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:
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Gene Fusion
Cooccurrence
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Experiments
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[Homology]
Score
fabDMalonyl CoA-ACP transacylase; Derived by automated computational analysis using gene prediction method: Protein Homology. (314 aa)    
Predicted Functional Partners:
fabF
3-oxoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
 0.999
fabF-2
3-oxoacyl-ACP synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
 0.999
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
 
 0.993
fabH
3-oxoacyl-ACP synthase; 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.
 
 
 0.991
KLV26685.1
3-oxoacyl-ACP synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.990
accD
acetyl-CoA carboxyl transferase; Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA; Belongs to the AccD/PCCB family.
 
 
 0.988
fabG-3
3-oxoacyl-ACP reductase; Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. Belongs to the short-chain dehydrogenases/reductases (SDR) family.
 
 0.984
accA
acetyl-CoA carboxylase subunit alpha; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
 
 
 0.979
dltC
Alanine-phosphoribitol ligase; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
  
 0.966
KLV26247.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.946
Your Current Organism:
Bacillus circulans
NCBI taxonomy Id: 1397
Other names: ATCC 24, ATCC 4513, ATCC 9140, B. circulans, BCRC 10605, Bacillus sp. 3399BRRJ, Bacillus sp. NCIM 2107, Bacillus sp. NCIM 5045, Bacillus sp. NCIM 5046, CCM 2048, CCRC 10605, CCRC:10605, CCUG 7416, CIP 52.75, DSM 11, IAM 12462, IFO 13626, JCM 2504, LMG 13261, LMG 6926, LMG:13261, LMG:6926, NBRC 13626, NCCB 75011, NCIB 9374, NCIMB 9374, NCTC 2610, NRRL B-378, NRRL B-380
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