A85B_MYCTA
ID A85B_MYCTA Reviewed; 325 AA.
AC A5U3Q3; P31952; Q9RMI0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=MRA_1897;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-325.
RA Fan X.-L., Xu Z.H.K., Bai G.-C.H., Li Y.;
RT "Cloning of Ag85B gene of Mycobacterium tuberculosis and its construction
RT of eukaryotic expression vector.";
RL Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 16:314-316(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000611; ABQ73653.1; -; Genomic_DNA.
DR EMBL; AF198032; AAF13448.1; -; Genomic_DNA.
DR RefSeq; WP_003409456.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U3Q3; -.
DR SMR; A5U3Q3; -.
DR STRING; 419947.MRA_1897; -.
DR ESTHER; myctu-a85b; A85-Mycolyl-transferase.
DR EnsemblBacteria; ABQ73653; ABQ73653; MRA_1897.
DR GeneID; 45425859; -.
DR KEGG; mra:MRA_1897; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_026624_3_1_11; -.
DR OMA; GANMPAE; -.
DR OrthoDB; 1828423at2; -.
DR Proteomes; UP000001988; 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:0000255"
FT CHAIN 41..325
FT /note="Diacylglycerol acyltransferase/mycolyltransferase
FT Ag85B"
FT /id="PRO_0000300058"
FT REGION 98..108
FT /note="Fibronectin-binding"
FT /evidence="ECO:0000250"
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; 34581 MW; B993B5442FD5567D CRC64;
MTDVSRKIRA WGRRLMIGTA AAVVLPGLVG LAGGAATAGA FSRPGLPVEY LQVPSPSMGR
DIKVQFQSGG NNSPAVYLLD GLRAQDDYNG WDINTPAFEW YYQSGLSIVM PVGGQSSFYS
DWYSPACGKA GCQTYKWETF LTSELPQWLS ANRAVKPTGS AAIGLSMAGS SAMILAAYHP
QQFIYAGSLS ALLDPSQGMG PSLIGLAMGD AGGYKAADMW GPSSDPAWER NDPTQQIPKL
VANNTRLWVY CGNGTPNELG GANIPAEFLE NFVRSSNLKF QDAYNAAGGH NAVFNFPPNG
THSWEYWGAQ LNAMKGDLQS SLGAG
