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.
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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.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
sulACell division inhibitor SulA; Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division. (168 aa)    
Predicted Functional Partners:
ARA77657.1
DNA repair protein RecN; May be involved in recombinational repair of damaged DNA.
   
  
 0.911
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.
    
 
 0.796
hslU
ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
    
   0.766
ARA74401.1
YceK/YidQ family lipoprotein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.738
secM
SecA regulator SecM; Regulates secA expression by translational coupling of the secM secA operon. Translational pausing at a specific Pro residue 5 residues before the end of the protein may allow disruption of a mRNA repressor helix that normally suppresses secA translation initiation. Belongs to the SecM family.
  
     0.702
ARA77511.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.701
ARA74458.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.698
lexA
Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single- stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
  
  
 0.697
outS
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.675
ARA74675.1
Intracellular growth attenuator protein igaA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.661
Your Current Organism:
Pectobacterium brasiliense
NCBI taxonomy Id: 180957
Other names: CFBP 6617, Erwinia carotovora subsp. brasiliensis, LMG 21371, LMG:21371, NCPPB 4609, P. brasiliense, Pectobacterium brasiliense Portier et al. 2019, Pectobacterium brasiliensis, Pectobacterium carotovorum subsp. brasiliense, Pectobacterium carotovorum subsp. brasiliensis, strain 212
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