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Escherichia coli K-12 substr. MG1655 Enzyme: ribosomal-protein-L12-serine acetyltransferase



Gene: rimL Accession Numbers: EG10853 (EcoCyc), b1427, ECK1420

Regulation Summary Diagram: ?

Summary:
RimL is the acetyl transferase that acetylates the Nα-terminal serine residue of ribosomal protein L12, converting it into its modified form, L7 [Isono81, Tanaka89a, Miao07]. Acetylation of L12 does not appear to be essential for its function [Isono81].

RimL can also acetylate a mutant ribosomal protein L12 which contains alanine instead of serine at the N-terminal position (after cleavage of the leading methionine); substitution of the adjacent amino acid with aspartate leads to lower catalytic efficiency [Miao07].

A rimL mutant lacks ribosomal protein L7, the acetylated form of ribosomal protein L12 [Isono81].

RimL shows similarity to RimJ [Tanaka89a].

Locations: cytosol

Map Position: [1,496,962 -> 1,497,501] (32.26 centisomes)
Length: 540 bp / 179 aa

Molecular Weight of Polypeptide: 20.681 kD (from nucleotide sequence), 20.3 kD (experimental) [Tanaka89a ]

Unification Links: ASAP:ABE-0004763 , CGSC:275 , EchoBASE:EB0846 , EcoGene:EG10853 , EcoliWiki:b1427 , ModBase:P13857 , OU-Microarray:b1427 , PortEco:rimL , PR:PRO_000023761 , Protein Model Portal:P13857 , RefSeq:NP_415944 , RegulonDB:EG10853 , SMR:P13857 , String:511145.b1427 , Swiss-Model:P13857 , UniProt:P13857

Relationship Links: EcoO157Cyc:Homolog:Z2291 , EcoO157Cyc:Homolog:Z2291-MONOMER , InterPro:IN-FAMILY:IPR000182 , InterPro:IN-FAMILY:IPR016181 , Pfam:IN-FAMILY:PF00583 , Prosite:IN-FAMILY:PS51186

In Paralogous Gene Group: 248 (2 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006464 - cellular protein modification process Inferred from experiment [Miao07]
GO:0006474 - N-terminal protein amino acid acetylation Inferred from experiment [Miao07]
GO:0017198 - N-terminal peptidyl-serine acetylation Inferred from experiment [Isono81]
Molecular Function: GO:0004596 - peptide alpha-N-acetyltransferase activity Inferred from experiment [Miao07]
GO:0008080 - N-acetyltransferase activity Inferred from experiment Inferred by computational analysis [GOA01, Miao07]
GO:0008999 - ribosomal-protein-alanine N-acetyltransferase activity Inferred from experiment [Miao07]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016746 - transferase activity, transferring acyl groups Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Miao07]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer protein related posttranslational modification

Essentiality data for rimL knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Credits:
Last-Curated ? 23-Apr-2007 by Keseler I , SRI International


Enzymatic reaction of: ribosomal-protein-L12-serine acetyltransferase

EC Number: 2.3.1.-

50S ribosomal subunit protein L12 + acetyl-CoA <=> 50S ribosomal subunit protein L7 + coenzyme A

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Kinetic Parameters:

Substrate
Km (μM)
Citations
50S ribosomal subunit protein L12
0.55
[Miao07]


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 11 -> 172
[UniProt09]
UniProt: N-acetyltransferase;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1427 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10853; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Isono81: Isono S, Isono K (1981). "Ribosomal protein modification in Escherichia coli. III. Studies of mutants lacking an acetylase activity specific for protein L12." Mol Gen Genet 183(3);473-7. PMID: 7038378

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Miao07: Miao L, Fang H, Li Y, Chen H (2007). "Studies of the in vitro N(alpha)-acetyltransferase activities of E. coli RimL protein." Biochem Biophys Res Commun 357(3):641-7. PMID: 17445774

Tanaka89a: Tanaka S, Matsushita Y, Yoshikawa A, Isono K (1989). "Cloning and molecular characterization of the gene rimL which encodes an enzyme acetylating ribosomal protein L12 of Escherichia coli K12." Mol Gen Genet 217(2-3);289-93. PMID: 2671655

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, BIOCYC14B.