ID   A85B_MYCAV              Reviewed;         330 AA.
AC   Q06947;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Diacylglycerol acyltransferase/mycolyltransferase Ag85B;
DE            Short=DGAT;
DE            EC=2.3.1.122;
DE            EC=2.3.1.20;
DE   AltName: Full=30 kDa extracellular protein;
DE   AltName: Full=Acyl-CoA:diacylglycerol acyltransferase;
DE   AltName: Full=Antigen 85 complex B;
DE            Short=85B;
DE            Short=Ag85B;
DE   AltName: Full=Extracellular alpha-antigen;
DE   AltName: Full=Fibronectin-binding protein B;
DE            Short=Fbps B;
DE   Flags: Precursor;
GN   Name=fbpB;
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=7681039; DOI=10.1128/iai.61.4.1173-1179.1993;
RA   Ohara N., Matsuo K., Yamaguchi R., Yamazaki A., Tasaka H., Yamada T.;
RT   "Cloning and sequencing of the gene for alpha antigen from Mycobacterium
RT   avium and mapping of B-cell epitopes.";
RL   Infect. Immun. 61:1173-1179(1993).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- 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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
CC       {ECO:0000305}.
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DR   EMBL; X63437; CAA45032.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q06947; -.
DR   SMR; Q06947; -.
DR   ESTHER; mycav-a85b; A85-Mycolyl-transferase.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Disulfide bond; Secreted; Signal; Transferase.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000250"
FT   CHAIN           41..330
FT                   /note="Diacylglycerol acyltransferase/mycolyltransferase
FT                   Ag85B"
FT                   /id="PRO_0000000216"
FT   REGION          98..108
FT                   /note="Fibronectin-binding"
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000250"
FT   BINDING         82..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         272..275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         302..304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        127..132
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   330 AA;  34734 MW;  6ACA5980E840B2D8 CRC64;
     MTDLSEKVRA WGRRLLVGAA AAVTLPGLIG LAGGAATANA FSRPGLPVEY LQVPSAGMGR
     DIKVQFQSGG NGSPAVYLLD GLRAQDDYNG WDINTPAFEW YYQSGLSVIM PVGGQSSFYA
     DWYQPACGKA GCSTYKWETF LTSELPSYLA SNKGVKRTGN AAVGISMSGS SAMILAVNHP
     DQFIYAGSLS ALLDPSQGMG PSLIGLAMGD AGGYKADAMW GPSSDPAWQR NDPSLHIPEL
     VGHNTRLWLY CGNGTPSELG GANMPAEFLE NFVRSSNLKF QDAYNGAGGH NAVFNFNANG
     THSWEYWGAQ LNAMKPDLQG TLGASPGGGG