ID   A85A_MYCAV              Reviewed;         347 AA.
AC   O52956;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 82.
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 avium.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9284137; DOI=10.1128/iai.65.9.3680-3685.1997;
RA   Ohara N., Ohara-Wada N., Kitaura H., Nishiyama T., Matsumoto S., Yamada T.;
RT   "Analysis of the genes encoding the antigen 85 complex and MPT51 from
RT   Mycobacterium avium.";
RL   Infect. Immun. 65:3680-3685(1997).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D78144; BAA24156.1; -; Genomic_DNA.
DR   RefSeq; WP_011723409.1; NZ_NSFM01000001.1.
DR   AlphaFoldDB; O52956; -.
DR   SMR; O52956; -.
DR   ESTHER; mycav-a85a; A85-Mycolyl-transferase.
DR   GeneID; 66692010; -.
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..43
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..347
FT                   /note="Diacylglycerol acyltransferase/mycolyltransferase
FT                   Ag85A"
FT                   /id="PRO_0000000210"
FT   REGION          101..111
FT                   /note="Fibronectin-binding"
FT   REGION          326..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   347 AA;  36096 MW;  DFAFF3DE504C208E CRC64;
     MTLVDRLRGA VAGMPRRLVV GAAGAALLSG LIGAVGGSAT AGAFSRPGLP VEYLQVPSAA
     MGRDIKVQFQ SGGANSPALY LLDGMRAQDD FNGWDINTPA FEWYNQSGIS VAMPVGGQSS
     FYSDWYKPAC GKAGCTTYKW ETFLTSELPQ YLSAQKQVKP TGSGVVGLSM AGSSALILAA
     YHPDQFVYAG SLSALLDPSQ GMGPSLIGLA MGDAGGYKAA DMWGPKEDPA WARNDPSLQV
     GKLVANNTRI WVYCGNGKPS DLGGDNLPAK FLEGFVRTSN LKFQDAYNGA GGHNAVWNFD
     ANGTHDWPYW GAQLQAMKPD LQSVLGATPG AGPATAAATN AGNGQGT