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
lgtProlipoprotein diacylglyceryl transferase; Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins; Belongs to the Lgt family. (263 aa)    
Predicted Functional Partners:
trpA
Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
  
    0.876
trpB
Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
    0.847
nth
Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate.
  
    0.801
yidC
Membrane protein oxaA; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
 
  
 0.797
secF
Protein-export membrane protein SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily.
 
  
 0.689
alaS
alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
  
    0.665
AEH22720.1
Hypothetical protein.
       0.652
gpsA
KEGG: tye:THEYE_A0581 glycerol-3-phosphate dehydrogenase [NAD(P)+] (NAD(P)H-dependent glycerol-3-phosphate dehydrogenase) (NAD(P)H-dependentdihydroxyacetone-phosphate reductase); HAMAP: Glycerol-3-phosphate dehydrogenase [NAD(P)+]; PFAM: NAD-dependent glycerol-3-phosphate dehydrogenase, C-terminal; NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal.
  
    0.613
AEH22693.1
Hypothetical protein; KEGG: slp:Slip_2381 single-stranded nucleic acid binding R3H domain protein.
  
    0.583
AEH23694.1
Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family.
  
    0.569
Your Current Organism:
Thermodesulfobacterium geofontis
NCBI taxonomy Id: 795359
Other names: T. geofontis OPF15, Thermodesulfobacterium geofontis OPF15, Thermodesulfobacterium sp. OPF15
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.