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Database: UniProt
Entry: U3U3W7_9ENTR
LinkDB: U3U3W7_9ENTR
Original site: U3U3W7_9ENTR 
ID   U3U3W7_9ENTR            Unreviewed;       894 AA.
AC   U3U3W7;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=GCN5-like N-acetyltransferase {ECO:0000313|EMBL:BAN98052.1};
GN   ORFNames=E05_32860 {ECO:0000313|EMBL:BAN98052.1};
OS   Plautia stali symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN98052.1, ECO:0000313|Proteomes:UP000016901};
RN   [1] {ECO:0000313|EMBL:BAN98052.1, ECO:0000313|Proteomes:UP000016901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA   Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT   "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT   lipopolysaccharide.";
RL   Microbiol. Res. 167:48-54(2011).
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DR   EMBL; AP012551; BAN98052.1; -; Genomic_DNA.
DR   AlphaFoldDB; U3U3W7; -.
DR   KEGG; psts:E05_32860; -.
DR   eggNOG; COG1042; Bacteria.
DR   eggNOG; COG1670; Bacteria.
DR   HOGENOM; CLU_007415_0_2_6; -.
DR   Proteomes; UP000016901; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF13549; ATP-grasp_5; 1.
DR   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016901};
KW   Transferase {ECO:0000313|EMBL:BAN98052.1}.
FT   DOMAIN          725..880
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   894 AA;  97471 MW;  738478782E1A2031 CRC64;
     MMSQRGLEAL LRPKSIAVLG ASVKPGRAGY LMMRNLLAGG FGGPVLPVTP KYKAVSGVLA
     WPDVASLPFA PDLAIICTHA RRNLELLQQL GEKGCKACII LSAPTSQLEA LKACASQWQM
     RLLGPNSLGL LAPWQGLNAS FSPVPIAKGR IAFISQSAAV SNTILDWAQQ RNLGFSWFIA
     LGDSLDIDVD DLLDFLARDG KTSAILLYLE HLSDARRFVS ASRSAARNKL ILVIKSGRSH
     QAQAMIGTAS GLDAAWDAAI QRAGLLRVQD THELFSAVES LSHMCPLRGE RLMIISNGAA
     PAALALDELY ARNGKLATLD EPTLQALAAL LPEGIGRGNP LDLKDHATPA LYVACVTQLL
     DSHELDALMI IHSPSAVSPA SETAAQIIAA VAAHSRGKQV TLLTNWCGEH SSQEARRAFT
     QAGIPTWRTP EGTVTAFMHQ VEYRRNQKQL RETPALPLGL TQNSTEAHQL LQQALDSGIT
     TLDTHEVQPI LQAYGLATLP TWIASDSQAA ATIADQIGYP VALKLRSPDI AHKSDEQGVM
     LYLRSAAEVE QAADAIFDRV RETHPQARID GLLVQANRAG AQELRVVVEH DPLFGPIIML
     GEGGVEWQPD KQAAVALPPL NMTLARYLVI QALKSGKVRS RSALRPLDIT GLSQLLVQVS
     NLVVDCPEIQ RLDIHPLLAS ANTFTLLDVT LQLAPFHGDS EARLAIRPYP HHLEEQVQLK
     DGQRCLFRPI LPEDEPQLRA FIAQVTKEDL YYRYFSEINE FTHDDLANMT QIDYDREMAI
     VAVRQHNGAD EIIGVTRAIS DADNIDAEFS VLVRSDLKGL GMGRRLLEKM IRYTRDHGLQ
     QLNGITMPHN TCMITLARKL NFRVNIQLDD GIVSLNLPLA DTGDLAVEKG KKPP
//
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