RIMI_SALTY
ID RIMI_SALTY Reviewed; 148 AA.
AC Q8ZJW4;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
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:18596200};
GN Name=rimI {ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000303|PubMed:18596200};
GN OrderedLocusNames=STM4558 {ECO:0000312|EMBL:AAL23373.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2] {ECO:0007744|PDB:2CNM, ECO:0007744|PDB:2CNS, ECO:0007744|PDB:2CNT}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEXES WITH COA; ACETYL-COA
RP AND BISUBSTRATE INHIBITOR, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18596200; DOI=10.1110/ps.035899.108;
RA Vetting M.W., Bareich D.C., Yu M., Blanchard J.S.;
RT "Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT
RT responsible for N(alpha)-acetylation of ribosomal protein S18.";
RL Protein Sci. 17:1781-1790(2008).
CC -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein S18.
CC {ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000269|PubMed:18596200}.
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:18596200};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02210,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimI subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000305}.
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DR EMBL; AE006468; AAL23373.1; -; Genomic_DNA.
DR RefSeq; NP_463414.1; NC_003197.2.
DR RefSeq; WP_001092436.1; NC_003197.2.
DR PDB; 2CNM; X-ray; 2.60 A; A/B/C=1-148.
DR PDB; 2CNS; X-ray; 2.50 A; A/B/C=1-148.
DR PDB; 2CNT; X-ray; 2.40 A; A/B/C/D=1-148.
DR PDBsum; 2CNM; -.
DR PDBsum; 2CNS; -.
DR PDBsum; 2CNT; -.
DR AlphaFoldDB; Q8ZJW4; -.
DR SMR; Q8ZJW4; -.
DR STRING; 99287.STM4558; -.
DR PaxDb; Q8ZJW4; -.
DR EnsemblBacteria; AAL23373; AAL23373; STM4558.
DR GeneID; 1256084; -.
DR KEGG; stm:STM4558; -.
DR PATRIC; fig|99287.12.peg.4799; -.
DR HOGENOM; CLU_013985_23_2_6; -.
DR OMA; GERYLNY; -.
DR PhylomeDB; Q8ZJW4; -.
DR BioCyc; SENT99287:STM4558-MON; -.
DR BRENDA; 2.3.1.266; 5542.
DR EvolutionaryTrace; Q8ZJW4; -.
DR Proteomes; UP000001014; 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:0008999; F:ribosomal protein S5-alanine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0017189; P:N-terminal peptidyl-alanine acetylation; IBA:GO_Central.
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 3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..148
FT /note="[Ribosomal protein S18]-alanine N-acetyltransferase"
FT /id="PRO_0000446679"
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 ECO:0000305|PubMed:18596200"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210,
FT ECO:0000305|PubMed:18596200"
FT BINDING 69..71
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210,
FT ECO:0000269|PubMed:18596200"
FT BINDING 77..82
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210,
FT ECO:0000269|PubMed:18596200"
FT BINDING 108
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02210,
FT ECO:0000269|PubMed:18596200"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2CNT"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2CNT"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:2CNT"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:2CNT"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2CNT"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:2CNT"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:2CNT"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2CNT"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2CNT"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:2CNT"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:2CNT"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:2CNT"
FT STRAND 121..132
FT /evidence="ECO:0007829|PDB:2CNT"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:2CNT"
SQ SEQUENCE 148 AA; 16687 MW; 7B5A9EE217EC520A CRC64;
MNTISILSTT DLPAAWQIEQ RAHAFPWSEK TFFGNQGERY LNLKLTADDR MAAFAITQVV
LDEATLFNIA VDPDFQRRGL GRMLLEHLID ELETRGVVTL WLEVRASNAA AIALYESLGF
NEATIRRNYY PTAQGHEDAI IMALPISM
