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minD minD mnmG mnmG rsmG rsmG mnmE mnmE mreB mreB yhdE yhdE nadB nadB pta pta nadC nadC lacZ lacZ sbcC sbcC sbcD sbcD maa maa nadA nadA fabF fabF
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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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
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Your Input:
minDInhibitor of FtsZ ring polymerization; ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. (270 aa)
mnmG5-methylaminomethyl-2-thiouridine modification at tRNA U34; NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. (629 aa)
rsmG16S rRNA m(7)G527 methyltransferase, SAM-dependent; Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. Requires the intact 30S subunit for methylation; Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family. (207 aa)
mnmEtRNA U34 5-methylaminomethyl-2-thiouridine modification GTPase; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34. (454 aa)
mreBCell wall structural complex MreBCD, actin-like component MreB; Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization maintains elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreB polyme [...] (347 aa)
yhdEdTTP/UTP pyrophosphatase; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze TTP and the modified nucleotides 5-methyl-UTP (m(5)UTP), pseudo-UTP and 5-methyl-CTP (m(5)CTP). Has weak activity with CTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. Important in maintenance of cell shape. (197 aa)
nadBQuinolinate synthase, L-aspartate oxidase (B protein) subunit; Catalyzes the oxidation of L-aspartate to iminoaspartate. (540 aa)
ptaPhosphate acetyltransferase; Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA is converted to acetate and allowing the cell to dump the excess of acetylation potential in exchange for energy in the form of ATP. In the N-terminal section; belongs to the CobB/CobQ family. (714 aa)
nadCQuinolinate phosphoribosyltransferase; Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. (297 aa)
lacZbeta-D-galactosidase; Protein involved in carbohydrate catabolic process; Belongs to the glycosyl hydrolase 2 family. (1024 aa)
sbcCExonuclease, dsDNA, ATP-dependent; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity. (1048 aa)
sbcDExonuclease, dsDNA, ATP-dependent; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity; Belongs to the SbcD family. (400 aa)
maaMaltose O-acetyltransferase; Catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars. Acetylates glucose exclusively at the C6 position and maltose at the C6 position of the non-reducing end glucosyl moiety. Is able to acetylate maltooligosaccharides ; Belongs to the transferase hexapeptide repeat family. (183 aa)
nadAQuinolinate synthase, subunit A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. Belongs to the quinolinate synthase A family. Type 1 subfamily. (347 aa)
fabF3-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. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis. (413 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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