ID A0A2A7MC22_9CLOT Unreviewed; 145 AA.
AC A0A2A7MC22;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=[Ribosomal protein bS18]-alanine N-acetyltransferase {ECO:0000256|RuleBase:RU363094};
DE EC=2.3.1.266 {ECO:0000256|RuleBase:RU363094};
GN Name=rimI {ECO:0000313|EMBL:PEG29314.1};
GN Synonyms=rimI_1 {ECO:0000313|EMBL:VCT83025.1};
GN ORFNames=CNEO_45172 {ECO:0000313|EMBL:CAG9711255.1},
GN CNEONATNEC25_00618 {ECO:0000313|EMBL:VCT83025.1}, CQ394_18270
GN {ECO:0000313|EMBL:PEG29314.1};
OS Clostridium neonatale.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=137838 {ECO:0000313|EMBL:PEG29314.1, ECO:0000313|Proteomes:UP000220840};
RN [1] {ECO:0000313|EMBL:PEG29314.1, ECO:0000313|Proteomes:UP000220840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC99A005 {ECO:0000313|EMBL:PEG29314.1,
RC ECO:0000313|Proteomes:UP000220840};
RA Bernard K., Burdz T., Wiebe D., Balcewich B., Alfa M., Bernier A.-M.;
RT "Effective Description of Clostridium neonatale sp. nov. linked to
RT necrotizing enterocolitis in neonates and a clarification of species
RT assignable to the genus Clostridium (Prazmowski 1880) emend. Lawson and
RT Rainey 2016.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VCT83025.1, ECO:0000313|Proteomes:UP000431451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEC25 {ECO:0000313|EMBL:VCT83025.1,
RC ECO:0000313|Proteomes:UP000431451};
RG IHU Genomes;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAG9711255.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CC3_PB {ECO:0000313|EMBL:CAG9711255.1};
RA Mesa V.;
RL Submitted (OCT-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein bS18.
CC {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|RuleBase:RU363094};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU363094}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimI subfamily.
CC {ECO:0000256|RuleBase:RU363094}.
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DR EMBL; CAKJVE010000004; CAG9711255.1; -; Genomic_DNA.
DR EMBL; PDCJ01000004; PEG29314.1; -; Genomic_DNA.
DR EMBL; UWJD01000001; VCT83025.1; -; Genomic_DNA.
DR RefSeq; WP_058293795.1; NZ_UWJD01000001.1.
DR STRING; 137838.GCA_001458595_00864; -.
DR GeneID; 68875939; -.
DR OrthoDB; 9794566at2; -.
DR Proteomes; UP000220840; Unassembled WGS sequence.
DR Proteomes; UP000431451; Unassembled WGS sequence.
DR Proteomes; UP000789738; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR006464; AcTrfase_RimI/Ard1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR NCBIfam; TIGR01575; rimI; 1.
DR PANTHER; PTHR43420; ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43420:SF44; AMINOGLYCOSIDE N(6')-ACETYLTRANSFERASE TYPE 1; 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:0000313|EMBL:CAG9711255.1};
KW Cytoplasm {ECO:0000256|RuleBase:RU363094};
KW Reference proteome {ECO:0000313|Proteomes:UP000220840};
KW Transferase {ECO:0000313|EMBL:PEG29314.1}.
FT DOMAIN 3..145
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 145 AA; 16493 MW; 1C4A4CA31AB99E05 CRC64;
MNVQIRIMNE NDAVEVAKIS ILSFSSPWST ESYIQEIKNP VALYLVAVIN NNIVGFIGTW
NVLDESHITN VAVHPDFRKQ KIGSLLLENL INTCEKQHNT SSFDLEVRAN NIPAQKLYSK
FGFKNNGIRK GYYTDNKEDA ILMCR
//