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
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
ECA0879Putative zinc protease; Similar to Escherichia coli probable zinc protease PqqL or b1494 SWALL:PQQL_ECOLI (SWALL:P31828) (931 aa) fasta scores: E(): 1.1e-43, 25.42% id in 948 aa, and to Pasteurella multocida PqqL or pm0804 SWALL:Q9CML5 (EMBL:AE006119) (923 aa) fasta scores: E(): 1.9e-47, 23.52% id in 948 aa; deleted EC_number 3.4.99.-; Belongs to the peptidase M16 family. (924 aa)    
Predicted Functional Partners:
nuoC
NADH-quinone oxidoreductase chain C/D; 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 30 kDa subunit family.
   
 
 0.990
nuoF
NADH-quinone oxidoreductase chain F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
 0.882
nuoG
NADH-quinone oxidoreductase chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. Belongs to the complex I 75 kDa subunit family.
   
 0.862
atpH
ATP synthase delta chain; 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.
   
 0.851
atpA
ATP synthase alpha chain; 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.
   
 0.833
nuoE
NADH-quinone oxidoreductase chain E; Similar to Escherichia coli, Escherichia coli O6, and Shigella flexneri NADH-quinone oxidoreductase chain E NuoE or b2285 or c2826 or sf2361 SWALL:NUOE_ECOLI (SWALL:P33601) (166 aa) fasta scores: E(): 2.7e-53, 84.27% id in 159 aa.
   
 
 0.830
ECA0880
Putative ABC transporter ATP-binding protein; Similar to Pasteurella multocida hypothetical protein Pm0041 SWALL:Q9CPJ6 (EMBL:AE006038) (564 aa) fasta scores: E(): 7.9e-99, 48.01% id in 554 aa, and to Escherichia coli hypothetical ABC transporter ATP-binding protein YddA SWALL:YDDA_ECOLI (SWALL:P31826) (561 aa) fasta scores: E(): 5.7e-71, 38.24% id in 536 aa.
  
  
 0.815
nuoB
NADH-quinone oxidoreductase chain B; 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.
   
 
 0.736
cyoA
Similar to Escherichia coli, and Escherichia coli O6 ubiquinol oxidase polypeptide ii precursor CyoA or b0432 or c0543 SWALL:CYOA_ECOLI (SWALL:P18400) (315 aa) fasta scores: E(): 2.4e-82, 67.18% id in 320 aa.
   
 0.727
cyoC
Cytochrome o ubiquinol oxidase subunit III; Similar to Escherichia coli, Escherichia coli O6, and Shigella flexneri cytochrome o ubiquinol oxidase subunit iii CyoC or b0430 or c0541 or sf0371 SWALL:CYOC_ECOLI (SWALL:P18402) (204 aa) fasta scores: E(): 2.7e-67, 78.53% id in 205 aa.
   
 0.721
Your Current Organism:
Pectobacterium atrosepticum
NCBI taxonomy Id: 218491
Other names: Erwinia carotovora subsp. atroseptica SCRI1043, Erwinia carotovora subsp. atroseptica str. SCRI1043, P. atrosepticum SCRI1043, Pectobacterium atrosepticum SCRI1043, Pectobacterium atrosepticum str. SCRI1043, Pectobacterium atrosepticum strain SCRI1043, Pectobacterium carotovora subsp. atroseptica SCRI1043, Pectobacterium carotovora subsp. atroseptica str. SCRI1043
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