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
pldBLysophospholipase L2; Similar to Escherichia coli lysophospholipase L2 PldB or b3825 SWALL:PLDB_ECOLI (SWALL:P07000) (340 aa) fasta scores: E(): 3e-78, 59.56% id in 324 aa. (345 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.
   
 
 0.966
aas
Aas bifunctional protein [includes: 2-acylglycerophosphoethanolamine acyltransferase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
  
 0.948
pldA
Phospholipase A1; Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Belongs to the phospholipase A1 family.
    
 0.918
ECA2428
Similar to Xanthomonas axonopodis glycerophosphodiester phosphodiesterase GlpQ or xac1147 SWALL:Q8PNC6 (EMBL:AE011744) (273 aa) fasta scores: E(): 1.4e-20, 32.25% id in 279 aa, and to Agrobacterium tumefaciens hypothetical protein atu4572 atu4572 or agr_l_598 SWALL:Q8U782 (EMBL:AE009385) (306 aa) fasta scores: E(): 1.1e-38, 39.31% id in 262 aa.
    
 0.914
glpQ
Similar to Escherichia coli glycerophosphoryl diester phosphodiesterase, periplasmic precursor GlpQ or b2239 SWALL:GLPQ_ECOLI (SWALL:P09394) (358 aa) fasta scores: E(): 4e-103, 72.7% id in 359 aa.
    
 0.914
ugpQ
Similar to Escherichia coli glycerophosphoryl diester phosphodiesterase UgpQ or b3449 SWALL:UGPQ_ECOLI (SWALL:P10908) (247 aa) fasta scores: E(): 1.3e-71, 73.55% id in 242 aa.
    
 0.914
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.
   
 
 0.900
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.
   
 
 0.876
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.
   
   0.844
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.
   
   0.734
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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