ID   A85A_MYCMR              Reviewed;         139 AA.
AC   Q9KH57;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 63.
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: Fragment;
GN   Name=fbpA;
OS   Mycobacterium marinum.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1781;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 927 / DSM 44344 / JCM 12275 / NCTC 2275 / TMC 1218;
RA   Stiear T.P., Jenkin G.A., Johnson P.D.R., Davies J.K.;
RT   "Comparative genetic analysis of Mycobacterium ulcerans and Mycobacterium
RT   marinum reveals evidence of recent divergence.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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; AF271345; AAF86326.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KH57; -.
DR   SMR; Q9KH57; -.
DR   ESTHER; mycul-a85a; A85-Mycolyl-transferase.
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   Pfam; PF00756; Esterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell wall; Cytoplasm; Secreted; Transferase.
FT   CHAIN           <1..>139
FT                   /note="Diacylglycerol acyltransferase/mycolyltransferase
FT                   Ag85A"
FT                   /id="PRO_0000093796"
FT   ACT_SITE        10
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         139
SQ   SEQUENCE   139 AA;  14449 MW;  6E0ED52C7CA48637 CRC64;
     PTGSGVVGLS MAGSSALILA AYHPDQFVYS GSLSALLDPS QGMGPSLIGL AMGDAGGYKA
     SDMWGPKDDP AWARNDPMLQ VGKLVANNTR IWVYCGNGKP SDLGGDNLPA KFLEGFVRTS
     NMKFQAAYNA AGGHNAVWN