ID   A85B_MYCKA              Reviewed;         325 AA.
AC   P21160;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 89.
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 kansasii.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2404875; DOI=10.1128/iai.58.2.550-556.1990;
RA   Matsuo K., Yamaguchi R., Yamazaki A., Tasaka H., Terasaka K., Yamada T.;
RT   "Cloning and expression of the gene for the cross-reactive alpha antigen of
RT   Mycobacterium kansasii.";
RL   Infect. Immun. 58:550-556(1990).
RN   [2]
RP   DOMAIN FIBRONECTIN BINDING.
RX   PubMed=9446601; DOI=10.1074/jbc.273.5.2905;
RA   Naito M., Ohara N., Matsumoto S., Yamada T.;
RT   "The novel fibronectin-binding motif and key residues of mycobacteria.";
RL   J. Biol. Chem. 273:2905-2909(1998).
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; X53897; CAA37868.1; -; Genomic_DNA.
DR   PIR; A37185; A37185.
DR   RefSeq; WP_023364215.1; NZ_UPHJ01000063.1.
DR   AlphaFoldDB; P21160; -.
DR   SMR; P21160; -.
DR   STRING; 1768.B1T50_00710; -.
DR   ESTHER; mycka-a85b; A85-Mycolyl-transferase.
DR   GeneID; 29700744; -.
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   1: Evidence at protein level;
KW   Acyltransferase; Disulfide bond; Secreted; Signal; Transferase.
FT   SIGNAL          1..40
FT   CHAIN           41..325
FT                   /note="Diacylglycerol acyltransferase/mycolyltransferase
FT                   Ag85B"
FT                   /id="PRO_0000000219"
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   325 AA;  34323 MW;  5F2281BCC48AE30D CRC64;
     MTDVSGKIRA WGRRLLVGAA AAAALPGLVG LAGGAATAGA FSRPGLPVEY LQVPSAAMGR
     SIKVQFQSGG DNSPAVYLLD GLRAQDDYNG WDINTPAFEW YYQSGLSVIM PVGGQSSFYS
     DWYSPACGKA GCTTYKWETF LTSELPQWLS ANRSVKPTGS AAVGISMAGS SALILSVYHP
     QQFIYAGSLS ALMDPSQGMG PSLIGLAMGD AGGYKASDMW GPSSDPAWQR NDPSLHIPEL
     VANNTRLWIY CGNGTPSELG GANVPAEFLE NFVRSSNLKF QDAYNAAGGH NAVFNLDANG
     THSWEYWGAQ LNAMKGDLQA SLGAR