ID   BAEC_BACVZ              Reviewed;         289 AA.
AC   A7Z4X8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Polyketide biosynthesis malonyl CoA-acyl carrier protein transacylase BaeC;
DE            Short=AT;
DE            EC=2.3.1.39;
GN   Name=baeC; OrderedLocusNames=RBAM_016910;
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: Involved in some intermediate steps for the synthesis of the
CC       antibiotic polyketide bacillaene which is involved in secondary
CC       metabolism. It catalyzes the transfer of the malonyl-CoA group to the
CC       acyl-carrier-protein AcpK (Mal-AcpK) (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:16707694}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC       {ECO:0000269|PubMed:16707694}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FabD family. {ECO:0000305}.
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DR   EMBL; CP000560; ABS74054.1; -; Genomic_DNA.
DR   RefSeq; WP_012117589.1; NC_009725.2.
DR   AlphaFoldDB; A7Z4X8; -.
DR   SMR; A7Z4X8; -.
DR   STRING; 326423.RBAM_016910; -.
DR   EnsemblBacteria; ABS74054; ABS74054; RBAM_016910.
DR   KEGG; bay:RBAM_016910; -.
DR   HOGENOM; CLU_030558_1_3_9; -.
DR   OMA; LNKTQFT; -.
DR   UniPathway; UPA01003; -.
DR   Proteomes; UP000001120; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
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; IPR024925; Malonyl_CoA-ACP_transAc.
DR   InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   PIRSF; PIRSF000446; Mct; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   TIGRFAMs; TIGR00128; fabD; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Antibiotic biosynthesis; Cytoplasm; Transferase.
FT   CHAIN           1..289
FT                   /note="Polyketide biosynthesis malonyl CoA-acyl carrier
FT                   protein transacylase BaeC"
FT                   /id="PRO_0000388003"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  32318 MW;  C85AA1EED2BDCE95 CRC64;
     MITYLFPGQG SQKQGMGSSL FDEFKDLTEQ ADETLGYSMK RLCLENPYSN LHKTQFTQPA
     LYVVNVLSYL KKIQDNDIKP DYVAGHSLGE YNALFAAGAF DFITGLQLVR KRGELMSMAT
     DGKMAAVMGL TAAQVSDALQ THGLHTIDIA NMNSPHQVVI SGRKEDIERA KSVFEGLKDV
     TMFHPLNVSG AFHSRYMSEA KQEFEKFLQS FHFSAISIPV ISNVHARPYE QDGIHSVLAD
     QIDHSVRWND SIRYLLDKGR MEFEEVGPGH VLTGLIHRIK NETEASPAM