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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene co-occurrence
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[Homology]
Score
Pcar_1981Zinc-dependent peptidase, M16 family; Belongs to the peptidase M16 family. (498 aa)    
Predicted Functional Partners:
nuoBCD
NADH dehydrogenase I, B/C/D subunits; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 20 kDa subunit family. In the C-terminal section; belongs to the complex I 49 [...]
  
 
 0.998
Pcar_1980
Zinc-dependent peptidase lipoprotein, M16 family.
  
0.991
hndC-5
NADPH oxidoreductase, major subunit.
  
 0.956
Pcar_2745
Cytochrome c; 3 heme-binding sites.
  
 0.842
Pcar_0020
NAD-dependent nucleoside diphosphate-sugar epimerase/dehydratase.
   
 
 0.752
coxB
Cytochrome c oxidase, coo3-type, cytochrome c subunit II, one heme-binding site; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
   
 
 0.729
coxC
Cytochrome c oxidase, coo3-type, subunit III.
   
   0.715
atpH-1
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.
   
 0.712
atpH-3
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.
   
 0.712
lon-1
ATP-dependent Lon protease (La); ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
  
 
 0.706
Your Current Organism:
Pelobacter carbinolicus
NCBI taxonomy Id: 338963
Other names: P. carbinolicus DSM 2380, Pelobacter carbinolicus DSM 2380, Pelobacter carbinolicus Gra Bd 1, Pelobacter carbinolicus str. DSM 2380, Pelobacter carbinolicus strain DSM 2380
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