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rimI protein (Escherichia coli K12 DH10B) - STRING interaction network
"rimI" - Ribosomal-protein-alanine N-acetyltransferase in Escherichia coli K12 DH10B
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second shell of interactors
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some 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
protein homology
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Gene Fusion
rimIRibosomal-protein-alanine N-acetyltransferase; This enzyme acetylates the N-terminal alanine of ribosomal protein S18 (148 aa)    
Predicted Functional Partners:
DNA polymerase III subunit psi; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The exact function of the psi subunit is unknown (137 aa)
Nucleotidase; Nucleotidase that shows high phosphatase activity toward non-canonical pyrimidine nucleotides and three canonical nucleoside 5’-monophosphates (UMP, dUMP, and dTMP), and very low activity against TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6- phosphogluconate. Appears to function as a house-cleaning nucleotidase in vivo, since the general nucleotidase activity of YjjG allows it to protect cells against non-canonical pyrimidine derivatives such as 5-fluoro-2’-deoxyuridine, 5-fluorouridine, 5- fluoroorotate, 5-fluorouracil, and 5-aza-2’-deoxycytidine, and prevents the incorpor [...] (225 aa)
Peptidase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. In fact, can act as a protease that specifically degrades TsaD in vitro; therefore TsaB may post-translationally regulate cellular pools of TsaD via p [...] (231 aa)
Peptide chain release factor 3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF- 1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP (529 aa)
16S ribosomal RNA m2G1207 methyltransferase; Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle (343 aa)
ribosomal-protein-S5-alanine N-acetyltransferase; This enzyme acetylates the N-terminal alanine of ribosomal protein S5. Plays also a role in the temperature regulation of pap pilin transcription (194 aa)
Ferric uptake regulator; Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. Regulates the expression of several outer-membrane proteins including the iron transport operon (148 aa)
Hypothetical protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (515 aa)
prolyl-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 [...] (572 aa)
Fused acyl-CoA synthetase- NAD(P)-binding subunit; ATP-binding subunit; Acetylates RNase R in exponential phase cells. Also required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta’ RNAP subunits. May acetylate Acs and inhibit its activity (886 aa)
Your Current Organism:
Escherichia coli K12 DH10B
NCBI taxonomy Id: 316385
Other names: E. coli str. K-12 substr. DH10B, Escherichia coli DH10B, Escherichia coli K12 DH10B, Escherichia coli str. K-12 substr. DH10B, Escherichia coli str. K12 substr. DH10B, Escherichia coli strain K12 substrain DH10B
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