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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
secDProtein-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. (403 aa)    
Predicted Functional Partners:
secF
Protein translocase subunit secF; 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.
0.999
Swol_1427
KEGG: tma:TM0859 preprotein translocase YajC subunit.
  
  
 0.938
Swol_0277
Preprotein translocase, SecG subunit; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family.
 
 
 
 0.892
secY
Protein translocase subunit secY/sec61 alpha; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
  
 
 0.881
secE
Protein translocase subunit secE/sec61 gamma; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
  
 
 0.863
Swol_1426
Metal dependent phosphohydrolase; KEGG: chy:CHY_1513 HDIG domain protein, ambiguity.
       0.764
queA
S-adenosylmethionine tRNA ribosyltransferase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
  
  
 0.717
tgt
Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...]
  
    0.707
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.
  
    0.672
atpA
Sodium-transporting two-sector ATPase; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.
  
    0.646
Your Current Organism:
Syntrophomonas wolfei Goettingen
NCBI taxonomy Id: 335541
Other names: S. wolfei subsp. wolfei str. Goettingen G311, Syntrophomonas wolfei str. Goettingen, Syntrophomonas wolfei subsp. wolfei Goettingen, Syntrophomonas wolfei subsp. wolfei str. Goettingen, Syntrophomonas wolfei subsp. wolfei str. Goettingen G311, Syntrophomonas wolfei subsp. wolfei str. Gottingen, Syntrophomonas wolfei subsp. wolfei strain Goettingen
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