STRINGSTRING
plsX plsX plsC plsC plsY plsY glpD glpD ugpQ ugpQ sgbE sgbE tpiA tpiA glpK glpK ulaF ulaF gcvH gcvH talA talA glpQ glpQ fliQ fliQ fliO fliO fliN fliN fliM fliM fliL fliL fliI fliI fliG fliG fliC fliC fliA fliA motB motB cheW cheW cheR cheR araA araA araD araD talB talB gcvT gcvT
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
Your Input:
plsXPutative phosphate acyltransferase; Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. (356 aa)
plsC1-acyl-sn-glycerol-3-phosphate acyltransferase; Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the 2 position. This enzyme can utilize either acyl-CoA or acyl-ACP as the fatty acyl donor. Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. (245 aa)
plsYPutative glycerol-3-phosphate acyltransferase; Catalyzes the transfer of an acyl group from acyl-ACP to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme can also utilize acyl-CoA as fatty acyl donor, but not acyl- PO(4) (Probable); Belongs to the PlsY family. (205 aa)
glpDSn-glycerol-3-phosphate dehydrogenase, aerobic, FAD/NAD(P)-binding; Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor. (501 aa)
ugpQGlycerophosphodiester phosphodiesterase, cytosolic; Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols. (247 aa)
sgbEL-ribulose-5-phosphate 4-epimerase; Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction). May be involved in the utilization of 2,3-diketo-L-gulonate. (231 aa)
tpiATriosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (255 aa)
glpKGlycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP; Belongs to the FGGY kinase family. (502 aa)
ulaFL-ribulose 5-phosphate 4-epimerase; Catalyzes the isomerization of L-ribulose 5-phosphate to D- xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization; Belongs to the aldolase class II family. AraD/FucA subfamily. (228 aa)
gcvHGlycine cleavage complex lipoylprotein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. (129 aa)
talATransaldolase A; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. (316 aa)
glpQGlycerophosphodiester phosphodiesterase, periplasmic; Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols. (358 aa)
fliQFlagellar biosynthesis protein; Required for the assembly of the rivet at the earliest stage of flagellar biosynthesis; Belongs to the FliQ/MopD/SpaQ family. (89 aa)
fliOFlagellar biosynthesis; Protein involved in flagellum assembly and taxis. (121 aa)
fliNFlagellar motor switching and energizing component; FliN is one of three proteins (FliG, FliN, FliM) that form a switch complex that is proposed to be located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. (137 aa)
fliMFlagellar motor switching and energizing component; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. (334 aa)
fliLFlagellar biosynthesis protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (154 aa)
fliIFlagellum-specific ATP synthase; Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum. May be involved in a specialized protein export pathway that proceeds without signal peptide cleavage; Belongs to the ATPase alpha/beta chains family. (457 aa)
fliGFlagellar motor switching and energizing component; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. (331 aa)
fliCFlagellar filament structural protein (flagellin); Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (498 aa)
fliARNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. (239 aa)
motBProtein that enables flagellar motor rotation; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Probably a linker that fastens the torque-generating machinery to the cell wall. Overexpression of this protein with MotA improves motility in a pdeH disruption, (a c-di-GMP phosphodiesterase) suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein YcgR and the flagellar stator. (308 aa)
cheWPurine-binding chemotaxis protein; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. It physically bridges CheA to the MCPs (methyl-accepting chemotaxis proteins) to allow regulated phosphotransfer to CheY and CheB. (167 aa)
cheRChemotaxis regulator, protein-glutamate methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. (286 aa)
araAL-arabinose isomerase; Catalyzes the conversion of L-arabinose to L-ribulose. (500 aa)
araDL-ribulose-5-phosphate 4-epimerase; Involved in the degradation of L-arabinose. Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D- xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon- carbon bond cleavage analogous to a class II aldolase reaction). (231 aa)
talBTransaldolase B; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. (317 aa)
gcvTAminomethyltransferase, tetrahydrofolate-dependent, subunit (T protein) of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine. (364 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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