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
flgJPeptidoglycan hydrolase flgJ (EC 3.2.1.-) (Muramidase flgJ). Flagellum-specific muramidase which hydrolyses the peptidoglycan layer to assemble the rod structure in the periplasmic space (by similarity). InterPro: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases Pfam: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidases no signal peptide no TMHs; High confidence in function and specificity. (355 aa)    
Predicted Functional Partners:
flgK
Flagellar hook-filament junction protein 1 (HAP1). no signal peptide no TMHs; High confidence in function and specificity.
 
  
 0.994
flgH
Flagellar L-ring protein precursor; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
 
  
 0.994
flgI
Flagellar P-ring protein precursor; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
 
  
 0.993
flgA
Flagella basal body P-ring formation protein flgA precursor. Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a chaperon protein for the P-ring assembly (by similarity). signal peptide no TMHs; High confidence in function and specificity.
 
  
 0.992
flgF
Flagellar basal-body rod protein flgF (Putative proximal rod protein). The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity.
 
  
 0.991
flgB
Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
 
 
 0.991
fliK
Flagellar hook-length control protein. Controls the length of the flagellar hook. no TMHs no signal peptide; Family membership.
 
  
 0.990
flgG
Flagellar basal-body rod protein flgG (Distal rod protein). The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity.
 
 
 0.988
fliH
Probable Flagellar assembly protein FliH, 38% identity to TrEMBL;Q7VYE7, Q7WJB3, Q8XSS5. Has PF02108,Flagellar assembly protein FliH;IPR000563, Flag_FliH; Many flagellar proteins are exported by a flagellum-specific export pathway. Attempts have been made to characterise the apparatus responsible for this process, by designing assays to screen for mutants with export defects. Experiments involving filament removal from temperature-sensitive flagellar mutants of Salmonella typhimurium have shown that, while most mutants were able to regrow filaments, flhA, fliH, fliI and fliN mutants sh [...]
 
  
 0.987
fliM
Flagellar motor switch protein fliM. FLIM IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE LOCATED AT THE BASE OF THE BASAL BODY. THIS COMPLEX INTERACTS WITH THE CHEY AND CHEZ CHEMOTAXIS PROTEINS IN ADDITION TO CONTACTING COMPONENTS OF THE MOTOR THAT DETERMINE THE DIRECTION OF FLAGELLAR ROTATION. InterPro: Flagellar motor switch protein FliM Pfam:Flagellar motor switch protein FliM no TMHs signale peptide: no analysis; High confidence in function and specificity.
 
 
 0.986
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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