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
ftsECell division ATP-binding protein FtsE; Part of the ABC transporter FtsEX involved in cellular division. (229 aa)    
Predicted Functional Partners:
ANO05279.1
Cell division protein FtsX; Part of the ABC transporter FtsEX involved in cellular division; Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.
 
 
 0.998
smpB
SsrA-binding protein; Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to [...]
  
  
 0.928
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.
 
 
 0.799
ftsY
Signal recognition particle-docking protein FtsY; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
     
 0.770
ffh
Signal recognition particle protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Belongs to the GTP-binding SRP family. SRP54 subfamily.
     
 0.684
ftsQ
Cell division protein FtsQ; Essential cell division protein; Belongs to the FtsQ/DivIB family. FtsQ subfamily.
      
 0.683
ANO04459.1
Invasion protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.667
ANO03816.1
Cell division protein FtsW; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family.
 
   
 0.641
ANO04751.1
Cell division protein FtsK; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
   
 0.631
ANO02380.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
     
 0.586
Your Current Organism:
Mycobacteroides immunogenum
NCBI taxonomy Id: 83262
Other names: ATCC 700505, CCUG 47286, DSM 45595, JCM 12691, M. immunogenum, MC 779, Mycobacterium immunogenum, Mycobacterium immunogenum Wilson et al. 2001, Mycobacteroides immunogenum (Wilson et al. 2001) Gupta et al. 2018, strain BH29
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