ID E3PVD2_ACESD Unreviewed; 185 AA.
AC E3PVD2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=[ribosomal protein S5]-alanine N-acetyltransferase {ECO:0000256|ARBA:ARBA00039124};
DE EC=2.3.1.267 {ECO:0000256|ARBA:ARBA00039124};
GN OrderedLocusNames=CLOST_2470 {ECO:0000313|EMBL:CBH22585.1};
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177 {ECO:0000313|EMBL:CBH22585.1, ECO:0000313|Proteomes:UP000007041};
RN [1] {ECO:0000313|Proteomes:UP000007041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC {ECO:0000313|Proteomes:UP000007041};
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[ribosomal protein uS5] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein uS5];
CC Xref=Rhea:RHEA:43752, Rhea:RHEA-COMP:10672, Rhea:RHEA-COMP:10673,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:64718, ChEBI:CHEBI:83683; EC=2.3.1.267;
CC Evidence={ECO:0000256|ARBA:ARBA00036822};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimJ subfamily.
CC {ECO:0000256|ARBA:ARBA00038502}.
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DR EMBL; FP565809; CBH22585.1; -; Genomic_DNA.
DR AlphaFoldDB; E3PVD2; -.
DR STRING; 1511.CLOST_2470; -.
DR KEGG; cst:CLOST_2470; -.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_013985_40_1_9; -.
DR BioCyc; CSTI499177:GJE9-2563-MONOMER; -.
DR Proteomes; UP000007041; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008999; F:peptide-alanine-alpha-N-acetyltransferase activity; IEA:RHEA.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR43792:SF8; [RIBOSOMAL PROTEIN S5]-ALANINE N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43792; GNAT FAMILY, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G00765)-RELATED-RELATED; 1.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:CBH22585.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000007041};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBH22585.1}.
FT DOMAIN 24..181
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 185 AA; 22047 MW; EDFF6217002DAA67 CRC64;
MNKIYETENL FLKGLDKSSA RQVLDYYMRN KAFLEELEII RNEEFYTLNF QEKLLEEEAR
YIENKNLVKL WLFKKDDDEK VIGSIAFNNI VRGAFLSCHL GYKLDANEIN KGYMTQALNK
GIDIVFNELG LHRIEANIMP KNKRSLRVVE KLGFYNEGIA YKYLKINNRW EDHIHMVLRN
ERLET
//
