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Diacylglycerol acyltransferase/mycolyltransferase Ag85B (DGAT) (EC 2.3.1.122) (EC 2.3.1.20) (30 kDa extracellular protein) (Acyl-CoA:diacylglycerol acyltransferase) (Antigen 85 complex B) (85B) (Ag85B) (Extracellular alpha-antigen) (Fibronectin-binding protein B) (Fbps B)

 A85B_MYCTU              Reviewed;         325 AA.
P9WQP1; D6MJP5; F2GHQ8; P0C5B9; P31952; Q9RMI0;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
12-SEP-2018, entry version 27.
RecName: Full=Diacylglycerol acyltransferase/mycolyltransferase Ag85B;
Short=DGAT;
EC=2.3.1.122;
EC=2.3.1.20;
AltName: Full=30 kDa extracellular protein;
AltName: Full=Acyl-CoA:diacylglycerol acyltransferase;
AltName: Full=Antigen 85 complex B;
Short=85B;
Short=Ag85B;
AltName: Full=Extracellular alpha-antigen;
AltName: Full=Fibronectin-binding protein B;
Short=Fbps B;
Flags: Precursor;
Name=fbpB; OrderedLocusNames=Rv1886c; ORFNames=MTCY180.32;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=7987013;
de Wit L., Palou M., Content J.;
"Nucleotide sequence of the 85B-protein gene of Mycobacterium bovis
BCG and Mycobacterium tuberculosis.";
DNA Seq. 4:267-270(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=8757831;
Harth G., Lee B.Y., Wang J., Clemens D.L., Horwitz M.A.;
"Novel insights into the genetics, biochemistry, and
immunocytochemistry of the 30-kilodalton major extracellular protein
of Mycobacterium tuberculosis.";
Infect. Immun. 64:3038-3047(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BJ10;
PubMed=20223296; DOI=10.1016/j.meegid.2010.03.003;
Chuang P.C., Chen Y.M., Chen H.Y., Jou R.;
"Single nucleotide polymorphisms in cell wall biosynthesis-associated
genes and phylogeny of Mycobacterium tuberculosis lineages.";
Infect. Genet. Evol. 10:459-466(2010).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[5]
PROTEIN SEQUENCE OF 41-50.
PubMed=2403534;
Wiker H.G., Sletten K., Nagai S., Harboe M.;
"Evidence for three separate genes encoding the proteins of the
mycobacterial antigen 85 complex.";
Infect. Immun. 58:272-274(1990).
[6]
FUNCTION IN THE FIBRONECTIN BINDING.
PubMed=3141278;
Abou-Zeid C., Ratliff T.L., Wiker H.G., Harboe M., Bennedsen J.,
Rook G.A.;
"Characterization of fibronectin-binding antigens released by
Mycobacterium tuberculosis and Mycobacterium bovis BCG.";
Infect. Immun. 56:3046-3051(1988).
[7]
FUNCTION AS A MYCOLYLTRANSFERASE, AND NOMENCLATURE.
PubMed=9162010; DOI=10.1126/science.276.5317.1420;
Belisle J.T., Vissa V.D., Sievert T., Takayama K., Brennan P.J.,
Besra G.S.;
"Role of the major antigen of Mycobacterium tuberculosis in cell wall
biogenesis.";
Science 276:1420-1422(1997).
[8]
FUNCTION AS A MYCOLYLTRANSFERASE, AND DISRUPTION PHENOTYPE.
PubMed=12010501; DOI=10.1046/j.1365-2958.2002.02953.x;
Puech V., Guilhot C., Perez E., Tropis M., Armitige L.Y., Gicquel B.,
Daffe M.;
"Evidence for a partial redundancy of the fibronectin-binding proteins
for the transfer of mycoloyl residues onto the cell wall
arabinogalactan termini of Mycobacterium tuberculosis.";
Mol. Microbiol. 44:1109-1122(2002).
[9]
IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
PubMed=19099550; DOI=10.1186/1752-0509-2-109;
Raman K., Yeturu K., Chandra N.;
"targetTB: a target identification pipeline for Mycobacterium
tuberculosis through an interactome, reactome and genome-scale
structural analysis.";
BMC Syst. Biol. 2:109-109(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[11]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 41-325 IN COMPLEX WITH
SUBSTRATE, ACTIVE SITE, REACTION MECHANISM, AND DISULFIDE BOND.
PubMed=11254389; DOI=10.1006/jmbi.2001.4461;
Anderson D.H., Harth G., Horwitz M.A., Eisenberg D.;
"An interfacial mechanism and a class of inhibitors inferred from two
crystal structures of the Mycobacterium tuberculosis 30 kDa major
secretory protein (Antigen 85B), a mycolyl transferase.";
J. Mol. Biol. 307:671-681(2001).
-!- FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are
responsible for the high affinity of mycobacteria for fibronectin,
a large adhesive glycoprotein, which facilitates the attachment of
M.tuberculosis to murine alveolar macrophages (AMs). They also
help to maintain the integrity of the cell wall by catalyzing the
transfer of mycolic acids to cell wall arabinogalactan and through
the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord
factor). They catalyze the transfer of a mycoloyl residue from one
molecule of alpha,alpha-trehalose monomycolate (TMM) to another
TMM, leading to the formation of TDM.
{ECO:0000269|PubMed:12010501, ECO:0000269|PubMed:3141278,
ECO:0000269|PubMed:9162010}.
-!- CATALYTIC ACTIVITY: 2 alpha,alpha'-trehalose 6-mycolate =
alpha,alpha'-trehalose + alpha,alpha'-trehalose 6,6'-bismycolate.
