ID D3T7A8_THEIA Unreviewed; 148 AA.
AC D3T7A8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=[Ribosomal protein bS18]-alanine N-acetyltransferase {ECO:0000256|RuleBase:RU363094};
DE EC=2.3.1.266 {ECO:0000256|RuleBase:RU363094};
GN OrderedLocusNames=Thit_0539 {ECO:0000313|EMBL:ADD01840.1};
OS Thermoanaerobacter italicus (strain DSM 9252 / Ab9).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=580331 {ECO:0000313|EMBL:ADD01840.1, ECO:0000313|Proteomes:UP000001552};
RN [1] {ECO:0000313|EMBL:ADD01840.1, ECO:0000313|Proteomes:UP000001552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9252 / JCM 16815 / Ab9 {ECO:0000313|Proteomes:UP000001552};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacter italicus Ab9.";
RL Submitted (FEB-2010) 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; CP001936; ADD01840.1; -; Genomic_DNA.
DR RefSeq; WP_012994663.1; NC_013921.1.
DR AlphaFoldDB; D3T7A8; -.
DR KEGG; tit:Thit_0539; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_23_3_9; -.
DR OrthoDB; 9794566at2; -.
DR Proteomes; UP000001552; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008999; F:peptide-alanine-alpha-N-acetyltransferase activity; IEA:RHEA.
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:SF59; [RIBOSOMAL PROTEIN S18]-ALANINE N-ACETYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR43420; 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 Cytoplasm {ECO:0000256|RuleBase:RU363094};
KW Transferase {ECO:0000313|EMBL:ADD01840.1}.
FT DOMAIN 3..148
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 148 AA; 16976 MW; C790A532AA3998F4 CRC64;
MDVIIRLMRK EDVEEVLEIE KLSFSTPWSK EAFISEVTKN SCAKYIVAEV DNKIVGYGGF
WVVVDEGHIT NIAVHPEYRS KGIGSKIMEG LIELAKKNGI ISMTLEVRES NIVAQHLYAK
FGFRPLGRRK GYYQDNNEDA IIMWKYDL
//
