ID K1LZP4_9LACT Unreviewed; 148 AA.
AC K1LZP4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=HMPREF9707_01114 {ECO:0000313|EMBL:EKB55563.1};
OS Falseniella ignava CCUG 37419.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Falseniella.
OX NCBI_TaxID=883112 {ECO:0000313|EMBL:EKB55563.1, ECO:0000313|Proteomes:UP000005147};
RN [1] {ECO:0000313|EMBL:EKB55563.1, ECO:0000313|Proteomes:UP000005147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 37419 {ECO:0000313|EMBL:EKB55563.1,
RC ECO:0000313|Proteomes:UP000005147};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Facklamia ignava CCUG 37419.";
RL Submitted (JUL-2012) 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:EKB55563.1}.
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DR EMBL; AGZE01000029; EKB55563.1; -; Genomic_DNA.
DR RefSeq; WP_006701760.1; NZ_JH932301.1.
DR AlphaFoldDB; K1LZP4; -.
DR STRING; 883112.HMPREF9707_01114; -.
DR PATRIC; fig|883112.3.peg.1110; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_23_2_9; -.
DR Proteomes; UP000005147; 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 Cytoplasm {ECO:0000256|RuleBase:RU363094};
KW Reference proteome {ECO:0000313|Proteomes:UP000005147};
KW Transferase {ECO:0000313|EMBL:EKB55563.1}.
FT DOMAIN 4..138
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 148 AA; 17350 MW; 8A2E62C07C528DF0 CRC64;
MQRLTGKQLT PAQKELIIES FSEFNDTLAT FRTERDNPYT VYFIEEGIGY VAGVELAREL
EILRCYISPA YRGQGYGYQL LRCILEQTTL ERCFLEVRAS NQRARSLYER VGFVTLGVRR
NYYKNPNEDA IMMEWSEANF DNETNFSH
//
