ID A0A373VJ63_9FIRM Unreviewed; 144 AA.
AC A0A373VJ63;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=[Ribosomal protein bS18]-alanine N-acetyltransferase {ECO:0000256|RuleBase:RU363094};
DE EC=2.3.1.266 {ECO:0000256|RuleBase:RU363094};
GN Name=rimI {ECO:0000313|EMBL:RGG59840.1};
GN ORFNames=DWX28_14475 {ECO:0000313|EMBL:RGG59840.1};
OS Blautia sp. AF19-10LB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=2292961 {ECO:0000313|EMBL:RGG59840.1, ECO:0000313|Proteomes:UP000262342};
RN [1] {ECO:0000313|EMBL:RGG59840.1, ECO:0000313|Proteomes:UP000262342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF19-10LB {ECO:0000313|EMBL:RGG59840.1,
RC ECO:0000313|Proteomes:UP000262342};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RGG59840.1}.
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DR EMBL; QTWS01000028; RGG59840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A373VJ63; -.
DR Proteomes; UP000262342; 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 Transferase {ECO:0000313|EMBL:RGG59840.1}.
FT DOMAIN 1..144
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 144 AA; 16705 MW; 9C9D49A04A2249AF CRC64;
MTFREMLIED LDQVMEIETD LFAIPWTKEG MFTFLTREDT MFFVVEEKGR ILGYCSMQTV
LDEGDILNVA VRSDRQKEGI GYFLVDSMLM LAQAQGISLV HLEVRESNGT ARRLYQRLGF
VEDGLRKNYY TDPLENAVLM TKKQ
//
