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
ACX96340.1PFAM: KR domain protein; Acyl transferase; Beta-ketoacyl synthase; Alcohol dehydrogenase GroES domain protein; Alcohol dehydrogenase zinc-binding domain protein; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KEGG: neu:NE1389 putative type I polyketide synthase WcbR. (2507 aa)    
Predicted Functional Partners:
ACX95386.1
TIGRFAM: tol-pal system-associated acyl-CoA thioesterase; PFAM: thioesterase superfamily protein; KEGG: mca:MCA1224 thioesterase family protein.
  
 
 0.999
ACX95796.1
PFAM: KR domain protein; Beta-ketoacyl synthase; Alcohol dehydrogenase GroES domain protein; short-chain dehydrogenase/reductase SDR; Acyl transferase; Alcohol dehydrogenase zinc-binding domain protein; phosphopantetheine-binding; NAD-dependent epimerase/dehydratase; KEGG: npu:Npun_F3360 beta-ketoacyl synthase.
 
 
0.999
ACX96747.1
TIGRFAM: malonyl CoA-acyl carrier protein transacylase; PFAM: Acyl transferase; KEGG: tbd:Tbd_1550 [acyl-carrier-protein] S-malonyltransferase.
 
0.999
nuoC
NADH (or F420H2) dehydrogenase, subunit C; 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; Belongs to the complex I 30 kDa subunit family.
   
 0.998
ACX96388.1
PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: csa:Csal_2936 4Fe-4S ferredoxin, iron-sulfur binding.
   
 0.997
ACX96612.1
PFAM: NADH ubiquinone oxidoreductase 20 kDa subunit; 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: acr:Acry_0607 NADH ubiquinone oxidoreductase, 20 kDa subunit.
   
 0.997
ACX96656.1
PFAM: AMP-dependent synthetase and ligase; KEGG: noc:Noc_1956 AMP-dependent synthetase and ligase.
 
 0.997
nuoI
NADH-quinone oxidoreductase, chain I; 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.
   
 0.997
nuoD
NADH dehydrogenase I, D subunit; 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; Belongs to the complex I 49 kDa subunit family.
   
 0.997
nuoB
NADH-quinone oxidoreductase, B subunit; 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.
   
 0.997
Your Current Organism:
Halothiobacillus neapolitanus
NCBI taxonomy Id: 555778
Other names: H. neapolitanus c2, Halothiobacillus neapolitanus ATCC 23641, Halothiobacillus neapolitanus c2, Halothiobacillus neapolitanus str. c2, Halothiobacillus neapolitanus strain c2
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