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.
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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
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[Homology]
Score
CCQ73861.1Putative hydrolase of the metallo-beta-lactamase superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (551 aa)    
Predicted Functional Partners:
birA
Biotin--[acetyl-CoA-carboxylase] synthetase; Function of strongly homologous gene; enzyme.
     0.916
coaX
Type III pantothenate kinase; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
       0.838
ispB
Octaprenyl diphosphate synthase; Function of strongly homologous gene; enzyme; Belongs to the FPP/GGPP synthase family.
  
    0.711
CCQ74145.1
Putative Geranyltranstransferase (Farnesyl-diphosphate synthase) (FPP synthase); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the FPP/GGPP synthase family.
  
    0.711
nuoN
NADH-quinone oxidoreductase chain N (NADH dehydrogenase I, chain N) (NDH-1, chain N); 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 subunit 2 family.
  
    0.694
nuoL
NADH-quinone oxidoreductase chain L (NADH dehydrogenase I, chain L) (NDH-1, chain L); Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
    0.693
tolB
Protein tolB precursor; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
      0.690
nuoM
NADH-quinone oxidoreductase chain M (NADH dehydrogenase I, chain M) (NDH-1, chain M); Function of homologous gene experimentally demonstrated in an other organism; enzyme.
       0.688
nuoK
NADH-quinone oxidoreductase chain K (NADH dehydrogenase I, chain K) (NDH-1, chain K); 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 subunit 4L family.
       0.688
nuoJ
NADH-quinone oxidoreductase chain J (NADH dehydrogenase I, chain J) (NDH-1, chain J); 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.
       0.688
Your Current Organism:
Magnetospira sp. QH2
NCBI taxonomy Id: 1288970
Other names: M. sp. QH-2, Magnetospira sp. QH-2, marine magnetic spirillum QH-2
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