RIMI_HAEDU
ID RIMI_HAEDU Reviewed; 145 AA.
AC Q7VP85;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=HD_0212;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; AE017143; AAP95202.1; -; Genomic_DNA.
DR RefSeq; WP_010944255.1; NC_002940.2.
DR AlphaFoldDB; Q7VP85; -.
DR SMR; Q7VP85; -.
DR STRING; 233412.HD_0212; -.
DR EnsemblBacteria; AAP95202; AAP95202; HD_0212.
DR GeneID; 60733329; -.
DR KEGG; hdu:HD_0212; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_23_2_6; -.
DR OMA; ATLMDIC; -.
DR Proteomes; UP000001022; 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; Reference proteome; Transferase.
FT CHAIN 1..145
FT /note="[Ribosomal protein S18]-alanine N-acetyltransferase"
FT /id="PRO_0000074564"
FT DOMAIN 1..145
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210"
FT ACT_SITE 113
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210"
FT BINDING 67..69
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210"
FT BINDING 106
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210"
SQ SEQUENCE 145 AA; 16489 MW; 36CA2591D8691A76 CRC64;
MIETIVEQDF NRLFEIEQAA HLVPWSKGTL LNNQGAKYLN LKYTEQDNII AFAICQTLLD
EATLFNLAVD PAFQAQGYAK KLLTALINQL QARGISTLWL EVRQSNTIAQ KLYDSVGFNQ
ITIRKNYYPM PDGSRENAVI MALYL
