A85A_MYCLE
ID A85A_MYCLE Reviewed; 330 AA.
AC Q05861;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Diacylglycerol acyltransferase/mycolyltransferase Ag85A;
DE Short=DGAT;
DE EC=2.3.1.122;
DE EC=2.3.1.20;
DE AltName: Full=Acyl-CoA:diacylglycerol acyltransferase;
DE AltName: Full=Antigen 85 complex A;
DE Short=85A;
DE Short=Ag85A;
DE AltName: Full=Fibronectin-binding protein A;
DE Short=Fbps A;
DE Flags: Precursor;
GN Name=fbpA; OrderedLocusNames=ML0097;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Thai53;
RX PubMed=7829901; DOI=10.11150/kansenshogakuzasshi1970.68.1330;
RA Yin Y.;
RT "Molecular cloning of alpha antigen like protein gene of Mycobacterium
RT leprae and its over production in Escherichia coli.";
RL Kansenshogaku Zasshi 68:1330-1337(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA de Mendonca-Lima L.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-330.
RX PubMed=8359887; DOI=10.1128/iai.61.9.3642-3647.1993;
RA Rinke de Wit T.F., Bekelie S., Osland A., Wieles B., Janson A.A.M.,
RA Thole J.E.R.;
RT "The Mycobacterium leprae antigen 85 complex gene family: identification of
RT the genes for the 85A, 85C, and related MPT51 proteins.";
RL Infect. Immun. 61:3642-3647(1993).
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.
CC FbpA mediates triacylglycerol (TAG) formation with long-chain acyl-CoA
CC as the acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as
CC the acyl acceptor. It has a preference for C26:0-CoA over C18:1-CoA (By
CC similarity). {ECO:0000250}.
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 -!- 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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Cytoplasm.
CC -!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
CC {ECO:0000305}.
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DR EMBL; D43841; BAA07864.1; -; Genomic_DNA.
DR EMBL; M90648; AAA91864.1; -; Genomic_DNA.
DR EMBL; AL583917; CAC29605.1; -; Genomic_DNA.
DR EMBL; Z21950; CAA79948.1; -; Genomic_DNA.
DR PIR; A86921; A86921.
DR PIR; S32107; S32107.
DR RefSeq; NP_301195.1; NC_002677.1.
DR RefSeq; WP_010907520.1; NC_002677.1.
DR AlphaFoldDB; Q05861; -.
DR SMR; Q05861; -.
DR STRING; 272631.ML0097; -.
DR ESTHER; mycle-a85a; A85-Mycolyl-transferase.
DR PRIDE; Q05861; -.
DR EnsemblBacteria; CAC29605; CAC29605; CAC29605.
DR KEGG; mle:ML0097; -.
DR PATRIC; fig|272631.5.peg.151; -.
DR Leproma; ML0097; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_026624_3_1_11; -.
DR OMA; AWARNDP; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; Cell wall; Cytoplasm; Disulfide bond; Reference proteome;
KW Secreted; Signal; Transferase.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..330
FT /note="Diacylglycerol acyltransferase/mycolyltransferase
FT Ag85A"
FT /id="PRO_0000000213"
FT REGION 100..110
FT /note="Fibronectin-binding"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT ACT_SITE 304
FT /evidence="ECO:0000250"
FT BINDING 84..85
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 274..277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 304..306
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 129..134
FT /evidence="ECO:0000250"
FT CONFLICT 149
FT /note="Q -> E (in Ref. 1; BAA07864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 35411 MW; 170C7C98C98FC5EC CRC64;
MKFVDRFRGA VAGMLRRLVV EAMGVALLSA LIGVVGSAPA EAFSRPGLPV EYLQVPSPSM
GRDIKVQFQN GGANSPALYL LDGLRAQDDF SGWDINTTAF EWYYQSGISV VMPVGGQSSF
YSDWYSPACG KAGCQTYKWE TFLTSELPQY LQSNKQIKPT GSAAVGLSMA GLSALTLAIY
HPDQFIYVGS MSGLLDPSNA MGPSLIGLAM GDAGGYKAAD MWGPSTDPAW KRNDPTVNVG
TLIANNTRIW MYCGNGKPTE LGGNNLPAKL LEGLVRTSNI KFQDGYNAGG GHNAVFNFPD
SGTHSWEYWG EQLNDMKPDL QQYLGATPGA
