ID   A85B_MYCSC              Reviewed;         330 AA.
AC   Q50397;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 76.
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 scrofulaceum.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1783;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19981 / DSM 43992 / JCM 6381 / NCTC 10803 / TMC 1323;
RX   PubMed=8047837; DOI=10.1111/j.1365-3083.1994.tb03446.x;
RA   Takano M., Ohara N., Mizuno A., Yamada T.;
RT   "Cloning, sequencing and expression in Escherichia coli of the gene for
RT   alpha antigen from Mycobacterium scrofulaceum.";
RL   Scand. J. Immunol. 40:165-170(1994).
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; D26187; BAA05332.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q50397; -.
DR   SMR; Q50397; -.
DR   STRING; 1783.BST44_18455; -.
DR   ESTHER; mycsc-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   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00756; Esterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS51318; TAT; 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_0000000221"
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;  34943 MW;  09D6E04B5E9ED221 CRC64;
     MTDLSKKVRA WGRRLLVGTA AAVTLPGLIG LAGGAPTAGA FSRPGLPVEY LQVPSAGMGR
     NIKVQFQSGG NNSPAVYLLD GLRAQDDYNG WDINTPAFEW YYQSGLSIIM PVGGQSSFYS
     DWYSPACGKA GCTTYKWETF LTSELPQYLQ SNKSVKPTGS AAVGISMAGS SALILAAYHP
     QQFIYAGSLS ALMDPSQGMG PSLIGLAMGD AGGYKASDMW GPSSDPAWQR NDPTIQIPKL
     VGNNTRLWVY CGNGTPSELG GANMPAEFLE NFVRSSNLKF QDAYNAAGGH NAVFHFDQNG
     THSWEYWGAQ LNAMKPDLQG TLGATPGGGG