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Database: UniProt
Entry: R7A8V7_9FIRM
LinkDB: R7A8V7_9FIRM
Original site: R7A8V7_9FIRM 
ID   R7A8V7_9FIRM            Unreviewed;       143 AA.
AC   R7A8V7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=[Ribosomal protein bS18]-alanine N-acetyltransferase {ECO:0000256|RuleBase:RU363094};
DE            EC=2.3.1.266 {ECO:0000256|RuleBase:RU363094};
GN   ORFNames=BN599_01646 {ECO:0000313|EMBL:CDD51924.1};
OS   Firmicutes bacterium CAG:308.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263016 {ECO:0000313|EMBL:CDD51924.1, ECO:0000313|Proteomes:UP000017945};
RN   [1] {ECO:0000313|EMBL:CDD51924.1, ECO:0000313|Proteomes:UP000017945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:308 {ECO:0000313|Proteomes:UP000017945};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDD51924.1}.
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DR   EMBL; CBHE010000092; CDD51924.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7A8V7; -.
DR   Proteomes; UP000017945; Unassembled WGS sequence.
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; PTHR43617:SF20; GCN5-RELATED 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   Cytoplasm {ECO:0000256|RuleBase:RU363094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017945};
KW   Transferase {ECO:0000313|EMBL:CDD51924.1}.
FT   DOMAIN          1..143
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   143 AA;  16656 MW;  309AC04DE610D0A9 CRC64;
     MIEIMRKEDL AQIVDLEKKC FNDAWNLKQI ENELEVNPFS NGYMLKENDK VVAYAFMWET
     FEMAQIARIG VDPDQRKKHY GQKMMEELFE KARSGGCEYM SLEVRESNTA AIKLYEKLGF
     VTVNVSKGYY SDNENAIVMT RAL
//
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