ID B1XUU7_POLNS Unreviewed; 176 AA.
AC B1XUU7;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 OrderedLocusNames=Pnec_0926 {ECO:0000313|EMBL:ACB44124.1};
OS Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=452638 {ECO:0000313|EMBL:ACB44124.1};
RN [1] {ECO:0000313|EMBL:ACB44124.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STIR1 {ECO:0000313|EMBL:ACB44124.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Hahn M., Richardson P.;
RT "Complete sequence of Polynucleobacter necessarius STIR1.";
RL Submitted (MAR-2008) 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|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; CP001010; ACB44124.1; -; Genomic_DNA.
DR AlphaFoldDB; B1XUU7; -.
DR STRING; 452638.Pnec_0926; -.
DR KEGG; pne:Pnec_0926; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_23_2_4; -.
DR OrthoDB; 9796919at2; -.
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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR043690; RimI.
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};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000313|EMBL:ACB44124.1}.
FT DOMAIN 13..173
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT ACT_SITE 138
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 131
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
SQ SEQUENCE 176 AA; 19705 MW; E83BBC4EA038551F CRC64;
MSNIKPAEGA AEPSFLPMQM TDLEDVLKIE SISHLHPWTR GNFSDSLAAG HWAYCVRPQA
EQILKGSYLD PAALWAYCIL FPAVDELHLL NITVSPHLCK LGLGQRMMAA IEGVAFQQKM
PRIILEVRPT NTAALALYQK LDYEQIGVRK NYYPVNPETG WREDALVLAK SIKLEA
//
