ID A0A1M6SZL3_9CLOT Unreviewed; 310 AA.
AC A0A1M6SZL3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=[ribosomal protein S5]-alanine N-acetyltransferase {ECO:0000256|ARBA:ARBA00039124};
DE EC=2.3.1.267 {ECO:0000256|ARBA:ARBA00039124};
GN ORFNames=SAMN02745163_03933 {ECO:0000313|EMBL:SHK50193.1};
OS Clostridium cavendishii DSM 21758.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121302 {ECO:0000313|EMBL:SHK50193.1, ECO:0000313|Proteomes:UP000184310};
RN [1] {ECO:0000313|EMBL:SHK50193.1, ECO:0000313|Proteomes:UP000184310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21758 {ECO:0000313|EMBL:SHK50193.1,
RC ECO:0000313|Proteomes:UP000184310};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQZB01000018; SHK50193.1; -; Genomic_DNA.
DR RefSeq; WP_072992151.1; NZ_FQZB01000018.1.
DR AlphaFoldDB; A0A1M6SZL3; -.
DR STRING; 1121302.SAMN02745163_03933; -.
DR OrthoDB; 9801656at2; -.
DR Proteomes; UP000184310; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000184310};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SHK50193.1}.
FT DOMAIN 142..304
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 310 AA; 36247 MW; 5BE82A4094E81561 CRC64;
MSGEKNITIE LLNGTKIEYI IRDKIGITIG RFKIIELDKE NKRASIRLKF YREDNYKLFK
ESISLIVNAL FKDKEIYKVN VFVSDNTNIN AFLDLGFILE GIIGENLFIN CVYRDELIFG
INRFSFKEKC KIIQFQLDGV NIDLRNLSPE HAEEMLDYYK RNENHLKNFE PSRDMSFYTY
ETQKNILLES YKQFIDGSSL DLGIFKDNYL IGKLKLSNIV YGIFKSAFLG YSIDEEYQGK
GYMKEAVNLL CTYAFEEMGL HRIEASTLVD NKKSQGVLRS CGFKEVGLNE KYLYINGEWK
DHITFCKIKE
//