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
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Textmining
[Homology]
Score
flhFPutative flagellar biosynthesis protein flhF (Flagella associated GTP-binding protein). Necessary for flagellar priosinthesis. May be involved in translocation of the flagellum (by similarity). Belongs to the family of of subunits of the signal recognition particale in bacteria like FtsY, the pilA protein and the flagellar biosynthesis protein flhF. InterPro: AAA ATPase superfamily, GTP-binding signal recognition particell (SRP54) G-domain no signal peptide no TMHs; Family membership. (510 aa)    
Predicted Functional Partners:
fleN
Hypothetical flagellar related protein FleN. Homology to fleN of Pseudomonas fluorescens of 27% (AAN03366). No domains predicted. No signal peptide. No TMHs.
 
 
 0.998
flhA
Flagellar biosynthesis protein flhA; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family.
 
  
 0.975
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.
 
 
 0.974
flhB
Flagellar biosynthetic protein FlhB; Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the type III secretion exporter family.
 
  
 0.972
fliG
Flagellar motor switch protein fliG. FLIG 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 (BY SIMILARITY). fliG: flagellar motor switch protein Pfam: fliG C-terminal domain no signal peptide no TMHs; High confidence in function and specificity.
 
 
 0.967
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 [...]
 
  
 0.965
flgJ
Peptidoglycan 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.
 
  
 0.963
fliK
Flagellar hook-length control protein. Controls the length of the flagellar hook. no TMHs no signal peptide; Family membership.
 
  
 0.960
flgB
Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
 
  
 0.960
cheV2
Probable chemotaxis protein, CheW. IPR001789; Response_reg. Pfam: PF01584; CheW. PF00072; Response_reg. SMART: SM00260; CheW. SM00448; REC. Chemotaxis protein cheV. CHEMOTAXIS INVOLVES BOTH A PHOSPHORYLATION-DEPENDENT EXCITATION AND A METHYLATION-DEPENDENT ADAPTATION. CHEV AND CHEW FUNCTION TOGETHER TO COUPLE CHEA ACTIVATION TO METHYL-ACCEPTING CHEMOTAXIS PROTEIN RECEPTOR STATUS AND POSSIBLE CHEA-DEPENDENT PHOSPHORYLATION OF CHEV CONTRIBUTES TO ADAPTATION; High confidence in function and specificity.
 
 
 0.959
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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