ID W1IUS2_9GAMM Unreviewed; 196 AA.
AC W1IUS2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=[ribosomal protein S5]-alanine N-acetyltransferase {ECO:0000256|ARBA:ARBA00039124};
DE EC=2.3.1.267 {ECO:0000256|ARBA:ARBA00039124};
GN Name=rimJ {ECO:0000313|EMBL:CDL81371.1};
GN ORFNames=XSR1_120090 {ECO:0000313|EMBL:CDL81371.1};
OS Xenorhabdus szentirmaii DSM 16338.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL81371.1, ECO:0000313|Proteomes:UP000019202};
RN [1] {ECO:0000313|EMBL:CDL81371.1, ECO:0000313|Proteomes:UP000019202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL81371.1,
RC ECO:0000313|Proteomes:UP000019202};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacteria,
RT Xenorhabdus cabanillasi strain JM26 and Xenorhabdus szentirmai strain DSM
RT 16338.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:CDL81371.1}.
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DR EMBL; CBXF010000024; CDL81371.1; -; Genomic_DNA.
DR RefSeq; WP_038234900.1; NZ_NIBV01000002.1.
DR AlphaFoldDB; W1IUS2; -.
DR STRING; 1427518.XSR1_120090; -.
DR OrthoDB; 9801669at2; -.
DR Proteomes; UP000019202; 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 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:CDL81371.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000019202};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDL81371.1}.
FT DOMAIN 18..183
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 196 AA; 23117 MW; DFD9C6B3DEF1F5CE CRC64;
MFGYRSALPK IRFITDRMIV RLVYERDAYK LAEYYSENKD FLKPWEPARD GTFYQPSGWT
NKLSYISELQ RQEATFNFLL LDPDENEIMG VANFTNVMRG AFYSCYLGYS LGEKWQGQGV
MYEALLPTIR YMQRHQKMHR IMANYMPHNH RSGNLLKKLG FEQEGYAKNY LMIDGVWQDH
VLTSLIDDTW GKTTGI
//
