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
CAZ98392.1Conserved hypothetical protein; Protein that consists of an TfoX module found in the N-terminal part of the tfoX gene product required for DNA transformation; Localized in the cytoplasm. (108 aa)    
Predicted Functional Partners:
kefC
The K(+)/H(+) antiporter KefC is a Glutathione-regulated potassium-efflux system protein responsible for glutathione-gated K+ efflux. Activation of KefC K+ efflux system only occurs in the presence of glutathione and a reactive electrophile such as methylglyoxal or N-ethylmaleimide. KefC is important for cell survival during exposure to toxic metabolites, possibly because they can release K+, allowing H+ uptake. H+ uptake (acidification of the cytoplasm) accompanying or following K+ efflux may serve as a further protective mechanism against electrophile toxicity; Contains 12 transmembr [...]
 
     0.820
kefF
K+/H+ antiporter, ancillary protein KefF, also called Glutathione-regulated potassium-efflux system ancillary protein is required for full activity of KefC. This ancillary protein stimulates transport activity of KefC about 10-fold. It is unlikely that kefF has oxidoreductase activity, it has probably evolved from its function as oxidoreductase to be regulator of kefC; Belongs to the NAD(P)H dehydrogenase (quinone) family; Localized in the cytoplasm; High confidence in function and specificity.
       0.757
CAZ95076.1
Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein.
  
     0.674
CAZ98552.1
Conserved hypothetical protein; Localized in the cytoplasm.
 
     0.668
CAZ97788.1
Conserved hypothetical protein; Contains a N-terminal DUF 11 domain. Protein that would bind calcium ions by several EF-hand calcium-binding domains or/and by trombospondin type III domains; Signal peptide cleaved between the residues 27 and 28; Putatively localized in the outer membrane.
  
     0.649
CAZ96815.1
Modular protein containing a N-terminal domain adopting a parallel beta-helix fold and a C-terminal carbohydrate binding module of the family 13 (CBM13). The N-terminal domain is distantly related to the polysaccharide lyases of the family 9 (PL9). Features a signal peptide cleaved between residues 26 and 27. Localized in the periplasm; Specificity unclear.
  
     0.629
CAZ96814.1
Beta-helix fold protein; This protein likely adopts a right handed parallel beta-helix fold. Displays also a C-terminal PKD domain; Signal peptide cleaved between the residues 28 and 29; Localized in the periplasmic space; Function unclear.
  
     0.611
CAZ98389.1
Putative protein.
       0.542
CAZ95328.1
Glycoside hydrolase, family GH114; Glycoside hydrolases hydrolyse the glycosidic bond between two or more carbohydrates or between a carbohydrate and a non-carbohydrate moiety. Belongs to the family 114 of the glycoside hydrolases. Family GH114 contains endo-alpha-1,4-polygalactosaminidases, but the specificity of this protein is unclear. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 29 and 30. Localized in the outer membrane; Specificity unclear.
  
     0.498
npdA
NAD-dependent deacetylase activates the enzyme acetyl-CoA synthetase by deacetylating its catalytic Lysine in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. It binds one zinc ion as a cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the sirtuin family. Class III subfamily.
   
   0.495
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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