ID   A85A_MYCUL              Reviewed;         337 AA.
AC   P58248;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Diacylglycerol acyltransferase/mycolyltransferase Ag85A;
DE            Short=DGAT;
DE            EC=2.3.1.122;
DE            EC=2.3.1.20;
DE   AltName: Full=Acyl-CoA:diacylglycerol acyltransferase;
DE   AltName: Full=Antigen 85 complex A;
DE            Short=85A;
DE            Short=Ag85A;
DE   AltName: Full=Fibronectin-binding protein A;
DE            Short=Fbps A;
DE   Flags: Precursor;
GN   Name=fbpA;
OS   Mycobacterium ulcerans.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1809;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ITM 5150;
RA   Tanghe A.J.;
RT   "Protective efficacy of DNA vaccine encoding antigen 85A from M. bovis BCG
RT   against Buruli Ulcer.";
RL   Thesis (2001), Universite Libre de Bruxelles, Belgium.
CC   -!- FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible
CC       for the high affinity of mycobacteria for fibronectin, a large adhesive
CC       glycoprotein, which facilitates the attachment of M.tuberculosis to
CC       murine alveolar macrophages (AMs). They also help to maintain the
CC       integrity of the cell wall by catalyzing the transfer of mycolic acids
CC       to cell wall arabinogalactan, and through the synthesis of alpha,alpha-
CC       trehalose dimycolate (TDM, cord factor). They catalyze the transfer of
CC       a mycoloyl residue from one molecule of alpha,alpha-trehalose
CC       monomycolate (TMM) to another TMM, leading to the formation of TDM.
CC       FbpA mediates triacylglycerol (TAG) formation with long-chain acyl-CoA
CC       as the acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as
CC       the acyl acceptor. It has a preference for C26:0-CoA over C18:1-CoA (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC         + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose
CC         6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234;
CC         EC=2.3.1.122;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Cytoplasm.
CC   -!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
CC       {ECO:0000305}.
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DR   EMBL; AJ300576; CAC40861.1; -; Genomic_DNA.
DR   RefSeq; WP_011742456.1; NZ_MDUB01000111.1.
DR   AlphaFoldDB; P58248; -.
DR   SMR; P58248; -.
DR   ESTHER; mycul-a85a; A85-Mycolyl-transferase.
DR   OMA; AWARNDP; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050348; F:trehalose O-mycolyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000801; Esterase-like.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00756; Esterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell wall; Cytoplasm; Disulfide bond; Secreted; Signal;
KW   Transferase.
FT   SIGNAL          1..42
FT                   /evidence="ECO:0000250"
FT   CHAIN           43..337
FT                   /note="Diacylglycerol acyltransferase/mycolyltransferase
FT                   Ag85A"
FT                   /id="PRO_0000000215"
FT   REGION          101..111
FT                   /note="Fibronectin-binding"
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000250"
FT   BINDING         85..86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         275..278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         305..307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        130..135
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   337 AA;  35643 MW;  99022BE4077E5773 CRC64;
     MKLVDRFRGA ATGTSRRLMV GAVGAALLSG LVGFVGGSAT ASAFSRPGLP VEYLQVPSVA
     MGRNIKVQFQ SGGANSPALY LLDGMRAQDD FSGWDINTPA FEWYYQSGIS VAMPVGGQSS
     FYSDWYNPAC GKAGCTTYKW ETFLTSELPQ YLSANKGVKP TGSGVVGLSM AGSSALILAA
     YHPDQFVYSG SLSALLDPSQ GIGPSLIGLA MGDAGGYKAS DMWGPKDDPA WARNDPMLQV
     GKLVANNTRI WVYCGNGKPS DLGGDNLPAK FLEGFVRTSN MKFQAAYNAA GGHNAVWNFD
     DNGTHSWEYW GAQLNAMRPD LQHTLGATPN TGDTQGA