RIMI_SHIFL
ID RIMI_SHIFL Reviewed; 148 AA.
AC P0A947; P09453;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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};
GN OrderedLocusNames=SF4404, S4676;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45819.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19594.1; -; Genomic_DNA.
DR RefSeq; NP_710112.1; NC_004337.2.
DR RefSeq; WP_001092461.1; NZ_WPGW01000013.1.
DR AlphaFoldDB; P0A947; -.
DR SMR; P0A947; -.
DR STRING; 198214.SF4404; -.
DR EnsemblBacteria; AAN45819; AAN45819; SF4404.
DR EnsemblBacteria; AAP19594; AAP19594; S4676.
DR GeneID; 1023573; -.
DR GeneID; 58459937; -.
DR KEGG; sfl:SF4404; -.
DR KEGG; sfx:S4676; -.
DR PATRIC; fig|198214.7.peg.5191; -.
DR HOGENOM; CLU_013985_23_2_6; -.
DR OMA; GERYLNY; -.
DR OrthoDB; 1826274at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..148
FT /note="[Ribosomal protein S18]-alanine N-acetyltransferase"
FT /id="PRO_0000074566"
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
