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
acpPAcyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. (77 aa)    
Predicted Functional Partners:
SFA41925.1
[acyl-carrier-protein] S-malonyltransferase.
 
 0.999
SFA46618.1
Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
   
 0.999
SFA48910.1
NADH dehydrogenase subunit C.
   
 0.998
nuoB
NADH dehydrogenase subunit 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 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.
   
 0.997
SFA48919.1
NADH dehydrogenase subunit I.
   
 0.997
SFA48338.1
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains.
   
 0.994
nuoD
NADH dehydrogenase subunit 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 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.
   
 0.994
SFA54679.1
Deoxyadenosine/deoxycytidine kinase.
   
 0.994
SFA43100.1
3-oxoacyl-[acyl-carrier-protein] synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
 
 0.992
nuoH
NADH-quinone oxidoreductase subunit H; 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.
    
  0.991
Your Current Organism:
Parageobacillus thermantarcticus
NCBI taxonomy Id: 186116
Other names: BGSC 20A1, Bacillus thermantarcticus, Bacillus thermantarcticus corrig. Nicolaus et al. 2002, Bacillus thermoantarcticus, DSM 9572, Geobacillus sp. R-35644, Geobacillus thermantarcticus, Geobacillus thermantarcticus (Nicolaus et al. 2002) Coorevits et al. 2012, LMG 23032, LMG:23032, P. thermantarcticus, strain M1, strain R-35644
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