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
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[Homology]
Score
sgsA3The N-sulfoglucosamine sulfohydrolase, called also Sulfoglucosamine sulfamidase is involved in the glycosaminoglycan degradation. It hydrolyzes the N-sulfate groups from the D-glucosamine-N-sulfate-6-O-sulfate residues in heparan sulfate and heparin; Belongs to the family 1 of sulfatases (S1: formylglycine-dependent sulfatases), subfamily 8; Signal peptide putatively cleaved between the residues 25 and 26; Possibly localized in the periplasmic space; High confidence in function and specificity. (496 aa)    
Predicted Functional Partners:
CAZ96356.1
Alpha-galactosidase, family GH110; Alpha-galactosidase catalyzes the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides. Belongs to the family 110 of the glycoside hydrolases. Likely adopts a right handed parallel beta-helix fold. Signal peptide cleaved between the residues 19 and 20. Localized in the periplasmic space; High confidence in function and specificity.
 
     0.849
CAZ96355.1
Alpha-galactosidase, family GH110; Alpha-galactosidase catalyzes the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides. Belongs to the family 110 of the glycoside hydrolases. Likely adopts a right handed parallel beta-helix fold. Signal peptide cleaved between the residues 26 and 27. Localized in the periplasmic space; High confidence in function and specificity.
 
     0.830
CAZ96353.1
Sulfatase, family S1-16; The family 1 of sulfatases is composed of enzymes that require the posttranslational oxidation of a conserved cysteine (or serine) to a catalytic formylglycine to hydrolyze various sulfate ester substrates; Belongs to the family 1 of sulfatases (S1: formylglycine-dependent sulfatases), subfamily 16; Signal peptide cleaved between the residues 19 and 20; Localized in the periplasmic space; Family membership.
 
    
0.804
CAZ96354.1
Sulfatase, family S1-20; Modular protein consisting of a N-terminal domain belonging to the family 1 of sulfatases and a C-terminal PA14 domain putatively involved in the protein or carbohydrate binding; The family 1 of sulfatases is composed of enzymes that require the posttranslational oxidation of a conserved cysteine (or serine) to a catalytic formylglycine to hydrolyze various sulfate ester substrates; Belongs to the family 1 of sulfatases (S1: formylglycine-dependent sulfatases), subfamily 20; Contains a lipoprotein signal peptide cleaved between the residues 22 and 23; Localized [...]
 
    
0.745
sgsA4
The N-sulfoglucosamine sulfohydrolase, called also Sulfoglucosamine sulfamidase is involved in the glycosaminoglycan degradation. It hydrolyzes the N-sulfate groups from the D-glucosamine-N-sulfate-6-O-sulfate residues in heparan sulfate and heparin; Belongs to the family 1 of sulfatases (S1: formylglycine-dependent sulfatases), subfamily 8; Lipoprotein with a signal peptide cleaved between the residues 26 and 27; Localized in the outer membrane; High confidence in function and specificity.
 
    
0.665
CAZ96376.1
The sensor proteins consist of a sensing beta-propeller fold periplasmic domain, variable in sequence, reflective of the many different environmental signals, and of a cytoplasmic part composed of a histidine kinase domain, a response regulator receiver domain and a response regulator effector domain (here a C-terminal AraC- type HTH domain); Contains one transmembrane segment; Localized in the cytoplasmic membrane; Family membership.
 
     0.635
CAZ96358.1
SusD/RagB family lipoprotein; Protein probably involved in nutrient binding and belonging to the SusD/RagB family; Gene very often associated with a gene encoding for a TonB-dependent receptor or transducer; Contains a lipoprotein signal peptide cleaved between the residues 22 and 23; Probably localized in the outer membrane; Family membership.
 
     0.598
CAZ96458.1
The sensor proteins consist of a sensing beta-propeller fold periplasmic domain, variable in sequence, reflective of the many different environmental signals, and of a cytoplasmic part composed of a histidine kinase domain, a response regulator receiver domain and a response regulator effector domain (here a C-terminal AraC- type HTH domain); Contains one transmembrane segment; Localized in the cytoplasmic membrane; Family membership.
 
     0.570
CAZ96359.1
TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules (here, the sulphated sugars) that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (35-109) and the Plug module (125-232) acting as a channel gate; The signal peptide is cleaved between the residues 32 and 33; Family membership.
 
     0.458
CAZ96828.1
Sugar-phosphate isomerases catalyse the conversion of sugar-phosphate to another sugar-phosphate; Contains a Glucose-6-phosphate isomerase domain; Binds 1 iron ion per subunit; Belongs to the cupin superfamily, archaeal-type GPI family; Localized in the cytoplasm; Specificity unclear.
  
     0.441
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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