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
Oant_2983PFAM: protein of unknown function DUF6 transmembrane; KEGG: sme:SMc02855 hypothetical protein. (313 aa)    
Predicted Functional Partners:
Oant_2984
PFAM: extracellular solute-binding protein family 5; KEGG: atc:AGR_L_3099 putative ABC transporter.
       0.527
Oant_2982
PFAM: monooxygenase FAD-binding; KEGG: nwi:Nwi_2327 hypothetical protein.
  
    0.446
Oant_0785
PFAM: protein of unknown function DUF1330; KEGG: bmb:BruAb1_2104 hypothetical protein.
  
     0.401
Oant_2985
PFAM: binding-protein-dependent transport systems inner membrane component; KEGG: atc:AGR_L_3101 probable peptide ABC transporter permease protein Y4TP.
       0.401
Oant_2986
PFAM: binding-protein-dependent transport systems inner membrane component; KEGG: atc:AGR_L_3102 dipeptide abc transporter, dipeptide-binding protein.
       0.401
Oant_2987
Amidohydrolase; Esterase that catalyzes the deacetylation of acetyl-(R)- mandelate (in vitro). Can also hydrolyze acetyl glycolate, but with lower efficiency. Has very low N-acetyl-D-amino acid deacetylase activity with N-acetyl-D-serine and N-acetyl-D-threonine (in vitro). Theoretical substrate docking studies suggest that other N-acetylated amino acids may optimally occupy the active site and may in fact be the physiological substrates.
       0.401
Your Current Organism:
Ochrobactrum anthropi
NCBI taxonomy Id: 439375
Other names: O. anthropi ATCC 49188, Ochrobactrum anthropi ATCC 49188, Ochrobactrum anthropi DSM 6882, Ochrobactrum anthropi LMG 3331, Ochrobactrum anthropi str. ATCC 49188, Ochrobactrum anthropi strain ATCC 49188
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