STRINGSTRING
STRING protein 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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
mreBRod shape-determining protein MreB; Derived by automated computational analysis using gene prediction method: Protein Homology. (347 aa)    
Predicted Functional Partners:
mreC
Rod shape-determining protein MreC; Involved in formation and maintenance of cell shape.
 
 
 0.996
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
 
 
 0.972
mrdA
Penicillin-binding protein 2; Catalyzes cross-linking of the peptidoglycan cell wall.
 
 
 
 0.939
AMF98460.1
Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.910
topA
DNA topoisomerase I subunit omega; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus rem [...]
     
 0.894
pyrH
UMP kinase; Catalyzes the reversible phosphorylation of UMP to UDP.
  
  
 0.891
AMF98587.1
Rod shape-determining protein RodA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family.
 
 
 0.868
gapA
Glyceraldehyde-3-phosphate dehydrogenase; Required for glycolysis; catalyzes the formation of 3-phospho-D-glyceroyl phosphate from D-glyceraldehyde 3-phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
  
  
 0.849
ftsA
Cell division protein FtsA; Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Belongs to the FtsA/MreB family.
 
 
 0.846
AMF99880.1
Rod shape-determining protein RodA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family.
 
 
 0.843
Your Current Organism:
Vibrio harveyi
NCBI taxonomy Id: 669
Other names: ATCC 14126, Achromobacter harveyi, Beneckea harveyi, Beneckea neptuna, CAIM 513, CCUG 28584, CECT 525, CIP 103192, DSM 19623, IFO 15634, LMG 4044, LMG:4044, Lucibacterium harveyi, NBRC 15634, NCCB 80033, NCTC 12970, Photobacterium harveyi, Pseudomonas harveyi, V. harveyi, Vibrio carchariae, Vibrio sp. HENC-01, Vibrio sp. HENC-02, Vibrio sp. PG 001, Vibrio sp. PG 002, Vibrio sp. PG 006, Vibrio sp. PG 007, Vibrio trachuri
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.