ID Q8RGD2_FUSNN Unreviewed; 143 AA.
AC Q8RGD2;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=FN0369 {ECO:0000313|EMBL:AAL94572.1};
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=190304 {ECO:0000313|EMBL:AAL94572.1, ECO:0000313|Proteomes:UP000002521};
RN [1] {ECO:0000313|EMBL:AAL94572.1, ECO:0000313|Proteomes:UP000002521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 /
RC KCTC 2640 / LMG 13131 / VPI 4355 {ECO:0000313|Proteomes:UP000002521};
RX PubMed=11889109; DOI=10.1128/JB.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N., Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL94572.1; -; Genomic_DNA.
DR RefSeq; NP_603273.1; NC_003454.1.
DR RefSeq; WP_005902598.1; NZ_CP028101.1.
DR AlphaFoldDB; Q8RGD2; -.
DR STRING; 190304.FN0369; -.
DR PaxDb; 190304-FN0369; -.
DR EnsemblBacteria; AAL94572; AAL94572; FN0369.
DR GeneID; 79783378; -.
DR KEGG; fnu:FN0369; -.
DR PATRIC; fig|190304.8.peg.946; -.
DR eggNOG; COG0456; Bacteria.
DR HOGENOM; CLU_013985_23_0_0; -.
DR InParanoid; Q8RGD2; -.
DR BioCyc; FNUC190304:G1FZS-966-MONOMER; -.
DR Proteomes; UP000002521; 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; 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:AAL94572.1};
KW Cytoplasm {ECO:0000256|RuleBase:RU363094};
KW Reference proteome {ECO:0000313|Proteomes:UP000002521};
KW Transferase {ECO:0000313|EMBL:AAL94572.1}.
FT DOMAIN 1..141
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 143 AA; 16908 MW; 64F7C17C4BAA9E21 CRC64;
MIKKLEINDT DYIDQIFNLE KEIFKNSAFN RTYLDTLIKG DNSFIYVYLI DSKVCGYLIV
LDSIDIYEIL AIATIEECRN KDIAQELLNK IKTKDIFLEV RESNQPAINF YKKNKFKEIS
IRKNYYSKPN ENAIIMKLEV NNE
//
