ID   RIMI_ECO57              Reviewed;         148 AA.
AC   P0A946; P09453;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=Z5974, ECs5331;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
RC   STRAIN=O157:H7 / EHEC;
RG   Center for Structural Genomics of Infectious Diseases (CSGID);
RA   Filippova E.V., Minasov G., Kiryukhina O., Shuvalova L., Grimshaw S.,
RA   Wolfe A.J., Anderson W.F.;
RT   "Crystal structure of the ribosomal-protein-S18-alanine N-acetyltransferase
RT   from Escherichia coli.";
RL   Submitted (MAR-2016) to the PDB data bank.
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; AE005174; AAG59553.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38754.1; -; Genomic_DNA.
DR   PIR; C91295; C91295.
DR   PIR; E86136; E86136.
DR   RefSeq; NP_313358.1; NC_002695.1.
DR   RefSeq; WP_001092461.1; NZ_SWKA01000005.1.
DR   PDB; 5ISV; X-ray; 1.35 A; A/B=1-148.
DR   PDBsum; 5ISV; -.
DR   AlphaFoldDB; P0A946; -.
DR   SMR; P0A946; -.
DR   STRING; 155864.EDL933_5714; -.
DR   DNASU; 959682; -.
DR   EnsemblBacteria; AAG59553; AAG59553; Z5974.
DR   EnsemblBacteria; BAB38754; BAB38754; ECs_5331.
DR   GeneID; 58459937; -.
DR   GeneID; 913548; -.
DR   KEGG; ece:Z5974; -.
DR   KEGG; ecs:ECs_5331; -.
DR   PATRIC; fig|386585.9.peg.5575; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_013985_23_2_6; -.
DR   OMA; GERYLNY; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   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_0000074562"
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   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   HELIX           9..11
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   HELIX           12..22
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   HELIX           29..34
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   STRAND          50..60
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   STRAND          63..71
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   HELIX           80..94
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   STRAND          99..105
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   HELIX           109..117
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   STRAND          121..131
FT                   /evidence="ECO:0007829|PDB:5ISV"
FT   STRAND          133..145
FT                   /evidence="ECO:0007829|PDB:5ISV"
SQ   SEQUENCE   148 AA;  16610 MW;  46A8412D38D42F86 CRC64;
     MNTISSLETT DLPAAYHIEQ RAHAFPWSEK TFASNQGERY LNFQLTQNGK MAAFAITQVV
     LDEATLFNIA VDPDYQRQGL GRALLEHLID ELEKRGVATL WLEVRASNAA AIALYESLGF
     NEATIRRNYY PTTDGREDAI IMALPISM