ID A0A2Z6GFD0_9PROT Unreviewed; 144 AA.
AC A0A2Z6GFD0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=[Ribosomal protein bS18]-alanine N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000256|RuleBase:RU363094};
DE EC=2.3.1.266 {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000256|RuleBase:RU363094};
GN Name=rimI {ECO:0000256|HAMAP-Rule:MF_02210};
GN ORFNames=OYT1_ch2693 {ECO:0000313|EMBL:BBE52200.1};
OS Ferriphaselus amnicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Ferriphaselus.
OX NCBI_TaxID=1188319 {ECO:0000313|EMBL:BBE52200.1, ECO:0000313|Proteomes:UP000033070};
RN [1] {ECO:0000313|EMBL:BBE52200.1, ECO:0000313|Proteomes:UP000033070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OYT1 {ECO:0000313|EMBL:BBE52200.1,
RC ECO:0000313|Proteomes:UP000033070};
RA Kato S., Itoh T., Ohkuma M.;
RT "OYT1 Genome Sequencing.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein bS18.
CC {ECO:0000256|HAMAP-Rule:MF_02210, 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|HAMAP-Rule:MF_02210,
CC ECO:0000256|RuleBase:RU363094};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02210,
CC ECO:0000256|RuleBase:RU363094}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimI subfamily.
CC {ECO:0000256|ARBA:ARBA00005395, ECO:0000256|HAMAP-Rule:MF_02210,
CC ECO:0000256|RuleBase:RU363094}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02210}.
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DR EMBL; AP018738; BBE52200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6GFD0; -.
DR STRING; 1188319.OYT1_02231; -.
DR KEGG; fam:OYT1_ch2693; -.
DR Proteomes; UP000033070; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008999; F:peptide-alanine-alpha-N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR HAMAP; MF_02210; RimI; 1.
DR InterPro; IPR006464; AcTrfase_RimI/Ard1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR043690; RimI.
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 Acyltransferase {ECO:0000256|HAMAP-Rule:MF_02210};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000256|RuleBase:RU363094};
KW Reference proteome {ECO:0000313|Proteomes:UP000033070};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000313|EMBL:BBE52200.1}.
FT DOMAIN 1..144
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT ACT_SITE 113
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 67..69
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 106
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
SQ SEQUENCE 144 AA; 15803 MW; F620B74F5D2DE6A3 CRC64;
MIRAMTLADV DAVLAIEQAV HAHPWTRGNF ADALASGYSG WVDELDGVLR GYAVLMLGVG
EAELLTIGVA TSSQRLGLAT HLMQWLESQA QSYNFERLCL EVRPSNTAGL ALYCKTGFIE
IGRRRGYYPA ANGREDAILM EKRL
//