-!- CATALYTIC ACTIVITY: Acyl-CoA + 1,2-diacylglycerol = CoA +
triacylglycerol.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene produce normally
mycoloylated cell wall components. {ECO:0000269|PubMed:12010501}.
-!- MISCELLANEOUS: Was identified as a high-confidence drug target.
-!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; X62398; CAA44269.1; -; Genomic_DNA.
EMBL; U38939; AAC44294.1; -; Genomic_DNA.
EMBL; GQ150316; ADD50054.1; -; Genomic_DNA.
EMBL; AL123456; CCP44652.1; -; Genomic_DNA.
PIR; C70516; C70516.
RefSeq; NP_216402.1; NC_000962.3.
RefSeq; WP_003409456.1; NZ_KK339370.1.
PDB; 1F0N; X-ray; 1.80 A; A=41-325.
PDB; 1F0P; X-ray; 1.90 A; A=41-325.
PDB; 5TRZ; X-ray; 2.25 A; P/Q=102-110.
PDB; 5TS1; X-ray; 2.30 A; P/Q/R/S=101-109.
PDBsum; 1F0N; -.
PDBsum; 1F0P; -.
PDBsum; 5TRZ; -.
PDBsum; 5TS1; -.
ProteinModelPortal; P9WQP1; -.
SMR; P9WQP1; -.
STRING; 83332.Rv1886c; -.
ESTHER; myctu-a85b; A85-Mycolyl-transferase.
MoonProt; P9WQP1; -.
PaxDb; P9WQP1; -.
EnsemblBacteria; CCP44652; CCP44652; Rv1886c.
GeneID; 885785; -.
KEGG; mtu:Rv1886c; -.
TubercuList; Rv1886c; -.
eggNOG; COG0627; LUCA.
KO; K18851; -.
OMA; YNIDAMA; -.
PhylomeDB; P9WQP1; -.
BioCyc; MetaCyc:G185E-6081-MONOMER; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0001968; F:fibronectin binding; IDA:CAFA.
GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IDA:MTBBASE.
GO; GO:0050348; F:trehalose O-mycolyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0035375; F:zymogen binding; IPI:CAFA.
GO; GO:0044119; P:growth of symbiont in host cell; IMP:MTBBASE.
GO; GO:0044044; P:interaction with host via substance in symbiont surface; IDA:CAFA.
GO; GO:0010756; P:positive regulation of plasminogen activation; IDA:CAFA.
GO; GO:0040009; P:regulation of growth rate; IMP:UniProtKB.
GO; GO:0046677; P:response to antibiotic; IDA:MTBBASE.
GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR000801; Esterase_put.
Pfam; PF00756; Esterase; 1.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Complete proteome;
Direct protein sequencing; Disulfide bond; Reference proteome;
Secreted; Signal; Transferase.
SIGNAL 1 40 {ECO:0000255}.
CHAIN 41 325 Diacylglycerol
acyltransferase/mycolyltransferase Ag85B.
/FTId=PRO_0000000222.
REGION 82 83 Substrate binding.
REGION 98 108 Fibronectin-binding. {ECO:0000250}.
REGION 272 275 Substrate binding.
REGION 302 304 Substrate binding.
ACT_SITE 166 166 Nucleophile.
{ECO:0000305|PubMed:11254389}.
ACT_SITE 270 270 {ECO:0000305|PubMed:11254389}.
ACT_SITE 302 302 {ECO:0000305|PubMed:11254389}.
BINDING 166 166 Substrate. {ECO:0000269|PubMed:11254389}.
BINDING 194 194 Substrate. {ECO:0000269|PubMed:11254389}.
BINDING 279 279 Substrate. {ECO:0000269|PubMed:11254389}.
DISULFID 127 132 {ECO:0000269|PubMed:11254389}.
STRAND 48 55 {ECO:0000244|PDB:1F0N}.
TURN 56 59 {ECO:0000244|PDB:1F0N}.
STRAND 60 67 {ECO:0000244|PDB:1F0N}.
STRAND 75 79 {ECO:0000244|PDB:1F0N}.
STRAND 86 88 {ECO:0000244|PDB:1F0N}.
HELIX 90 94 {ECO:0000244|PDB:1F0N}.
HELIX 97 101 {ECO:0000244|PDB:1F0N}.
STRAND 107 111 {ECO:0000244|PDB:1F0N}.
STRAND 126 128 {ECO:0000244|PDB:1F0N}.
STRAND 131 133 {ECO:0000244|PDB:1F0N}.
HELIX 137 142 {ECO:0000244|PDB:1F0N}.
HELIX 144 153 {ECO:0000244|PDB:1F0N}.
STRAND 157 165 {ECO:0000244|PDB:1F0N}.
HELIX 167 178 {ECO:0000244|PDB:1F0N}.
TURN 180 182 {ECO:0000244|PDB:1F0N}.
STRAND 183 190 {ECO:0000244|PDB:1F0N}.
HELIX 200 210 {ECO:0000244|PDB:1F0N}.
HELIX 216 220 {ECO:0000244|PDB:1F0N}.
HELIX 227 230 {ECO:0000244|PDB:1F0N}.
TURN 233 236 {ECO:0000244|PDB:1F0N}.
HELIX 237 242 {ECO:0000244|PDB:1F0N}.
STRAND 246 250 {ECO:0000244|PDB:1F0N}.
HELIX 264 286 {ECO:0000244|PDB:1F0N}.
STRAND 291 295 {ECO:0000244|PDB:1F0N}.
HELIX 304 322 {ECO:0000244|PDB:1F0N}.
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


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