pepP protein (Xanthomonas campestris) - STRING interaction network

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

pepP

Aminopeptidase P; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark. (444 aa)

Predicted Functional Partners:

XCC3260

0.830

pepN-2

0.802

pepN

0.799

pepN-3

0.795

XCC3262

0.697

XCC3261

0.620

ppc

0.539

mutT

0.481

pepQ-2

0.461

map

0.449

Your Current Organism:

Xanthomonas campestris

NCBI taxonomy Id: 190485
Other names: X. campestris pv. campestris str. ATCC 33913, Xanthomonas campestris pv. campestris str. ATCC 33913

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
XCC3260	XCC3261	XCC3260	XCC3261	Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the UPF0149 family.	Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.788
XCC3260	XCC3262	XCC3260	XCC3262	Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the UPF0149 family.	Conserved hypothetical protein; Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.	0.782
XCC3260	pepP	XCC3260	XCC3259	Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the UPF0149 family.	Aminopeptidase P; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.830
XCC3261	XCC3260	XCC3261	XCC3260	Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the UPF0149 family.	0.788
XCC3261	XCC3262	XCC3261	XCC3262	Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	Conserved hypothetical protein; Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.	0.968
XCC3261	pepP	XCC3261	XCC3259	Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	Aminopeptidase P; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.620
XCC3262	XCC3260	XCC3262	XCC3260	Conserved hypothetical protein; Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.	Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the UPF0149 family.	0.782
XCC3262	XCC3261	XCC3262	XCC3261	Conserved hypothetical protein; Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.	Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.968
XCC3262	pepP	XCC3262	XCC3259	Conserved hypothetical protein; Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.	Aminopeptidase P; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.697
map	pepN	XCC1382	XCC1054	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.614
map	pepN-2	XCC1382	XCC3168	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.614
map	pepN-3	XCC1382	XCC3485	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Aminopeptidase; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.614
map	pepP	XCC1382	XCC3259	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Aminopeptidase P; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.449
map	pepQ-2	XCC1382	XCC3257	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	0.831
map	ppc	XCC1382	XCC0754	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Phosphoenolpyruvate carboxylase; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.	0.470
mutT	pepP	XCC1965	XCC3259	7, 8-dihydro-8-oxoguanine-triphosphatase; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the Nudix hydrolase family. NudJ subfamily.	Aminopeptidase P; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.481
pepN	map	XCC1054	XCC1382	Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	0.614
pepN	pepP	XCC1054	XCC3259	Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	Aminopeptidase P; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.799
pepN	pepQ-2	XCC1054	XCC3257	Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position.	0.791
pepN-2	map	XCC3168	XCC1382	Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	0.614

page 1 of 3

Server load: low (20%) [HD]

Permalink

Network

Neighborhood

Experiments

Co-occurrence

Textmining

Co-expression

Databases

Fusion

© STRING Consortium 2026

Credits

Access

Info

About