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
CAZ95026.1Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 27 and 28; Localized in the periplasmic space; Conserved hypothetical protein. (185 aa)    
Predicted Functional Partners:
CAZ95025.1
Conserved hypothetical protein; Localized in the cytoplasm.
       0.601
phhA
Phenylalanine 4-monooxygenase, also known as phenylalanine-4-hydroxylase, is involved in L-phenylalanine biodegradation. It catalyzes the reaction: L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin. It binds Fe(2+) ion as a cofactor. PhhA belongs to the biopterin-dependent aromatic amino acid hydroxylase family. Localized in the cytoplasm; High confidence in function and specificity.
 
     0.588
CAZ96483.1
This enzyme belongs to the family 2 of the aspartic peptidases. An activated water molecule is the nucleophile these peptidases and is bound by two aspartic residues, one from each monomer of the homo-dimeric molecule. Localized in the cytoplasm; Specificity unclear.
  
     0.543
CAZ98112.1
Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein.
  
     0.486
CAZ97071.1
Conserved hypothetical protein; Localized in the cytoplasm.
  
     0.455
dcyD
D-cysteine desulfhydrase catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D-alanine. It uses pyridoxal phosphate as a cofactor. Localized in the cytoplasm; High confidence in function and specificity.
 
     0.449
porT
PorT is essential for the transport of some proteins across the outer membrane from the periplasm to the cell surface; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; High confidence in function and specificity.
  
     0.445
CAZ96606.1
Conserved hypothetical protein; Signal peptide possibly cleaved between the residues 18 and 19; Putatively localized in the outer membrane.
  
     0.439
CAZ95024.1
Conserved hypothetical protein; Localized in the cytoplasm.
       0.433
sprE
The SprE protein could be involved in the gliding motility; Contains four tetratrico peptide repeats (TPRs). TPRs mediate proteinprotein interactions. TPR adopts a helixturnhelix arrangement, with adjacent TPR motifs packing in a parallel fashion, resulting in a spiral of repeating anti-parallel alpha-helices. SprE contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the outer membrane; Function unclear.
  
     0.423
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: medium (42%) [HD]