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The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
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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
KFX04059.1LysR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the LysR transcriptional regulatory family. (331 aa)    
Predicted Functional Partners:
KFX06807.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.717
KFX05368.1
LysR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the LysR transcriptional regulatory family.
  
     0.696
KFX03726.1
Protein disulfide isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.662
KFX03746.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.658
KFX07210.1
Multiple stress resistance protein BhsA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.639
fliT
Flagellar biosynthesis protein FliT; Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus.
  
     0.631
lpxM
Lipid A biosynthesis (KDO)2-(lauroyl)-lipid IVA acyltransferase; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A.
  
     0.625
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.
  
     0.616
KFX06780.1
Membrane assembly protein AsmA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.599
KFX07461.1
GTP-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.596
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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