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
Cla_1198Sodium- and chloride-dependent transporter, SNF family; Pfam match to PF00209.9 SNF. (444 aa)    
Predicted Functional Partners:
Cla_1199
Sodium- and chloride-dependent transporter, SNF family; Pfam match to PF00209.9 SNF.
 
   
0.789
Cla_1200
Sodium- and chloride-dependent transporter, SNF family; Pfam match to PF00209.9 SNF.
 
   
0.789
pycB
Pyruvate carboxylase, subunit B; Pfam matches to PF00682.10 HMGL-like, and to PF00364.13 Biotin_lipoyl.
       0.621
pckA
Phosphoenolpyruvate carboxykinase; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
       0.595
atpE
ATP synthase F0 sector, C subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
       0.524
Your Current Organism:
Campylobacter lari
NCBI taxonomy Id: 306263
Other names: C. lari RM2100, Campylobacter lari RM2100, Campylobacter lari str. RM2100, Campylobacter lari strain RM2100
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