ID A0A0S1XVS3_9BORD Unreviewed; 442 AA.
AC A0A0S1XVS3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=[Ribosomal protein bS18]-alanine N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_02210};
DE EC=2.3.1.266 {ECO:0000256|HAMAP-Rule:MF_02210};
GN Name=rimI {ECO:0000256|HAMAP-Rule:MF_02210};
GN ORFNames=ASB57_00915 {ECO:0000313|EMBL:ALM81717.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM81717.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM81717.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM81717.1,
RC ECO:0000313|Proteomes:UP000064621};
RA Hou L.;
RT "Draft genome of Bordetella sp. N.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein bS18.
CC {ECO:0000256|HAMAP-Rule:MF_02210}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02210}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimI subfamily.
CC {ECO:0000256|ARBA:ARBA00005395, ECO:0000256|HAMAP-Rule:MF_02210}.
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; CP013111; ALM81717.1; -; Genomic_DNA.
DR RefSeq; WP_057649760.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1XVS3; -.
DR STRING; 1746199.ASB57_00915; -.
DR OrthoDB; 9796919at2; -.
DR Proteomes; UP000064621; 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 GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.30.420.40; -; 2.
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; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR043690; RimI.
DR InterPro; IPR022496; T6A_TsaB.
DR NCBIfam; TIGR01575; rimI; 1.
DR NCBIfam; TIGR03725; T6A_YeaZ; 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 Pfam; PF00814; TsaD; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000064621};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000313|EMBL:ALM81717.1}.
FT DOMAIN 288..434
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT ACT_SITE 401
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 355..357
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 394
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
SQ SEQUENCE 442 AA; 46735 MW; 6B5F73DFCED0D728 CRC64;
MNLTLLALET SSTRCGVALL HGDSKNPHVL IQEHEGAQEH AERLLPMARD LLTQAGLDVA
DLDAVAFGQG PGGFTGLRVA CGVAQGIALA RDIPVLPVVS HQAVAALVPA RPDQAVVVAL
DARMEEVYLA VYRRLDGAAD DTRWEVLQAP MLIAAAEAVP WIEAQVDGWS AQCGVPLSVV
IAGDAWDSLA AHMAPSADWP RFDATRPEAR LVARLAAQAW QRGEAVAAEL AAPLYVRDKV
AFTTAERMGG QGGNPKAAIA AASAQQLPPT PAPQLGALGA GGGTGAEAEL GPLHSDDLDE
MARIEAAVQA FPWTRGNFAD ALASAYDTCG VRRDGRLLGF CILMHAPDVS HLLVIAVEKS
LHGQGLGSHL MRWCEARTAA RGIGGLLLEV RPSNARALTF YERHGFLRIG VRRGYYPAGK
GQREDAVVMQ KRLARDDGAA ND
//
