ID   A85C_MYCAV              Reviewed;         352 AA.
AC   O52972;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Diacylglycerol acyltransferase/mycolyltransferase Ag85C;
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 C;
DE            Short=85C;
DE            Short=Ag85C;
DE   AltName: Full=Fibronectin-binding protein C;
DE            Short=Fbps C;
DE   Flags: Precursor;
GN   Name=fbpC;
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].
RC   STRAIN=ATCC 15769 / DSM 44157 / 1982;
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 to 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=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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
CC       {ECO:0000305}.
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DR   EMBL; D87323; BAA24161.1; -; Genomic_DNA.
DR   RefSeq; WP_009979822.1; NZ_NSEV01000064.1.
DR   AlphaFoldDB; O52972; -.
DR   SMR; O52972; -.
DR   ESTHER; mycav-a85c; 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; Secreted; Signal; Transferase.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..352
FT                   /note="Diacylglycerol acyltransferase/mycolyltransferase
FT                   Ag85C"
FT                   /id="PRO_0000000223"
FT   REGION          102..112
FT                   /note="Fibronectin-binding"
FT   REGION          332..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        170
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000250"
FT   BINDING         86..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         276..279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         306..308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   352 AA;  37756 MW;  A29277CB650D60A4 CRC64;
     MSFIEKVRKL RGAAATMPRR LAIAAVGASL LSGVAVAAGG SPVAGAFSKP GLPVEYLEVP
     SPSMGRNIKV QFQGGGPHAV YLLDGLRAQD DYNGWDINTP AFEEFYQSGL SVIMPVGGQS
     SFYSNWYQPS SGNGQNYTYK WETFLTQEMP LWMQSNKQVS PAGNAAVGLS MSGGSALILA
     AYYPQQFPYA ASLSGFLNPS EGWWPTLIGL AMNDSGGYNA NSMWGPSTDP AWKRNDPMVQ
     IPRLVANNTR IWVYCGNGTP SDLGGDNVPA KFLEGLTLRT NEQFQNNYAA AGGRNGVFNF
     PANGTHSWPY WNQQLMAMKP DMQQVLLSGN TTAAPAQPAQ PAQPAQPAQP AT