RIML_ECOLI
ID RIML_ECOLI Reviewed; 179 AA.
AC P13857;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ribosomal-protein-serine acetyltransferase;
DE EC=2.3.1.-;
DE AltName: Full=Acetylating enzyme for N-terminal of ribosomal protein L7/L12;
GN Name=rimL; OrderedLocusNames=b1427, JW1423;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MB2052;
RX PubMed=2671655; DOI=10.1007/bf02464895;
RA Tanaka S., Matsushita Y., Yoshikawa A., Isono K.;
RT "Cloning and molecular characterization of the gene rimL which encodes an
RT enzyme acetylating ribosomal protein L12 of Escherichia coli K12.";
RL Mol. Gen. Genet. 217:289-293(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
CC -!- FUNCTION: This enzyme acetylates the N-terminal serine of ribosomal
CC protein L7/L12.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[ribosomal protein bL12] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[ribosomal protein bL12];
CC Xref=Rhea:RHEA:43760, Rhea:RHEA-COMP:10681, Rhea:RHEA-COMP:10682,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:64738, ChEBI:CHEBI:83690;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimL subfamily.
CC {ECO:0000305}.
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DR EMBL; X15860; CAA33869.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74509.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15048.1; -; Genomic_DNA.
DR PIR; S04776; XXECPL.
DR RefSeq; NP_415944.1; NC_000913.3.
DR RefSeq; WP_000140873.1; NZ_SSZK01000021.1.
DR AlphaFoldDB; P13857; -.
DR SMR; P13857; -.
DR BioGRID; 4260179; 50.
DR IntAct; P13857; 2.
DR STRING; 511145.b1427; -.
DR SWISS-2DPAGE; P13857; -.
DR jPOST; P13857; -.
DR PaxDb; P13857; -.
DR PRIDE; P13857; -.
DR EnsemblBacteria; AAC74509; AAC74509; b1427.
DR EnsemblBacteria; BAA15048; BAA15048; BAA15048.
DR GeneID; 945998; -.
DR KEGG; ecj:JW1423; -.
DR KEGG; eco:b1427; -.
DR PATRIC; fig|1411691.4.peg.844; -.
DR EchoBASE; EB0846; -.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_013985_3_0_6; -.
DR InParanoid; P13857; -.
DR OMA; SQWLAWP; -.
DR PhylomeDB; P13857; -.
DR BioCyc; EcoCyc:EG10853-MON; -.
DR PRO; PR:P13857; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:EcoliWiki.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008999; F:ribosomal protein S5-alanine N-acetyltransferase activity; IDA:EcoliWiki.
DR GO; GO:0017198; P:N-terminal peptidyl-serine acetylation; IMP:EcoCyc.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:EcoliWiki.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..179
FT /note="Ribosomal-protein-serine acetyltransferase"
FT /id="PRO_0000074570"
FT DOMAIN 11..172
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 179 AA; 20681 MW; 9946F97C2A20CB1D CRC64;
MTETIKVSES LELHAVAENH VKPLYQLICK NKTWLQQSLN WPQFVQSEED TRKTVQGNVM
LHQRGYAKMF MIFKEDELIG VISFNRIEPL NKTAEIGYWL DESHQGQGII SQALQALIHH
YAQSGELRRF VIKCRVDNPQ SNQVALRNGF ILEGCLKQAE FLNDAYDDVN LYARIIDSQ
