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.
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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Deba_2173WbqC-like family protein; InterPro IPR014985; KEGG: psb:Psyr_1578 hypothetical protein; PFAM: WbqC-like family protein; SPTR: Q4ZW46 Putative uncharacterized protein; PFAM: WbqC-like protein family. (235 aa)    
Predicted Functional Partners:
atpA
ATP synthase F1, alpha subunit; 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.
  
 0.971
atpD
ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.
  
 0.971
atpC
ATP synthase F1, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.
  
 0.971
atpH
ATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family.
  
 0.968
atpB-2
ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
  
 0.967
Deba_1450
H+transporting two-sector ATPase C subunit; InterPro IPR002379; KEGG: pcu:pc1676 V-type ATP synthase subunit K; PFAM: H+transporting two-sector ATPase C subunit; SPTR: Q6MAJ9 Putative V-type sodium ATP synthase subunit K (NtpK); PFAM: ATP synthase subunit C.
  
 0.938
atpE
ATP synthase F0, C subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
  
 0.938
atpF
H+transporting two-sector ATPase B/B' subunit; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family.
  
 
 0.919
atpF-2
ATP synthase F0, B subunit; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family.
  
 
 0.919
Deba_1755
Rieske (2Fe-2S) iron-sulfur domain protein; COGs: COG0723 Rieske Fe-S protein; InterPro IPR017941:IPR005805:IPR017909; KEGG: sth:STH3146 plastoquinol--plastocyanin reductase; PFAM: Rieske [2Fe-2S] iron-sulphur domain; SPTR: Q67JM2 Plastoquinol--plastocyanin reductase; PFAM: Rieske [2Fe-2S] domain.
   
 
 0.854
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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