A85A_MYCGO
ID A85A_MYCGO Reviewed; 339 AA.
AC O06052;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 gordonae.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14470 / DSM 44160 / JCM 6382 / NCTC 10267 / TMC 1324;
RX PubMed=9281410; DOI=10.1006/mcpr.1997.0110;
RA Dumonceaux M., Fauville Dufaux M., Ooms J., De Wit L., Sonck P.,
RA Content J.;
RT "Cloning of the antigen 85A from Mycobacterium gordonae and its use for the
RT specific PCR identification of these mycobacteria.";
RL Mol. Cell. Probes 11:251-258(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}.
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DR EMBL; Y10378; CAA71406.1; -; Genomic_DNA.
DR AlphaFoldDB; O06052; -.
DR SMR; O06052; -.
DR STRING; 1778.A9W97_06290; -.
DR ESTHER; mycgo-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; Disulfide bond; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..339
FT /note="Diacylglycerol acyltransferase/mycolyltransferase
FT Ag85A"
FT /id="PRO_0000000212"
FT REGION 101..111
FT /note="Fibronectin-binding"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT ACT_SITE 304
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 274..277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 304..306
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 130..135
FT /evidence="ECO:0000250"
SQ SEQUENCE 339 AA; 35474 MW; 909B7E0E3969E2DE CRC64;
MKLVDRFRGA VTGMPRRLMV GAVGAALLSG LVGFVGGSAT ASAFSRPGLP VEYLQVPSAA
MGRNIKIQFQ SGGANSPALY LLDGMRAQDD YNGWDINTPA FEWYNQSGIS VVMPVGGQSS
FYSDWYNPAC GKAGCTTYKW ETFLTSELPA YLASNKQVKP TGSAAVGLSM AGSSALILAA
YHPDQFVYAG SLSALLDPSQ AMGPSLIGLA MGDAGGYKAS DMWGPRGPAW QRNDPSLQVG
KLVANNSRLW IYCGDGKPSD LGGNNLPAKF LEGFVRTSNL KFQEAYNGAG GHNAVFNFDA
NGTHDWPYWG APVQAMKGDL QSTLGATPGA GPATAAASA
