ID D3HBD8_STRM6 Unreviewed; 145 AA.
AC D3HBD8;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=[Ribosomal protein bS18]-alanine N-acetyltransferase {ECO:0000256|RuleBase:RU363094};
DE EC=2.3.1.266 {ECO:0000256|RuleBase:RU363094};
GN OrderedLocusNames=smi_1952 {ECO:0000313|EMBL:CBJ23188.1};
OS Streptococcus mitis (strain B6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=365659 {ECO:0000313|EMBL:CBJ23188.1, ECO:0000313|Proteomes:UP000008563};
RN [1] {ECO:0000313|EMBL:CBJ23188.1, ECO:0000313|Proteomes:UP000008563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B6 {ECO:0000313|EMBL:CBJ23188.1,
RC ECO:0000313|Proteomes:UP000008563};
RX PubMed=20195536; DOI=10.1371/journal.pone.0009426;
RA Denapaite D., Brueckner R., Nuhn M., Reichmann P., Henrich B., Maurer P.,
RA Schaehle Y., Selbmann P., Zimmermann W., Wambutt R., Hakenbeck R.;
RT "The genome of Streptococcus mitis B6--what is a commensal?";
RL PLoS ONE 5:E9426-E9426(2010).
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}.
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DR EMBL; FN568063; CBJ23188.1; -; Genomic_DNA.
DR RefSeq; WP_000569814.1; NC_013853.1.
DR RefSeq; YP_003447048.1; NC_013853.1.
DR AlphaFoldDB; D3HBD8; -.
DR STRING; 365659.smi_1952; -.
DR KEGG; smb:smi_1952; -.
DR PATRIC; fig|365659.3.peg.1967; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_23_2_9; -.
DR OrthoDB; 9794566at2; -.
DR Proteomes; UP000008563; Chromosome.
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 Transferase {ECO:0000313|EMBL:CBJ23188.1}.
FT DOMAIN 2..143
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 145 AA; 16479 MW; F45EE4FA32EBE3BC CRC64;
MIEIKRIQQK PDLAQDIYAV MAAVYPVSPW TLEQIQADLS QDQTWYALAY DGTEVIGFLA
VQENIFEAEV LQIAVKGAYQ GKGIASALFA QLSTDKEIFL EVRKSNQRAQ AFYKKEKMAV
IAERKAYYHD PVEDAIIMKR EIDEG
//
