A85B_MYCBP
ID A85B_MYCBP Reviewed; 325 AA.
AC A1KJU9; P12942;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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; OrderedLocusNames=BCG_1923c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=7987013;
RA de Wit L., Palou M., Content J.;
RT "Nucleotide sequence of the 85B-protein gene of Mycobacterium bovis BCG and
RT Mycobacterium tuberculosis.";
RL DNA Seq. 4:267-270(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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 Mycobacteria 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; X62397; CAA44268.1; -; Genomic_DNA.
DR EMBL; AM408590; CAL71910.1; -; Genomic_DNA.
DR PIR; S29663; S29663.
DR RefSeq; WP_011799226.1; NC_008769.1.
DR AlphaFoldDB; A1KJU9; -.
DR SMR; A1KJU9; -.
DR ESTHER; myctu-a85b; A85-Mycolyl-transferase.
DR PRIDE; A1KJU9; -.
DR KEGG; mbb:BCG_1923c; -.
DR HOGENOM; CLU_026624_3_1_11; -.
DR OMA; GANMPAE; -.
DR Proteomes; UP000001472; Chromosome.
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; Disulfide bond; Secreted; Signal; Transferase.
FT SIGNAL 1..40
FT /evidence="ECO:0000250"
FT CHAIN 41..325
FT /note="Diacylglycerol acyltransferase/mycolyltransferase
FT Ag85B"
FT /id="PRO_0000285178"
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; 34547 MW; B7775F40C131BC7D CRC64;
MTDVSRKIRA WGRRLMIGTA AAVVLPGLVG LAGGAATAGA FSRPGLPVEY LQVPSPSMGR
DIKVQFQSGG NNSPAVYLLD GLRAQDDYNG WDINTPAFEW YYQSGLSIVM PVGGQSSFYS
DWYSPACGKA GCQTYKWETL LTSELPQWLS ANRAVKPTGS AAIGLSMAGS SAMILAAYHP
QQFIYAGSLS ALLDPSQGMG PSLIGLAMGD AGGYKAADMW GPSSDPAWER NDPTQQIPKL
VANNTRLWVY CGNGTPNELG GANIPAEFLE NFVRSSNLKF QDAYNAAGGH NAVFNFPPNG
THSWEYWGAQ LNAMKGDLQS SLGAG
