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
KFX03760.1Universal stress global response regulator UspA; Involved in resistance to DNA-damaging agents; Derived by automated computational analysis using gene prediction method: Protein Homology. (145 aa)    
Predicted Functional Partners:
KFX06091.1
DNA polymerase III subunit psi; 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. The exact function of the psi subunit is unknown.
  
     0.769
mukF
Condesin subunit F; Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Not required for mini-F plasmid partitioning. Probably acts via its interaction with MukB and MukE. Overexpression results in anucleate cells. It has a calcium binding activity.
  
     0.764
zapB
Septal ring assembly protein ZapB; Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA.
  
    0.763
KFX07158.1
Porin; Allows for ions and hydrophilic solutes to cross the outer membrane; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.757
KFX03490.1
Cytochrome D ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.745
KFX00560.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.740
KFX06780.1
Membrane assembly protein AsmA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.736
helD
DNA helicase IV; Catalyzes the ATP-dependent unwinding of duplex DNA in the 3' to 5' direction with respect to the bound single strand; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.716
ftsN
Cell division protein FtsN; Essential cell division protein that activates septal peptidoglycan synthesis and constriction of the cell. Acts on both sides of the membrane, via interaction with FtsA in the cytoplasm and interaction with the FtsQBL complex in the periplasm. These interactions may induce a conformational switch in both FtsA and FtsQBL, leading to septal peptidoglycan synthesis by FtsI and associated synthases.
  
    0.716
lpoB
Penicillin-binding protein; Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). Belongs to the LpoB family.
  
   
 0.690
Your Current Organism:
Pectobacterium betavasculorum
NCBI taxonomy Id: 55207
Other names: ATCC 43762, CFBP 2122, CIP 105193, DSM 18076, Erwinia carotovora subsp. betavasculorum, ICMP 4226, LMG 2464, LMG 2466, LMG:2464, LMG:2466, NCPPB 2795, P. betavasculorum, Pectobacterium carotovorum subsp. betavasculorum, UCPB 193
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