A85B_MYCLE
ID A85B_MYCLE Reviewed; 327 AA.
AC P31951; Q9RIA5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 119.
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=ML2028; ORFNames=MLCB561.03c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1945858; DOI=10.1093/nar/19.20.5789;
RA de Mendonca-Lima L., Content J., van Heuverswyn H., Degrave W.;
RT "Nucleotide sequence of the gene coding for the 85-B antigen of
RT Mycobacterium leprae.";
RL Nucleic Acids Res. 19:5789-5789(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; X60934; CAA43269.1; -; Genomic_DNA.
DR EMBL; AL049571; CAB40285.1; -; Genomic_DNA.
DR EMBL; AL583924; CAC30983.1; -; Genomic_DNA.
DR PIR; G87162; G87162.
DR PIR; S20038; S20038.
DR PIR; S34434; S34434.
DR RefSeq; NP_302359.1; NC_002677.1.
DR RefSeq; WP_010908679.1; NC_002677.1.
DR AlphaFoldDB; P31951; -.
DR SMR; P31951; -.
DR STRING; 272631.ML2028; -.
DR ESTHER; mycle-a85b; A85-Mycolyl-transferase.
DR EnsemblBacteria; CAC30983; CAC30983; CAC30983.
DR KEGG; mle:ML2028; -.
DR PATRIC; fig|272631.5.peg.3822; -.
DR Leproma; ML2028; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_026624_3_1_11; -.
DR OMA; GANMPAE; -.
DR Proteomes; UP000000806; 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; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..327
FT /note="Diacylglycerol acyltransferase/mycolyltransferase
FT Ag85B"
FT /id="PRO_0000000220"
FT REGION 96..106
FT /note="Fibronectin-binding"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /evidence="ECO:0000250"
FT ACT_SITE 300
FT /evidence="ECO:0000250"
FT BINDING 80..81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300..302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 125..130
FT /evidence="ECO:0000250"
FT CONFLICT 59
FT /note="S -> T (in Ref. 1; CAA43269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 34807 MW; 2B0EB9B37AAF985C CRC64;
MIDVSGKIRA WGRWLLVGAA ATLPSLISLA GGAATASAFS RPGLPVEYLQ VPSEAMGRSI
KVQFQNGGNG SPAVYLLDGL RAQDDYNGWD INTSAFEWYY QSGLSVVMPV GGQSSFYSDW
YSPACGKAGC TTYKWETFLT SELPKWLSAN RSVKSTGSAV VGLSMAGSSA LILAAYHPDQ
FIYAGSLSAL MDSSQGIEPQ LIGLAMGDAG GYKAADMWGP PNDPAWQRND PILQAGKLVA
NNTHLWVYCG NGTPSELGGT NVPAEFLENF VHGSNLKFQD AYNGAGGHNA VFNLNADGTH
SWEYWGAQLN AMKPDLQNTL MAVPRSG
