ID R9MC25_9FIRM Unreviewed; 147 AA.
AC R9MC25;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=[Ribosomal protein bS18]-alanine N-acetyltransferase {ECO:0000256|RuleBase:RU363094};
DE EC=2.3.1.266 {ECO:0000256|RuleBase:RU363094};
GN ORFNames=C818_03575 {ECO:0000313|EMBL:EOS68226.1};
OS Lachnospiraceae bacterium MD308.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235799 {ECO:0000313|EMBL:EOS68226.1, ECO:0000313|Proteomes:UP000014117};
RN [1] {ECO:0000313|EMBL:EOS68226.1, ECO:0000313|Proteomes:UP000014117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-2 {ECO:0000313|EMBL:EOS68226.1,
RC ECO:0000313|Proteomes:UP000014117};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 3-2.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein bS18.
CC {ECO:0000256|RuleBase:RU363094}.
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:0000256|RuleBase:RU363094};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU363094}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimI subfamily.
CC {ECO:0000256|RuleBase:RU363094}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOS68226.1}.
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; ASTE01000039; EOS68226.1; -; Genomic_DNA.
DR AlphaFoldDB; R9MC25; -.
DR STRING; 1235799.C818_03575; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_23_2_9; -.
DR OrthoDB; 9794566at2; -.
DR Proteomes; UP000014117; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008999; F:peptide-alanine-alpha-N-acetyltransferase activity; IEA:RHEA.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR006464; AcTrfase_RimI/Ard1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR NCBIfam; TIGR01575; rimI; 1.
DR PANTHER; PTHR43617:SF20; [RIBOSOMAL PROTEIN S18]-ALANINE N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43617; L-AMINO ACID N-ACETYLTRANSFERASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU363094};
KW Reference proteome {ECO:0000313|Proteomes:UP000014117};
KW Transferase {ECO:0000313|EMBL:EOS68226.1}.
FT DOMAIN 2..146
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 147 AA; 16816 MW; 00B86264A38194DC CRC64;
MLLIKKIETE DVERISQLEK EGFSDPWSVA GIRESLEQTY TILLGAWLSE TLVGYVICYC
VSDEAEIARI AVGRSFRRQG VATMLLEELK DICLKRQSEK ILLDVRKSNE AAAGFYEKCG
FTRDGIRKNY YREPTEDAVL MSFQFGK
//
