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
ABS23790.1KEGG: btl:BALH_4529 possible PAP2 family protein. (219 aa)    
Predicted Functional Partners:
nuoH
NADH dehydrogenase (quinone); 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. This subunit may bind ubiquinone.
   
 
 0.932
ABS24007.1
TIGRFAM: NADH (or F420H2) dehydrogenase, subunit C; PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; KEGG: bat:BAS5148 NADH dehydrogenase I, C subunit, putative.
   
 0.864
ABS23215.1
PFAM: protein of unknown function DUF185; KEGG: bat:BAS4162 hypothetical protein.
     
 0.843
ABS24004.1
TIGRFAM: NADH-quinone oxidoreductase, chain I; PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: btk:BT9727_4977 NADH dehydrogenase I, subunit I (NADH-quinone oxidoreductase, chain I).
   
 
 0.837
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 a menaquinone. 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.
   
 
 0.835
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 a menaquinone. 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.
   
 
 0.824
ABS21841.1
PFAM: NAD-dependent epimerase/dehydratase; KEGG: bce:BC2022 oxidoreductase.
    
 0.812
ABS23487.1
TIGRFAM: glyceraldehyde-3-phosphate dehydrogenase, type I; PFAM: glyceraldehyde 3-phosphate dehydrogenase; KEGG: bat:BAS4478 glyceraldehyde 3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
   
  
 0.716
ABS23879.1
TIGRFAM: glyceraldehyde-3-phosphate dehydrogenase, type I; PFAM: glyceraldehyde 3-phosphate dehydrogenase; KEGG: bca:BCE_5242 glyceraldehyde-3-phosphate dehydrogenase; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
   
  
 0.716
ABS21543.1
PFAM: RNA binding S1 domain protein; KEGG: bce:BC1498 30S ribosomal protein S1.
   
    0.699
Your Current Organism:
Bacillus cytotoxicus
NCBI taxonomy Id: 315749
Other names: B. cytotoxicus NVH 391-98, Bacillus cereus NVH 391-98, Bacillus cereus subsp. cytotoxicus NVH 391-98, Bacillus cereus subsp. cytotoxis NVH 391-98, Bacillus cytotoxicus NVH 391-98, Bacillus cytotoxicus str. NVH 391-98, Bacillus cytotoxicus strain NVH 391-98, Bacillus cytotoxis NVH 391-98
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