ID D0L131_HALNC Unreviewed; 164 AA.
AC D0L131;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=Hneap_1574 {ECO:0000313|EMBL:ACX96404.1};
OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS neapolitanus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Halothiobacillaceae; Halothiobacillus.
OX NCBI_TaxID=555778 {ECO:0000313|EMBL:ACX96404.1, ECO:0000313|Proteomes:UP000009102};
RN [1] {ECO:0000313|EMBL:ACX96404.1, ECO:0000313|Proteomes:UP000009102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2 {ECO:0000313|Proteomes:UP000009102};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Kerfeld C., Cannon G., Heinhort S.;
RT "Complete sequence of Halothiobacillus neapolitanus c2.";
RL Submitted (OCT-2009) 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; CP001801; ACX96404.1; -; Genomic_DNA.
DR RefSeq; WP_012824438.1; NC_013422.1.
DR AlphaFoldDB; D0L131; -.
DR STRING; 555778.Hneap_1574; -.
DR KEGG; hna:Hneap_1574; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_23_2_6; -.
DR OrthoDB; 9796919at2; -.
DR Proteomes; UP000009102; 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; PTHR43420; ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43420:SF12; N-ACETYLTRANSFERASE DOMAIN-CONTAINING PROTEIN; 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 ECO:0000313|EMBL:ACX96404.1}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02210};
KW Reference proteome {ECO:0000313|Proteomes:UP000009102};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000313|EMBL:ACX96404.1}.
FT DOMAIN 19..164
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT ACT_SITE 120
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT ACT_SITE 132
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 94..99
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 125
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
SQ SEQUENCE 164 AA; 18684 MW; 2810167035DB58B0 CRC64;
MNAQTDQSPA VSPVHPPIAH ILSLDEEDLP AVQRIEQAAH IFPWSERVFK DCIRSGYYLD
GAYDGAKLLG FSVVMPILNE WHLLNLCVDP KRQRRGIGRL LLEYMIEQAR KAEVSSLWLE
VREENAAARQ LYAAYGFKQV GLRKAYYPAK DGREDALVLM RTLD
//
