RIMI_BACSU
ID RIMI_BACSU Reviewed; 151 AA.
AC O05517; Q797D4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Putative [ribosomal protein S18]-alanine N-acetyltransferase {ECO:0000250|UniProtKB:P0A944};
DE EC=2.3.1.266 {ECO:0000250|UniProtKB:P0A944};
DE AltName: Full=Acetylating enzyme for N-terminal of ribosomal protein S18;
GN Name=rimI; Synonyms=ydiD; OrderedLocusNames=BSU05930;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein S18.
CC {ECO:0000250|UniProtKB:P0A944}.
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:0000250|UniProtKB:P0A944};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A944}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimI subfamily.
CC {ECO:0000305}.
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DR EMBL; D88802; BAA19717.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12412.1; -; Genomic_DNA.
DR PIR; E69786; E69786.
DR RefSeq; NP_388474.1; NC_000964.3.
DR RefSeq; WP_003243019.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O05517; -.
DR SMR; O05517; -.
DR STRING; 224308.BSU05930; -.
DR PaxDb; O05517; -.
DR PRIDE; O05517; -.
DR DNASU; 937997; -.
DR EnsemblBacteria; CAB12412; CAB12412; BSU_05930.
DR GeneID; 937997; -.
DR KEGG; bsu:BSU05930; -.
DR PATRIC; fig|224308.179.peg.638; -.
DR eggNOG; COG0456; Bacteria.
DR InParanoid; O05517; -.
DR OMA; GERYLNY; -.
DR PhylomeDB; O05517; -.
DR BioCyc; BSUB:BSU05930-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IEA:InterPro.
DR InterPro; IPR006464; AcTrfase_RimI/Ard1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
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..151
FT /note="Putative [ribosomal protein S18]-alanine N-
FT acetyltransferase"
FT /id="PRO_0000360195"
FT DOMAIN 5..150
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8ZJW4"
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8ZJW4"
FT BINDING 74..76
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8ZJW4"
FT BINDING 113
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q8ZJW4"
SQ SEQUENCE 151 AA; 17377 MW; CABC7C1DE0ECA16F CRC64;
MKTKAAVRNM RLEDIDHVYE IEASSFTSPW TKDSFYHELL ENPYAHYLVI EKDGHLAGYC
GIWIVMDDAQ ITNIAIKPEY RGQSLGETLF RSAVELCKEK DARRLSLEVR VSNHPAQGLY
KKFGMQPGGI RKNYYTDNGE DALIMWVTIN E
