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
ACX96265.1PFAM: Stage II sporulation E family protein; SMART: protein phosphatase 2C domain protein; KEGG: rme:Rmet_2259 serine phosphatase. (403 aa)    
Predicted Functional Partners:
ACX96591.1
KEGG: sse:Ssed_3079 flagellar rod assembly protein/muramidase FlgJ; TIGRFAM: flagellar rod assembly protein/muramidase FlgJ; PFAM: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase; Flagellar protein FlgJ-like; SMART: Lysozyme subfamily 2.
   
    0.962
ACX96266.1
KEGG: aav:Aave_2928 hypothetical protein.
 
  
 0.920
ACX96267.1
PFAM: Domain of unknown function DUF1987; KEGG: rme:Rmet_2261 putative lipoprotein.
 
    0.905
ACX95557.1
Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), 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.
 
    0.865
ACX95291.1
Flagellar motor switch protein FliG; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), 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.
  
    0.850
ACX96599.1
Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
   
    0.838
ACX95726.1
Diguanylate phosphodiesterase; PFAM: EAL domain protein; SMART: EAL domain protein; KEGG: ppw:PputW619_3232 diguanylate phosphodiesterase.
 
    0.785
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.
 
  
 0.730
ACX96596.1
TIGRFAM: flagellar hook-basal body protein; PFAM: flagellar basal body FlaE domain protein; flagellar basal body rod protein; protein of unknown function DUF1078 domain protein; KEGG: noc:Noc_2375 hypothetical protein.
   
    0.711
ACX96639.1
Diguanylate cyclase/phosphodiesterase with GAF sensor; PFAM: EAL domain protein; GGDEF domain containing protein; GAF domain protein; SMART: EAL domain protein; GGDEF domain containing protein; GAF domain protein; KEGG: wsu:WS0108 GGDEF family protein.
  
  
 0.677
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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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.