ID   RIMI_HAEIN              Reviewed;         146 AA.
AC   P44305;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=HI_0010;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L42023; AAC21688.1; -; Genomic_DNA.
DR   RefSeq; NP_438183.1; NC_000907.1.
DR   RefSeq; WP_010868917.1; NC_000907.1.
DR   AlphaFoldDB; P44305; -.
DR   SMR; P44305; -.
DR   STRING; 71421.HI_0010; -.
DR   EnsemblBacteria; AAC21688; AAC21688; HI_0010.
DR   KEGG; hin:HI_0010; -.
DR   PATRIC; fig|71421.8.peg.10; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_013985_23_2_6; -.
DR   OMA; GERYLNY; -.
DR   PhylomeDB; P44305; -.
DR   BioCyc; HINF71421:G1GJ1-10-MON; -.
DR   Proteomes; UP000000579; 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   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..146
FT                   /note="[Ribosomal protein S18]-alanine N-acetyltransferase"
FT                   /id="PRO_0000074565"
FT   DOMAIN          2..146
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        114
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   146 AA;  16745 MW;  CA4B7DB5B9BADFD3 CRC64;
     MSIISQIEAC DFERLYEIEQ QAHLVPWSFG TLKNNQGERY LNLKLIENNQ IIGFAICQTV
     LDEATLFNIA ILPTYQGCGF GKLLLGKLIF QLKEKGVQTL WLEVRESNSA RFLYEKIGFN
     EVDIRKNYYP KPSGGRENAV VMACYL