A85B_MYCIA
ID A85B_MYCIA Reviewed; 330 AA.
AC Q49575; H8IM05; P94938;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 93.
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=OCU_26350;
OS Mycobacterium intracellulare (strain ATCC 13950 / DSM 43223 / JCM 6384 /
OS NCTC 13025 / 3600).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=487521;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600;
RX PubMed=8250904; DOI=10.1006/bbrc.1993.2417;
RA Kitaura H., Ohara N., Matsuo T., Tasaka H., Kobayashi K., Yamada T.;
RT "Cloning, sequencing and expression of the gene for alpha antigen from
RT Mycobacterium intracellulare and use of PCR for the rapid identification of
RT Mycobacterium intracellulare.";
RL Biochem. Biophys. Res. Commun. 196:1466-1473(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600;
RX PubMed=22535933; DOI=10.1128/jb.00295-12;
RA Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare strain ATCC
RT 13950T.";
RL J. Bacteriol. 194:2750-2750(2012).
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 -!- SEQUENCE CAUTION:
CC Sequence=AFC43854.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D16546; BAA03981.1; -; Genomic_DNA.
DR EMBL; D14253; BAA03243.1; -; Genomic_DNA.
DR EMBL; CP003322; AFC43854.1; ALT_INIT; Genomic_DNA.
DR PIR; JN0897; JN0897.
DR RefSeq; WP_009952996.1; NZ_ABIN01000047.1.
DR AlphaFoldDB; Q49575; -.
DR SMR; Q49575; -.
DR STRING; 487521.OCU_26350; -.
DR ESTHER; mycit-a85b; A85-Mycolyl-transferase.
DR EnsemblBacteria; AFC43854; AFC43854; OCU_26350.
DR GeneID; 66745300; -.
DR KEGG; mia:OCU_26350; -.
DR PATRIC; fig|487521.10.peg.2648; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_026624_3_1_11; -.
DR Proteomes; UP000008004; 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..330
FT /note="Diacylglycerol acyltransferase/mycolyltransferase
FT Ag85B"
FT /id="PRO_0000000218"
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"
FT CONFLICT 47..48
FT /note="PV -> EF (in Ref. 1; BAA03243)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="E -> D (in Ref. 1; BAA03243/BAA03981)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="Q -> S (in Ref. 1; BAA03243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 34522 MW; 76FDB684BF4E50D4 CRC64;
MTDLSEKVRA WGRRLVVGAA AAATLPGLIG IAGGAATANA FSRPGLPVEY LQVPSAGMGR
DIKVQFQSGG NGSPAVYLLD GLRAQDDYNG WDINTPAFEW YYQSGLSVIM PVGGQSSFYA
DWYQPACGKA GCSTYKWETF LTSELPQYLA SNKGVKSTGS AAVGISMSGS SAMILAVNHP
NQFVYAGSLS ALLDPSQGMG PSLIGLAMGD AGGYKADAMW GPSSDPAWQR NDPSLQIPAL
VGNNTRLWVY CGNGTPSELG GANMPAEFLE NFVRSSNLKF QDAYNAAGGH NAVFNFNANG
THSWEYWGAQ LNAMKPDLQS ALGASSGGGG
