RIMI_ECOLI
ID RIMI_ECOLI Reviewed; 148 AA.
AC P0A944; P09453; Q2M5U5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=[Ribosomal protein S18]-alanine N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000305};
DE EC=2.3.1.266 {ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000269|PubMed:2828880};
DE AltName: Full=KAT {ECO:0000303|PubMed:30352934};
DE AltName: Full=Peptidyl-lysine N-acetyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:30352934};
GN Name=rimI {ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000303|PubMed:6991870};
GN OrderedLocusNames=b4373, JW4335;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=2828880; DOI=10.1007/bf00331153;
RA Yoshikawa A., Isono S., Sheback A., Isono K.;
RT "Cloning and nucleotide sequencing of the genes rimI and rimJ which encode
RT enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli
RT K12.";
RL Mol. Gen. Genet. 209:481-488(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP C-TERMINUS.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8366044; DOI=10.1128/jb.175.17.5604-5610.1993;
RA Carter J.R., Franden M.A., Aebersold R.H., McHenry C.S.;
RT "Identification, isolation, and overexpression of the gene encoding the psi
RT subunit of DNA polymerase III holoenzyme.";
RL J. Bacteriol. 175:5604-5610(1993).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=6991870; DOI=10.1007/bf00272675;
RA Isono K., Isono S.;
RT "Ribosomal protein modification in Escherichia coli. II. Studies of a
RT mutant lacking the N-terminal acetylation of protein S18.";
RL Mol. Gen. Genet. 177:645-651(1980).
RN [7]
RP FUNCTION AS A LYSINE ACETYLTRANSFERASE, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF TYR-115.
RC STRAIN=K12;
RX PubMed=30352934; DOI=10.1128/mbio.01905-18;
RA Christensen D.G., Meyer J.G., Baumgartner J.T., D'Souza A.K., Nelson W.C.,
RA Payne S.H., Kuhn M.L., Schilling B., Wolfe A.J.;
RT "Identification of novel protein lysine acetyltransferases in Escherichia
RT coli.";
RL MBio 9:E01905-E01905(2018).
RN [8]
RP ERRATUM OF PUBMED:30352934.
RX PubMed=30967468; DOI=10.1128/mbio.00592-19;
RA Christensen D.G., Meyer J.G., Baumgartner J.T., D'Souza A.K., Nelson W.C.,
RA Payne S.H., Kuhn M.L., Schilling B., Wolfe A.J.;
RT "Correction for Christensen et al., 'Identification of novel protein lysine
RT acetyltransferases in Escherichia coli'.";
RL MBio 10:0-0(2019).
CC -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein S18
CC (PubMed:6991870, PubMed:2828880). Also acts as a N-epsilon-lysine
CC acetyltransferase that catalyzes acetylation of several proteins
CC (PubMed:30352934). {ECO:0000269|PubMed:2828880,
CC ECO:0000269|PubMed:30352934, ECO:0000269|PubMed:6991870}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein
CC bS18]; Xref=Rhea:RHEA:43756, Rhea:RHEA-COMP:10676, Rhea:RHEA-
CC COMP:10677, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:64718, ChEBI:CHEBI:83683; EC=2.3.1.266;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02210,
CC ECO:0000269|PubMed:2828880};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000269|PubMed:30352934};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02210,
CC ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutation of the gene impairs the acetylation of
CC the N-terminal alanine of ribosomal protein S18, but does not affect
CC acetylation of ribosomal proteins S5 and L12.
CC {ECO:0000269|PubMed:6991870}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimI subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000305}.
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DR EMBL; X06117; CAA29489.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97269.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77326.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78361.1; -; Genomic_DNA.
DR EMBL; L05387; AAA03077.1; -; Unassigned_DNA.
DR PIR; D65252; D65252.
DR RefSeq; NP_418790.1; NC_000913.3.
DR RefSeq; WP_001092461.1; NZ_SSZK01000015.1.
DR AlphaFoldDB; P0A944; -.
DR SMR; P0A944; -.
DR BioGRID; 4262786; 25.
DR BioGRID; 853171; 1.
DR DIP; DIP-48259N; -.
DR IntAct; P0A944; 1.
DR STRING; 511145.b4373; -.
DR jPOST; P0A944; -.
DR PaxDb; P0A944; -.
DR PRIDE; P0A944; -.
DR EnsemblBacteria; AAC77326; AAC77326; b4373.
DR EnsemblBacteria; BAE78361; BAE78361; BAE78361.
DR GeneID; 58459937; -.
DR GeneID; 948894; -.
DR KEGG; ecj:JW4335; -.
DR KEGG; eco:b4373; -.
DR PATRIC; fig|1411691.4.peg.2315; -.
DR EchoBASE; EB0843; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_23_2_6; -.
DR InParanoid; P0A944; -.
DR OMA; GERYLNY; -.
DR PhylomeDB; P0A944; -.
DR BioCyc; EcoCyc:EG10850-MON; -.
DR BioCyc; MetaCyc:EG10850-MON; -.
DR PRO; PR:P0A944; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0008080; F:N-acetyltransferase activity; IMP:EcoliWiki.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008999; F:ribosomal protein S5-alanine N-acetyltransferase activity; IMP:EcoliWiki.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IMP:EcoCyc.
DR GO; GO:0017189; P:N-terminal peptidyl-alanine acetylation; IMP:EcoliWiki.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IMP:EcoliWiki.
DR HAMAP; MF_02210; RimI; 1.
DR InterPro; IPR006464; AcTrfase_RimI/Ard1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR043690; RimI.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR01575; rimI; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..148
FT /note="[Ribosomal protein S18]-alanine N-acetyltransferase"
FT /id="PRO_0000074561"
FT DOMAIN 2..147
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210"
FT BINDING 69..71
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210"
FT BINDING 108
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210"
FT MUTAGEN 115
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30352934"
FT CONFLICT 143..148
FT /note="ALPISM -> RCQSVCNTRWNNEVGLDFL (in Ref. 1; CAA29489
FT and 2; AAA97269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 16610 MW; 46A8412D38D42F86 CRC64;
MNTISSLETT DLPAAYHIEQ RAHAFPWSEK TFASNQGERY LNFQLTQNGK MAAFAITQVV
LDEATLFNIA VDPDYQRQGL GRALLEHLID ELEKRGVATL WLEVRASNAA AIALYESLGF
NEATIRRNYY PTTDGREDAI IMALPISM
