ID C5NY18_9BACL Unreviewed; 150 AA.
AC C5NY18;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:EER67685.1};
GN ORFNames=GEMHA0001_0353 {ECO:0000313|EMBL:EER67685.1};
OS Gemella haemolysans ATCC 10379.
OC Bacteria; Bacillota; Bacilli; Bacillales; Gemellaceae; Gemella.
OX NCBI_TaxID=546270 {ECO:0000313|EMBL:EER67685.1, ECO:0000313|Proteomes:UP000006004};
RN [1] {ECO:0000313|EMBL:EER67685.1, ECO:0000313|Proteomes:UP000006004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER67685.1,
RC ECO:0000313|Proteomes:UP000006004};
RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EER67685.1, ECO:0000313|Proteomes:UP000006004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER67685.1,
RC ECO:0000313|Proteomes:UP000006004};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (JUN-2009) 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:EER67685.1}.
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DR EMBL; ACDZ02000014; EER67685.1; -; Genomic_DNA.
DR RefSeq; WP_003145020.1; NZ_ACDZ02000014.1.
DR AlphaFoldDB; C5NY18; -.
DR GeneID; 78010535; -.
DR eggNOG; COG0456; Bacteria.
DR OrthoDB; 9794566at2; -.
DR Proteomes; UP000006004; 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; PTHR43420; ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43420:SF44; AMINOGLYCOSIDE N(6')-ACETYLTRANSFERASE TYPE 1; 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 Acyltransferase {ECO:0000313|EMBL:EER67685.1};
KW Cytoplasm {ECO:0000256|RuleBase:RU363094};
KW Transferase {ECO:0000313|EMBL:EER67685.1}.
FT DOMAIN 2..146
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 150 AA; 17457 MW; 77F2071353A13861 CRC64;
MIKVNKVDVN DLDVLSRIDI DNFEDAWTKE MFKSELEHAN AEYYGLFNDD EIIGFCGGWL
VADEYQVNKI VIDKPHQNKK LGQIFFTYVM QLLKLKGVKK AIVEVRVSNM PAITVYEKAG
FSTIDIRKNY YKNNGENAYV MIRDFSNERI
//
