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
ACX95373.1KEGG: abo:ABO_0102 chemotaxis protein, putative. (190 aa)    
Predicted Functional Partners:
ACX95372.1
CheA signal transduction histidine kinase; PFAM: response regulator receiver; CheW domain protein; Hpt domain protein; ATP-binding region ATPase domain protein; SMART: response regulator receiver; Hpt domain protein; CheW domain protein; ATP-binding region ATPase domain protein; KEGG: tgr:Tgr7_2900 putative CheA signal transduction histidine kinase.
  
 
 0.999
ACX95569.1
CheA signal transduction histidine kinase; PFAM: ATP-binding region ATPase domain protein; CheW domain protein; Hpt domain protein; Signal transducing histidine kinase homodimeric; SMART: CheW domain protein; Hpt domain protein; ATP-binding region ATPase domain protein; KEGG: shn:Shewana3_1362 CheA signal transduction histidine kinases.
  
 
 0.870
ACX96884.1
KEGG: tmz:Tmz1t_1845 multi-sensor hybrid histidine kinase; TIGRFAM: PAS sensor protein; PFAM: ATP-binding region ATPase domain protein; response regulator receiver; PAS fold-3 domain protein; GAF domain protein; PAS fold-4 domain protein; PAS fold domain protein; histidine kinase A domain protein; SMART: ATP-binding region ATPase domain protein; histidine kinase A domain protein; response regulator receiver; PAC repeat-containing protein; GAF domain protein; PAS domain containing protein.
  
 
 0.864
ACX95371.1
PFAM: chemotaxis sensory transducer; SMART: chemotaxis sensory transducer; KEGG: tgr:Tgr7_2901 putative methyl-accepting chemotaxis sensory transducer.
  
 
 0.783
cheB
Response regulator receiver modulated CheB methylesterase; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family.
  
  
 0.684
ACX95478.1
TIGRFAM: flagellar protein FliS; PFAM: flagellar protein FliS; KEGG: hha:Hhal_0503 flagellar protein FliS.
  
  
 0.658
ACX95326.1
PFAM: chemotaxis sensory transducer; histidine kinase HAMP region domain protein; SMART: chemotaxis sensory transducer; histidine kinase HAMP region domain protein; KEGG: tgr:Tgr7_0851 methyl-accepting chemotaxis sensory transducer.
  
 
 0.623
ACX95960.1
PFAM: chemotaxis sensory transducer; histidine kinase HAMP region domain protein; SMART: chemotaxis sensory transducer; histidine kinase HAMP region domain protein; KEGG: tgr:Tgr7_1674 methyl-accepting chemotaxis sensory transducer.
  
 
 0.623
ACX96377.1
PFAM: chemotaxis sensory transducer; histidine kinase HAMP region domain protein; SMART: chemotaxis sensory transducer; histidine kinase HAMP region domain protein; KEGG: tcx:Tcr_1999 methyl-accepting chemotaxis sensory transducer.
  
 
 0.623
ACX95477.1
Flagellar hook-associated 2 domain protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
  
  
 0.619
Your Current Organism:
Halothiobacillus neapolitanus
NCBI taxonomy Id: 555778
Other names: H. neapolitanus c2, Halothiobacillus neapolitanus ATCC 23641, Halothiobacillus neapolitanus c2, Halothiobacillus neapolitanus str. c2, Halothiobacillus neapolitanus strain c2
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