ID   BAED_BACVZ              Reviewed;         324 AA.
AC   A7Z4X9;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Polyketide biosynthesis acyltransferase homolog BaeD;
DE            Short=AT;
DE            EC=2.3.1.-;
DE   AltName: Full=Transacylase;
GN   Name=baeD; OrderedLocusNames=RBAM_016920;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
RN   [2]
RP   PATHWAY, AND FUNCTION IN BACILLAENE BIOSYNTHESIS.
RX   PubMed=16707694; DOI=10.1128/jb.00052-06;
RA   Chen X.-H., Vater J., Piel J., Franke P., Scholz R., Schneider K.,
RA   Koumoutsi A., Hitzeroth G., Grammel N., Strittmatter A.W., Gottschalk G.,
RA   Suessmuth R.D., Borriss R.;
RT   "Structural and functional characterization of three polyketide synthase
RT   gene clusters in Bacillus amyloliquefaciens FZB 42.";
RL   J. Bacteriol. 188:4024-4036(2006).
CC   -!- FUNCTION: Probably involved in some intermediate steps for the
CC       synthesis of the antibiotic polyketide bacillaene which is involved in
CC       secondary metabolism. {ECO:0000269|PubMed:16707694}.
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC       {ECO:0000269|PubMed:16707694}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; CP000560; ABS74055.1; -; Genomic_DNA.
DR   RefSeq; WP_012117590.1; NC_009725.2.
DR   AlphaFoldDB; A7Z4X9; -.
DR   SMR; A7Z4X9; -.
DR   STRING; 326423.RBAM_016920; -.
DR   EnsemblBacteria; ABS74055; ABS74055; RBAM_016920.
DR   KEGG; bay:RBAM_016920; -.
DR   HOGENOM; CLU_030558_3_1_9; -.
DR   OMA; DSHFVIS; -.
DR   UniPathway; UPA01003; -.
DR   Proteomes; UP000001120; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.366.10; -; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Antibiotic biosynthesis; Cytoplasm; Transferase.
FT   CHAIN           1..324
FT                   /note="Polyketide biosynthesis acyltransferase homolog
FT                   BaeD"
FT                   /id="PRO_0000387999"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  36425 MW;  3F41F41BC8ACB0B8 CRC64;
     MNQPIVFMFS GQGSQYYQMG KELFAHNAAF RQKMLDLDDF AVSRFGYSVL KEMYHTGNRL
     SDPFDRLLFS HPAIFMAEYA LAYALEQRGI RPDYVIGASL GEYAAAAVSG VLSAEDALDC
     VLEQARIVTE TCRNGSMLAI LGDPALYQDD PLLGEHSELA SVNYHSHFVI SGEREHIKKI
     MDDLREKQIP HQLLPVSYGF HSALVDQAEQ PYKRFLAQKS IRTPFIPYIS SATGEAETDI
     QADFFWDIVR KPIRFREALQ FADSRQKGLY IDAGPSGTLA AFAKQILPAG SAERIRAIMT
     PFHKEQTHLQ QIEDSILSPP GRRL