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
CAZ98243.1Conserved hypothetical protein; Localized in the cytoplasm. (162 aa)    
Predicted Functional Partners:
suoX
Sulfite oxidase catalyzes oxidation of sulphite to sulphate, using cytochrome c as the physiological electron acceptor. It forms a homodimer and the monomer consists of an N-terminal heme domain, Contains a twin arginine translocation pathway signal peptide cleaved between the residues 21 and 22; Localized in the periplasm; High confidence in function and specificity.
 
   
 0.957
CAZ98244.1
Conserved protein belonging to the Fatty acid hydroxylase family. Members of this family are involved in cholesterol biosynthesis; Contains three transmembrane helices; Localized in the cytoplasmic membrane; Family membership.
 
     0.703
CAZ95761.1
Conserved hypothetical periplasmic protein; Contains a central Ig-like domain (residues 511-592); Signal peptide cleaved between the residues 26 and 27; Localized in the periplasmic space; Conserved hypothetical protein.
  
     0.536
CAZ95749.1
Conserved hypothetical protein; Localized in the cytoplasm.
  
     0.523
CAZ95263.1
N-Acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in peptidoglycan; Contains a signal peptide cleaved between the residues 27 and 28; Localized in the periplasmic space; High confidence in function and specificity.
  
     0.506
CAZ98310.1
Conserved protein containing a von Willebrand factor type A (vWF) domain. vWF domains adopt a classic alpha/beta Rossmann fold and usually contains an unusual metal ion coordination site at its surface. Its exact function is unknown. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Family membership.
  
     0.488
CAZ95760.1
Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein.
  
     0.478
CAZ94686.1
Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein.
  
     0.465
CAZ95967.1
Conserved hypothetical membrane protein; Contains a putative putative lipoprotein signal peptide cleaved between the residues 29 and 30; Possibly localized in the cytoplasm or outer membrane; Conserved hypothetical protein.
  
     0.463
CAZ98162.1
The response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. The protein consists of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA-binding activity, a LytTR-type HTH domain, which acts as transcriptional regulator; Localized in the cytoplasm; Family membership.
  
     0.451
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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