close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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
nucSNuclease S1 hydrolyzes only single stranded DNA and RNA without apparent specificity for bases; Binds 3 zinc ions as cofactors; Localized in the cytoplasm; High confidence in function and specificity. (256 aa)    
Predicted Functional Partners:
pbp1B
Penicillin-binding protein 1B, family GT51; Penicillin-binding protein 1B is a class A PBP involved in the synthesis of cross-linked peptidoglycan from the lipid II intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). The N-terminal domain belongs to the family 51 of the glycosyltransferases. Features an uncleaved signal peptide. Localized in the periplasm, anchored to the cytoplasmic membrane; High confidence in [...]
       0.543
CAZ94691.1
The hydrolases of the superfamily HAD (Haloacid dehalogenase) catalyse a nucleophilic displacement reaction, with water as the sole co-substrate. They are structurally different from the alpha/beta hydrolase family (abhydrolase); Belongs to the haloacid dehalogenase- like hydrolase superfamily, class II family, class IIB subfamily; Localized in the cytoplasm; Family membership.
       0.496
CAZ96470.1
TonB-dependent Transducer; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins; The presence of an additional N-terminal extension (Secretin/TonB (STN) domain (59-110)) that probably interacts with an anti-sigma factor, would be responsible of the signal transduction; Contains a carboxypeptidase regulatory domain (120-194) and the Plug module (212-335); The signal peptide is cleaved between the residue 29 and 30; Family membership.
  
     0.490
CAZ96996.1
TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (21-92) and the Plug module (109-232) acting as a channel gate; The signal peptide is cleaved between the residues 21 and 22; Family membership.
  
     0.468
CAZ94692.1
Conserved protein belonging to the DUF819 family. Features eleven transmembrane helices; Localized in the cytoplasmic membrane; Family membership.
       0.437
CAZ97825.1
Conserved hypothetical membrane protein; Contains four transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
  
     0.431
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
Server load: low (34%) [HD]