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
Swoo_0179Conserved hypothetical 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. (170 aa)    
Predicted Functional Partners:
lexA
LexA repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. 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.
 
  
 0.926
Swoo_3359
DNA repair protein RecN; May be involved in recombinational repair of damaged DNA.
   
  
 0.849
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.
    
 
 0.849
Swoo_2130
PFAM: YebG family protein; KEGG: sse:Ssed_2486 YebG family protein.
   
    0.811
hslU
Heat shock protein HslVU, ATPase 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.
    
   0.720
Swoo_0379
KEGG: sse:Ssed_4221 hypothetical protein.
   
    0.711
Swoo_2465
PFAM: peptidase S24 and S26 domain protein; KEGG: sse:Ssed_2172 SOS-response transcriptional repressor LexA -like protein; Belongs to the peptidase S24 family.
  
  
 0.599
recA
recA protein; 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.
   
    0.566
Swoo_0488
PFAM: protein of unknown function DUF484; KEGG: sse:Ssed_4128 protein of unknown function DUF484.
  
     0.546
Swoo_2601
KEGG: sse:Ssed_2002 hypothetical protein.
  
     0.498
Your Current Organism:
Shewanella woodyi
NCBI taxonomy Id: 392500
Other names: S. woodyi ATCC 51908, Shewanella woodyi ATCC 51908, Shewanella woodyi str. ATCC 51908, Shewanella woodyi strain ATCC 51908
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.