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
ODS24919.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (309 aa)    
Predicted Functional Partners:
ODS24674.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
     0.725
AB835_08480
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex ATPase subunit type 1 TsaE; Incomplete; partial in the middle of a contig; missing stop; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.689
ODS24673.1
Cell shape-determining protein CcmA; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.688
secA
Preprotein translocase subunit SecA; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. Belongs to the SecA family.
       0.580
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.
     
 0.533
argJ
Bifunctional ornithine acetyltransferase/N-acetylglutamate synthase; Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Belongs to the ArgJ family.
       0.527
ODS24916.1
7,8-dihydro-8-oxoguanine-triphosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Nudix hydrolase family.
       0.446
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.
 
   
 0.442
murF
Hypothetical protein; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein; Belongs to the MurCDEF family. MurF subfamily.
 
  
 0.440
ODS23012.1
Signal peptidase I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S26 family.
 
  
 0.436
Your Current Organism:
Endobugula sertula
NCBI taxonomy Id: 62101
Other names: Bugula neritina bacterial symbiont, C. Endobugula sertula, Candidatus Endobugula sertula
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.