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.
Knowledge-based Evidence
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 protein; 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:
recN
Recombination and repair protein; May be involved in recombinational repair of damaged DNA.
   
  
 0.915
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.
    
 
 0.853
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.
    
   0.835
AKA37462.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
    0.828
b4043
LexA repressor; 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.
 
  
 0.781
AKA38545.1
Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.636
kefA_2
Mechanosensitive channel protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.579
AKA37520.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.565
recA
Recombinase A; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
   
    0.563
putA
Transcriptional regulator; Oxidizes proline to glutamate for use as a carbon and nitrogen source; Belongs to the aldehyde dehydrogenase family. In the N-terminal section; belongs to the proline dehydrogenase family.
  
    0.554
Your Current Organism:
Yersinia ruckeri
NCBI taxonomy Id: 29486
Other names: ATCC 29473, CCM 6093, CCUG 14190, CDC 2396-61, CIP 82.80, DSM 18506, JCM 15110, JCM 2429, NCIB 2194, NCIMB 2194, NCTC 12986, Y. ruckeri
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