pepE protein (Salmonella enterica Typhimurium)

Nodes:

Network nodes represent proteins

splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

Node Color

colored nodes:
query proteins and first shell of interactors

white nodes:
second shell of interactors

Node Content

empty nodes:
proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.

Knowledge-based Evidence

from curated databases

textmining

Assay-based Predictions

experimentally determined

co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

gene fusions

Your Input:

Neighborhood

Gene Fusion

Co-occurrence

Co-expression

Experiments

Databases

Textmining

[Homology]

Score

pepE

(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids. (229 aa)

Predicted Functional Partners:

iadA

0.925

ybeK

0.738

pepP

0.730

yjjU

0.677

iroN

0.672

rpiA

0.653

purN

0.604

pepT

0.560

STM4191

0.558

sspA

0.549

Your Current Organism:

Salmonella enterica Typhimurium

NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2

Export your current network:

... as a bitmap image:

download

file format is 'PNG': portable network graphic

... as a high-resolution bitmap:

download

same PNG format, but at higher resolution

... as a vector graphic:

download

SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc

... as short tabular text output:

download

TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)

... as tabular text output:

download

TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)

... as an XML summary:

download

structured XML interaction data, according to the 'PSI-MI' data standard

... protein node degrees:

download

node degree of proteins in your network (given the current score cut-off)

... network coordinates:

download

a flat-file format describing the coordinates and colors of nodes in the network

... protein sequences:

download

MFA: multi-fasta format - containing the aminoacid sequences in the network

... protein annotations:

download

a tab-delimited file describing the names, domains and descriptions of proteins in your network

... functional annotations:

download

a tab-delimited file containing all known functional terms of proteins in your network

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
STM4191	pepE	STM4191	STM4190	Putative cytoplasmic protein.	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	0.558
iadA	pepE	STM4512	STM4190	Isoaspartyl dipeptidase; Catalyzes the hydrolytic cleavage of a subset of L- isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation.	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	0.925
iroN	pepE	STM2777	STM4190	TonB-dependent siderophore receptor protein; Similar to E. coli outer membrane receptor for ferric enterobactin (enterochelin) and colicins B and D (AAC73685.1); Blastp hit to AAC73685.1 (746 aa), 52% identity in aa 3 - 728, 44% identity in aa 245 - 746.	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	0.672
iroN	ybeK	STM2777	STM0661	TonB-dependent siderophore receptor protein; Similar to E. coli outer membrane receptor for ferric enterobactin (enterochelin) and colicins B and D (AAC73685.1); Blastp hit to AAC73685.1 (746 aa), 52% identity in aa 3 - 728, 44% identity in aa 245 - 746.	Putative purine nucleoside hydrolase; Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively.	0.674
iroN	yjjU	STM2777	STM4563	TonB-dependent siderophore receptor protein; Similar to E. coli outer membrane receptor for ferric enterobactin (enterochelin) and colicins B and D (AAC73685.1); Blastp hit to AAC73685.1 (746 aa), 52% identity in aa 3 - 728, 44% identity in aa 245 - 746.	Putative phosphoesterase; Similar to E. coli orf, hypothetical protein (AAC77330.1); Blastp hit to AAC77330.1 (357 aa), 85% identity in aa 1 - 357.	0.649
pepE	STM4191	STM4190	STM4191	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	Putative cytoplasmic protein.	0.558
pepE	iadA	STM4190	STM4512	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	Isoaspartyl dipeptidase; Catalyzes the hydrolytic cleavage of a subset of L- isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation.	0.925
pepE	iroN	STM4190	STM2777	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	TonB-dependent siderophore receptor protein; Similar to E. coli outer membrane receptor for ferric enterobactin (enterochelin) and colicins B and D (AAC73685.1); Blastp hit to AAC73685.1 (746 aa), 52% identity in aa 3 - 728, 44% identity in aa 245 - 746.	0.672
pepE	pepP	STM4190	STM3058	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441.	0.730
pepE	pepT	STM4190	STM1227	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family.	0.560
pepE	purN	STM4190	STM2500	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	Polyphosphate kinase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.	0.604
pepE	rpiA	STM4190	STM3063	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	Constitutive ribosephosphate isomerase; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.	0.653
pepE	sspA	STM4190	STM3342	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	Stringent starvation protein A; Regulator of transcription; similar to E. coli regulator of transcription; stringent starvation protein A (AAC76261.1); Blastp hit to AAC76261.1 (212 aa), 98% identity in aa 1 - 211; Belongs to the GST superfamily.	0.549
pepE	ybeK	STM4190	STM0661	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	Putative purine nucleoside hydrolase; Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively.	0.738
pepE	yjjU	STM4190	STM4563	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	Putative phosphoesterase; Similar to E. coli orf, hypothetical protein (AAC77330.1); Blastp hit to AAC77330.1 (357 aa), 85% identity in aa 1 - 357.	0.677
pepP	pepE	STM3058	STM4190	Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441.	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	0.730
pepP	pepT	STM3058	STM1227	Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441.	Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family.	0.895
pepT	pepE	STM1227	STM4190	Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family.	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	0.560
pepT	pepP	STM1227	STM3058	Putative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family.	Similar to E. coli proline aminopeptidase P II (AAC75946.1); Blastp hit to AAC75946.1 (441 aa), 91% identity in aa 4 - 441.	0.895
purN	pepE	STM2500	STM4190	Polyphosphate kinase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.	(alpha)-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.	0.604

page 1 of 2

Server load: medium (44%) [HD]

Permalink

Network

Neighborhood

Experiments

Fusion

Textmining

Co-occurrence

Databases

Co-expression

© STRING Consortium 2026

Credits

Access

Info

About