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Database: UniProt
Entry: A0A433K588_9GAMM
LinkDB: A0A433K588_9GAMM
Original site: A0A433K588_9GAMM 
ID   A0A433K588_9GAMM        Unreviewed;       538 AA.
AC   A0A433K588;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=GNAT family N-acetyltransferase {ECO:0000313|EMBL:RUR14223.1};
GN   ORFNames=ELY15_00215 {ECO:0000313|EMBL:RUR14223.1};
OS   Legionella sp. km772.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=2498111 {ECO:0000313|EMBL:RUR14223.1, ECO:0000313|Proteomes:UP000287796};
RN   [1] {ECO:0000313|EMBL:RUR14223.1, ECO:0000313|Proteomes:UP000287796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=km772 {ECO:0000313|Proteomes:UP000287796};
RA   Wu H.;
RT   "Legionella sp,whole genome shotgun sequence.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:RUR14223.1}.
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DR   EMBL; RZGQ01000001; RUR14223.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433K588; -.
DR   OrthoDB; 43980at2; -.
DR   Proteomes; UP000287796; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd05403; NT_KNTase_like; 1.
DR   Gene3D; 3.10.450.50; -; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR027843; DUF4440.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   PANTHER; PTHR31438; LYSINE N-ACYLTRANSFERASE C17G9.06C-RELATED; 1.
DR   PANTHER; PTHR31438:SF1; LYSINE N-ACYLTRANSFERASE C17G9.06C-RELATED; 1.
DR   Pfam; PF13523; Acetyltransf_8; 1.
DR   Pfam; PF14534; DUF4440; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287796};
KW   Transferase {ECO:0000313|EMBL:RUR14223.1}.
FT   DOMAIN          3..175
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   538 AA;  61236 MW;  0EDBF1E16181C2A1 CRC64;
     MKITFVPLAE SHFPLLLKWL ETPHVKNWWD QDVTYTLDLV KEKFGKHIHG LALSKNSNHK
     TYAYIICANK EMIGYIQAYN AHDFAQENGL NLNAISGSVC GVDLFIGEQP FLHKGCGVRI
     LNEFEEQILA PHFDWCLIDP AKDNLTAVKA FTKAGFKIFE QFQTESTAWM LKDLSSRNDP
     LPTIQKLIKE RYVQAKAIFW AGSVSEGRGT SASDLDLIIV FEEVAHAYRE AFIYDGWPID
     AFIHDLNTLR YFFEESRTGN GISGLCHMIL NGREVTNPST FSKNIKILAQ EVLNAGPAIW
     DQEQINKERF LITDVLDDIK YPTGRDEQIA SAAWLLEALG QFYFRSQNKW CASGKSIIRY
     LKSDNPDLAL EFMQAFQGLF QTSNSAALEL LVKKILDPYG GLFWNGFRSD APKESRINEA
     GILPKSIEAL ERSLLDSSVR QSTEQLNKLI ADDFLEFGSS GKVYNKHDCI KPDEYPRKFV
     VSDFKIKELS KDVTLATYKT TEDGIASLRS SIWQRYGDEW KMIFHQGTKC KVQNGHEE
//
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