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
ZMO0865Replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins. Belongs to the helicase family. DnaB subfamily. (511 aa)    
Predicted Functional Partners:
dnaG
DNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
 0.980
dnaA
Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity).
  
 
 
 0.973
murG
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase; 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.
 
  
 0.888
ZMO1542
KEGG: sit:TM1040_1425 single-strand binding protein; TIGRFAM: single-strand binding protein; PFAM: single-strand binding protein/Primosomal replication protein n.
 
 
 0.794
ZMO1091
KEGG: swi:Swit_0485 DNA polymerase III, delta prime subunit.
 
 
 
 0.737
tuf
Translation elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.
   
   0.732
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.
      
 0.726
ZMO0574
PFAM: UvrD/REP helicase; KEGG: swi:Swit_1212 ATP-dependent DNA helicase UvrD.
  
 
 0.684
ZMO1538
DNA polymerase III, alpha subunit; SMART: phosphoesterase PHP domain protein; TIGRFAM: DNA polymerase III, alpha subunit; KEGG: swi:Swit_2340 DNA polymerase III, alpha subunit; PFAM: PHP domain protein; DNA polymerase III alpha subunit.
 
 
 0.683
dnaX
DNA polymerase III, subunits gamma and tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
 
 
 
 0.680
Your Current Organism:
Zymomonas mobilis ZM4
NCBI taxonomy Id: 264203
Other names: Z. mobilis subsp. mobilis ZM4 = ATCC 31821, Zymomonas mobilis subsp. mobilis ATCC 31821, Zymomonas mobilis subsp. mobilis ATCC 31821 = ZM4, Zymomonas mobilis subsp. mobilis ZM4, Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.