ID E3HS29_ACHXA Unreviewed; 417 AA.
AC E3HS29;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 ECO:0000313|EMBL:ADP14821.1};
GN OrderedLocusNames=AXYL_01483 {ECO:0000313|EMBL:ADP14821.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP14821.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP14821.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP14821.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
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; CP002287; ADP14821.1; -; Genomic_DNA.
DR RefSeq; WP_013392163.1; NC_014640.1.
DR AlphaFoldDB; E3HS29; -.
DR STRING; 762376.AXYL_01483; -.
DR KEGG; axy:AXYL_01483; -.
DR PATRIC; fig|762376.5.peg.1480; -.
DR eggNOG; COG0456; Bacteria.
DR eggNOG; COG1214; Bacteria.
DR HOGENOM; CLU_052459_0_0_4; -.
DR OrthoDB; 9796919at2; -.
DR Proteomes; UP000006876; 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 ECO:0000313|EMBL:ADP14821.1}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02210};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000313|EMBL:ADP14821.1}.
FT DOMAIN 265..411
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT ACT_SITE 366
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT ACT_SITE 378
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 332..334
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 371
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
SQ SEQUENCE 417 AA; 44551 MW; BEA721B289C870AF CRC64;
MELNLLALET SSSRCGVALL RAVDGRLEVS VREHEGSQEH AERLLPMANE LLAESGLAPA
ALHAVAFGQG PGGFTGLRVA CGVAQGMGLG LGIPVLPIVS HQAVAAQVEA TPADAIVVAL
DARMNEVYLA VYRQAGVADG EISWEVLQAP LLIAAAEVVP WTAHHLPAWS AAAGQPLELL
LAGDAWDAYA SDMEHPAEWR RADSARRPEA ASVARLARQG WMRGEAVAPE LAAPLYVRDK
VAFTTAERMR GEGGNPKAQP SLAPWVPQPM TDADLDEVVA LEAHVQAFPW TRGNFADALA
AGYGAWVLRR EGKLAGFCVL MFAPDVAHLL VIAVAKPLHR QGLGGVLLGW CEQQARERGM
EGVLLEVRPS NESAINFYKR HGYLQIGVRR GYYPAEKGGR EDALVMQKRF ATDGAAA
//
