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 27-MAR-2024, entry version 68.
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; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//
