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yfiC yfiC valS valS miaA miaA yjeA yjeA lysU lysU yjbN yjbN trmA trmA yihZ yihZ rnpA rnpA spoU spoU rph rph yibK yibK selA selA glyQ glyQ glyS glyS trpS trpS fmt fmt yhdG yhdG truB truB cca cca yggH yggH lysS lysS yqcB yqcB ygbO ygbO argS argS aspS aspS yeaK yeaK thrS thrS pheS pheS tyrS tyrS hemA hemA pth pth asnS asnS smtA smtA serS serS glnS glnS leuS leuS cysS cysS ybbB ybbB ybaK ybaK yajK yajK tgt tgt queA queA proS proS yadB yadB yabO yabO ileS ileS trmD trmD yfiP yfiP yfgB yfgB hisS hisS gltX gltX yfcK yfcK truA truA yohI yohI metG metG
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query proteins and first shell of interactors
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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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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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yfiCHypothetical protein yfiC; Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC). (285 aa)
valSValyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (951 aa)
miaAtRNA delta(2)-isopentenylpyrophosphate transferase; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family. (316 aa)
yjeAPutative lysyl-tRNA synthetase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta- lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF- P 'Lys-34'; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. (352 aa)
lysULysyl-tRNA synthetase, heat inducible; Escherichia coli K-12 ortholog: b4129; Escherichia coli O157:H7 ortholog: z5732; Belongs to the class-II aminoacyl-tRNA synthetase family. (514 aa)
yjbNHypothetical protein yjbN; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs; Belongs to the Dus family. DusA subfamily. (331 aa)
trmAtRNA (Uracil-5-)-methyltransferase; Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA). (366 aa)
yihZD-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. (145 aa)
rnpARibonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. (119 aa)
spoUtRNA (Guanosine-2'-O-)-methyltransferase; Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. (229 aa)
rphRibonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. (246 aa)
yibKHypothetical tRNA/rRNA methyltransferase yibK; Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide. (157 aa)
selAL-seryl-tRNA(Sec) selenium transferase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis; Belongs to the SelA family. (463 aa)
glyQGlycyl-tRNA synthetase alpha chain; Escherichia coli K-12 ortholog: b3560; Escherichia coli O157:H7 ortholog: z4984. (303 aa)
glySGlycyl-tRNA synthetase beta chain; Escherichia coli K-12 ortholog: b3559; Escherichia coli O157:H7 ortholog: z4983. (689 aa)
trpSTryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (334 aa)
fmtMethionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. (315 aa)
yhdGHypothetical protein yhdG; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family. DusB subfamily. (321 aa)
truBtRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily. (314 aa)
ccatRNA nucleotidyltransferase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases. (412 aa)
yggHHypothetical methyltransferase yggH; Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family. (239 aa)
lysSLysyl-tRNA synthetase; Escherichia coli K-12 ortholog: b2890; Escherichia coli O157:H7 ortholog: z4228; Belongs to the class-II aminoacyl-tRNA synthetase family. (505 aa)
yqcBHypothetical protein yqcB; Responsible for synthesis of pseudouridine from uracil-65 in transfer RNAs; Belongs to the pseudouridine synthase RluA family. (260 aa)
ygbOProtein ygbO; Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs; Belongs to the pseudouridine synthase TruD family. (349 aa)
argSArginyl-tRNA synthetase; Escherichia coli K-12 ortholog: b1876; Escherichia coli O157:H7 ortholog: z2929. (577 aa)
aspSAspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (590 aa)
yeaKHypothetical protein yeaK; Escherichia coli K-12 ortholog: b1787; Escherichia coli O157:H7 ortholog: z2827. (167 aa)
thrSThreonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). (642 aa)
pheSPhenylalanyl-tRNA synthetase alpha chain; Escherichia coli K-12 ortholog: b1714; Escherichia coli O157:H7 ortholog: z2743; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (331 aa)
tyrSTyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. (428 aa)
hemAGlutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (484 aa)
pthPeptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family. (194 aa)
asnSAsparaginyl-tRNA synthetase; Escherichia coli K-12 ortholog: b0930; Escherichia coli O157:H7 ortholog: z1278. (466 aa)
smtAProtein smtA; Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in tRNAs; Belongs to the class I-like SAM-binding methyltransferase superfamily. CmoM family. (265 aa)
serSSeryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). (430 aa)
glnSGlutaminyl-tRNA synthetase; Escherichia coli K-12 ortholog: b0680; Escherichia coli O157:H7 ortholog: z0827. (554 aa)
leuSLeucyl-tRNA synthetase; Escherichia coli K-12 ortholog: b0642; Escherichia coli O157:H7 ortholog: z0789; Belongs to the class-I aminoacyl-tRNA synthetase family. (907 aa)
cysSCysteinyl-tRNA synthetase; Escherichia coli K-12 ortholog: b0526; Escherichia coli O157:H7 ortholog: z0681; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa)
ybbBHypothetical protein ybbB; Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2- selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiouridine (geS2U) and subsequent selenation of the latter derivative to 2-selenouridine (Se2U) in the tRNA chain. (319 aa)
ybaKProtein ybaK; Escherichia coli K-12 ortholog: b0481; Escherichia coli O157:H7 ortholog: z0600; Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily. (159 aa)
yajKThiamine biosynthesis protein thiI; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. (482 aa)
tgtQueuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form th [...] (375 aa)
queAS-adenosylmethionine:tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). (356 aa)
proSProlyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] (590 aa)
yadBHypothetical protein yadB; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. (308 aa)
yabORibosomal large subunit pseudouridine synthase A; Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32 in the anticodon stem and loop of transfer RNAs. (219 aa)
ileSIsoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. (938 aa)
trmDtRNA (Guanine-N(1)-)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. (255 aa)
yfiPHypothetical protein yfiP; Escherichia coli K-12 ortholog: b2583; Escherichia coli O157:H7 ortholog: z3868. (249 aa)
yfgBHypothetical protein yfgB; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. (384 aa)
hisSHistidyl-tRNA synthetase; Escherichia coli K-12 ortholog: b2514; Escherichia coli O157:H7 ortholog: z3777. (424 aa)
gltXGlutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). (471 aa)
yfcKHypothetical protein yfcK; Catalyzes the last two steps in the biosynthesis of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34; In the N-terminal section; belongs to the methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family. (688 aa)
truAtRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. (270 aa)
yohIHypothetical protein yohI; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U16 in tRNAs. Belongs to the Dus family. DusC subfamily. (338 aa)
metGMethionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (680 aa)
Your Current Organism:
Escherichia coli CFT073
NCBI taxonomy Id: 199310
Other names: E. coli CFT073, Escherichia coli str. CFT073, Escherichia coli strain CFT073
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