VM_10415 protein (Vibrio mimicus) - 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

Cooccurrence

Coexpression

Experiments

Databases

Textmining

[Homology]

Score

VM_10415

Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (108 aa)

Predicted Functional Partners:

lipB

0.719

lipA

0.719

VM_10400

0.643

VM_10395

0.533

Your Current Organism:

Vibrio mimicus

NCBI taxonomy Id: 674
Other names: ATCC 33653, CAIM 602, CCUG 13624, CIP 101888, DSM 19130, LMG 7896, LMG:7896, NCTC 11435, V. mimicus

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
VM_10395	VM_10400	VM_10395	VM_10400	D-alanyl-D-alanine carboxypeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family.	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family.	0.754
VM_10395	VM_10415	VM_10395	VM_10415	D-alanyl-D-alanine carboxypeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family.	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.	0.533
VM_10395	lipB	VM_10395	VM_10405	D-alanyl-D-alanine carboxypeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family.	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	0.402
VM_10400	VM_10395	VM_10400	VM_10395	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family.	D-alanyl-D-alanine carboxypeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family.	0.754
VM_10400	VM_10415	VM_10400	VM_10415	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family.	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.	0.643
VM_10400	lipA	VM_10400	VM_10410	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family.	Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.811
VM_10400	lipB	VM_10400	VM_10405	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family.	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	0.865
VM_10415	VM_10395	VM_10415	VM_10395	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.	D-alanyl-D-alanine carboxypeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family.	0.533
VM_10415	VM_10400	VM_10415	VM_10400	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family.	0.643
VM_10415	lipA	VM_10415	VM_10410	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.	Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.719
VM_10415	lipB	VM_10415	VM_10405	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	0.719
lipA	VM_10400	VM_10410	VM_10400	Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family.	0.811
lipA	VM_10415	VM_10410	VM_10415	Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.	0.719
lipA	lipB	VM_10410	VM_10405	Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	0.999
lipB	VM_10395	VM_10405	VM_10395	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	D-alanyl-D-alanine carboxypeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family.	0.402
lipB	VM_10400	VM_10405	VM_10400	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0250 family.	0.865
lipB	VM_10415	VM_10405	VM_10415	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.	0.719
lipB	lipA	VM_10405	VM_10410	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.999

Server load: low (24%) [HD]

Permalink

Network

Neighborhood

Databases

Fusion

Textmining

Cooccurrence

Experiments

Coexpression

© STRING Consortium 2026

Credits

Access

Info

About