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glcB glcB fis fis typA typA fadB fadB fadA fadA fadR fadR chiP chiP acrR acrR phoB phoB fadE fadE rnhA rnhA rpsL rpsL fadD fadD fliC fliC maeB maeB
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
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textmining
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Your Input:
glcBMalate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA. (723 aa)
fisGlobal DNA-binding transcriptional dual regulator; Activates ribosomal RNA transcription, as well other genes. Plays a direct role in upstream activation of rRNA promoters. Binds to a recombinational enhancer sequence that is required to stimulate hin- mediated DNA inversion. Prevents initiation of DNA replication from oriC. Binds to hundreds of transcriptionally active and inactive AT- rich sites, approximately half its binding sites are in non-coding DNA, which only accounts for about 10% of the genome. Belongs to the transcriptional regulatory Fis family. (98 aa)
typAGTP-binding protein; A 50S ribosomal subunit assembly protein with GTPase and nucleotide-independent chaperone activity. Genetic and deletion evidence suggests this is involved in ribosome assembly at low temperatures; it may also affect translation (Probable). Involved in incorporation of ribosomal protein L6 into precursor 44S ribosomal particles at low temperatures. Also has chaperone activity which does not require nucleotides. Binds GDP, ppGpp and GDPCP (a nonhydrolyzable GTP analog) with similar affinity; the conformation of the protein does not significantly change upon nucleoti [...] (607 aa)
fadBEnoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (729 aa)
fadA3-ketoacyl-CoA thiolase (thiolase I); Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids. (387 aa)
fadRFatty acid metabolism regulon transcriptional regulator; Multifunctional regulator of fatty acid metabolism. Represses transcription of at least eight genes required for fatty acid transport and beta-oxidation including fadA, fadB, fadD, fadL and fadE. Activates transcription of at least three genes required for unsaturated fatty acid biosynthesis: fabA, fabB and iclR, the gene encoding the transcriptional regulator of the aceBAK operon encoding the glyoxylate shunt enzymes. (239 aa)
chiPChitoporin, uptake of chitosugars; Involved in the uptake of chitosugars. (468 aa)
acrRTranscriptional repressor; Potential regulator protein for the acrAB genes. (215 aa)
phoBResponse regulator in two-component regulatory system with PhoR; This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited. (229 aa)
fadEAcyl coenzyme A dehydrogenase; Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs) to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty acid degradation. Is required for E.coli to utilize dodecanoate or oleate as the sole carbon and energy source for growth. (814 aa)
rnhARibonuclease HI, degrades RNA of DNA-RNA hybrids; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. RNase H participates in DNA replication; it helps to specify the origin of genomic replication by suppressing initiation at origins other than the oriC locus; along with the 5'-3' exonuclease of pol1, it removes RNA primers from the Okazaki fragments of lagging strand synthesis; and it defines the origin of replication for ColE1-type plasmids by specific cleavage of an RNA preprimer. (155 aa)
rpsL30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy. Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit; Belongs to the universal ribosomal protein uS12 family. (124 aa)
fadDacyl-CoA synthetase (long-chain-fatty-acid--CoA ligase); Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Activity is the highest with fatty acid substrates of > 10 carbon atoms. Is involved in the aerobic beta- oxidative degradation of fatty acids, which allows aerobic growth of E.coli on fatty acids as a sole carbon and energy source. (561 aa)
fliCFlagellar filament structural protein (flagellin); Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (498 aa)
maeBMalic enzyme: putative oxidoreductase/phosphotransacetylase; Putative multimodular enzyme; In the N-terminal section; belongs to the malic enzymes family. (759 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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