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
ftsZCell 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. (405 aa)    
Predicted Functional Partners:
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.
 
 0.985
AME00910.1
Cell division protein FtsZ; Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins. Belongs to the ZipA family.
  
 
 0.778
AME01797.1
Cell division protein FtsQ; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.728
minC
Septum site-determining protein MinC; Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization; Belongs to the MinC family.
   
 
 0.711
murG
Phosphatase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily.
 
 
 0.654
recA
acyl-CoA synthetase; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
  
 
 
 0.642
lpxC
UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase; Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis; Belongs to the LpxC family.
  
  
 0.633
ftsW
Cell division protein FtsW; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family.
 
 
 0.618
atpA
ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
   
  
 0.613
murC
UDP-N-acetylmuramate--alanine ligase; Cell wall formation; Belongs to the MurCDEF family.
 
 
 0.557
Your Current Organism:
Moraxella osloensis
NCBI taxonomy Id: 34062
Other names: ATCC 19976, CCUG 350, CIP 68.35, DSM 6998, LMG 5131, LMG:5131, M. osloensis, NCTC 10465, strain A1920
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.