OrderedLocusNames=STM4190;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-25.
RC STRAIN=LT2;
RX PubMed=8282693; DOI=10.1128/jb.176.1.166-172.1994;
RA Conlin C.A., Hakensson K., Liljas A., Miller C.G.;
RT "Cloning and nucleotide sequence of the cyclic AMP receptor protein-
RT regulated Salmonella typhimurium pepE gene and crystallization of its
RT product, an alpha-aspartyl dipeptidase.";
RL J. Bacteriol. 176:166-172(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP CHARACTERIZATION, ACTIVE SITES, AND MUTAGENESIS.
RX PubMed=10762256; DOI=10.1128/jb.182.9.2536-2543.2000;
RA Lassy R.A., Miller C.G.;
RT "Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a
RT serine hydrolase.";
RL J. Bacteriol. 182:2536-2543(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
RX PubMed=11106384; DOI=10.1073/pnas.260376797;
RA Hakansson K., Wang A.H.-J., Miller C.G.;
RT "The structure of aspartyl dipeptidase reveals a unique fold with a Ser-
RT His-Glu catalytic triad.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14097-14102(2000).
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.
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase S51 family. {ECO:0000305}.
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DR EMBL; U01246; AAA18923.1; -; Unassigned_DNA.
DR EMBL; AE006468; AAL23014.1; -; Genomic_DNA.
DR PIR; A36867; A36867.
DR RefSeq; NP_463055.1; NC_003197.2.
DR RefSeq; WP_000421792.1; NC_003197.2.
DR PDB; 1FY2; X-ray; 1.20 A; A=1-229.
DR PDB; 1FYE; X-ray; 1.20 A; A=1-229.
DR PDB; 6A4R; X-ray; 1.83 A; A/B=2-229.
DR PDB; 6A4S; X-ray; 1.90 A; A/B=2-229.
DR PDBsum; 1FY2; -.
DR PDBsum; 1FYE; -.
DR PDBsum; 6A4R; -.
DR PDBsum; 6A4S; -.
DR AlphaFoldDB; P36936; -.
DR SMR; P36936; -.
DR STRING; 99287.STM4190; -.
DR MEROPS; S51.001; -.
DR PaxDb; P36936; -.
DR EnsemblBacteria; AAL23014; AAL23014; STM4190.
DR GeneID; 1255716; -.
DR KEGG; stm:STM4190; -.
DR PATRIC; fig|99287.12.peg.4404; -.
DR HOGENOM; CLU_071689_0_0_6; -.
DR OMA; RDHDKYT; -.
DR PhylomeDB; P36936; -.
DR BioCyc; SENT99287:STM4190-MON; -.
DR BRENDA; 3.4.13.21; 5542.
DR EvolutionaryTrace; P36936; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Dipeptidase; Direct protein sequencing; Hydrolase;
KW Protease; Reference proteome; Serine protease.
FT CHAIN 1..229
FT /note="Peptidase E"
FT /id="PRO_0000209961"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10762256"
FT ACT_SITE 135
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10762256"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10762256"
FT VARIANT 120
FT /note="S -> T (in pepE1; deficient)"
FT VARIANT 137
FT /note="P -> S (in pepE1; deficient)"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1FY2"
FT TURN 16..20
FT /evidence="ECO:0007829|PDB:1FY2"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6A4S"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:1FY2"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1FY2"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1FY2"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:1FY2"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1FY2"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:1FY2"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:1FY2"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:1FY2"
SQ SEQUENCE 229 AA; 24769 MW; 41D40652C7D32220 CRC64;
MELLLLSNST LPGKAWLEHA LPLIANQLNG RRSAVFIPFA GVTQTWDEYT DKTAEVLAPL
GVNVTGIHRV ADPLAAIEKA EIIIVGGGNT FQLLKESRER GLLAPMADRV KRGALYIGWS
AGANLACPTI RTTNDMPIVD PNGFDALDLF PLQINPHFTN ALPEGHKGET REQRIRELLV
VAPELTVIGL PEGNWIQVSN GQAVLGGPNT TWVFKAGEEA VALEAGHRF
