RIMI_ECOL6
ID RIMI_ECOL6 Reviewed; 148 AA.
AC P0A945; P09453;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=[Ribosomal protein S18]-alanine N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_02210};
DE EC=2.3.1.266 {ECO:0000255|HAMAP-Rule:MF_02210};
GN Name=rimI {ECO:0000255|HAMAP-Rule:MF_02210}; OrderedLocusNames=c5453;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein S18.
CC {ECO:0000255|HAMAP-Rule:MF_02210}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02210}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimI subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000305}.
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DR EMBL; AE014075; AAN83873.1; -; Genomic_DNA.
DR RefSeq; WP_001092461.1; NC_004431.1.
DR AlphaFoldDB; P0A945; -.
DR SMR; P0A945; -.
DR STRING; 199310.c5453; -.
DR EnsemblBacteria; AAN83873; AAN83873; c5453.
DR GeneID; 58459937; -.
DR KEGG; ecc:c5453; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_23_2_6; -.
DR OMA; GERYLNY; -.
DR BioCyc; ECOL199310:C5453-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008999; F:ribosomal protein S5-alanine N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017189; P:N-terminal peptidyl-alanine acetylation; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Transferase.
FT CHAIN 1..148
FT /note="[Ribosomal protein S18]-alanine N-acetyltransferase"
FT /id="PRO_0000074563"
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"
SQ SEQUENCE 148 AA; 16610 MW; 46A8412D38D42F86 CRC64;
MNTISSLETT DLPAAYHIEQ RAHAFPWSEK TFASNQGERY LNFQLTQNGK MAAFAITQVV
LDEATLFNIA VDPDYQRQGL GRALLEHLID ELEKRGVATL WLEVRASNAA AIALYESLGF
NEATIRRNYY PTTDGREDAI IMALPISM
