STRINGSTRING
DVU_2670 protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"DVU_2670" - Cell division protein ZapA in Desulfovibrio vulgaris Hildenborough
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
DVU_2670Cell division protein ZapA; 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 (87 aa)    
Predicted Functional Partners:
DVU_2669
annotation not available (78 aa)
     
      0.966
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 (449 aa)
     
 
  0.800
DVU_2511
Uncharacterized protein; Identified by Glimmer2; putative (95 aa)
   
          0.780
DVU_1176
Uncharacterized protein; Identified by Glimmer2; putative (185 aa)
   
          0.780
DVU_1651
Uncharacterized protein; Identified by similarity to OMNI-NTL01SM00387 (123 aa)
   
          0.779
DVU_0731
Uncharacterized protein; Identified by Glimmer2; putative (453 aa)
   
          0.778
DVU_2071
annotation not available (318 aa)
   
          0.777
DVU_1657
Uncharacterized protein; Identified by Glimmer2; putative (99 aa)
   
          0.775
glmU
Bifunctional protein GlmU; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP- GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5- monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain; In the C-terminal section; belongs to the transferase hexapeptide repeat family (455 aa)
              0.774
DVU_3173
Uncharacterized protein; Identified by Glimmer2; putative (58 aa)
   
          0.772
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
Server load: low (17%) [HD]