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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
acpPAcyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. (76 aa)    
Predicted Functional Partners:
fabD
Malonyl CoA-acyl carrier protein transacylase; Identified by similarity to SP:P25715; match to protein family HMM PF00698; match to protein family HMM TIGR00128.
 0.996
nuoCD
NADH dehydrogenase I, C/D subunits; 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.
   
 0.989
fabH-1
3-oxoacyl-(acyl-carrier-protein) synthase III; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids; Belongs to the thiolase-like superfamily. FabH family.
 
 
 0.984
fabF
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.
 
 0.980
rpmF
Ribosomal protein L32; Identified by similarity to SP:P02435; match to protein family HMM PF01783; match to protein family HMM TIGR01031; Belongs to the bacterial ribosomal protein bL32 family.
  
 0.973
fabZ
(3R)-hydroxymyristoyl-(acyl-carrier-protein) dehydratase; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
 
 
 0.964
MCA2577
Putative dehydrogenase subunit; Identified by similarity to GP:4007678; match to protein family HMM PF01257; match to protein family HMM PF01512.
   
 0.942
MCA2724
NAD-reducing hydrogenase, alpha subunit; Identified by similarity to SP:P22317; match to protein family HMM PF01257; match to protein family HMM PF01512.
   
 0.942
tmk
Thymidylate kinase; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis; Belongs to the thymidylate kinase family.
 
  
 0.940
fabB
3-oxoacyl-(acyl-carrier-protein) synthase I; Identified by similarity to SP:P14926; match to protein family HMM PF00109; match to protein family HMM PF02801; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
 
 
 0.936
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
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