A85C_MYCLE
ID A85C_MYCLE Reviewed; 333 AA.
AC Q05862;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Diacylglycerol acyltransferase/mycolyltransferase Ag85C;
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 C;
DE Short=85C;
DE Short=Ag85C;
DE AltName: Full=Fibronectin-binding protein C;
DE Short=Fbps C;
DE Flags: Precursor;
GN Name=fbpC; Synonyms=fbpC2; OrderedLocusNames=ML2655;
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=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).
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).
CC -!- FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible
CC for the high affinity of mycobacteria to 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=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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
CC {ECO:0000305}.
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DR EMBL; Z21951; CAA79949.1; -; Genomic_DNA.
DR EMBL; M90649; AAA91865.1; -; Genomic_DNA.
DR EMBL; AL583926; CAC32187.1; -; Genomic_DNA.
DR PIR; S32114; S32114.
DR RefSeq; NP_302695.1; NC_002677.1.
DR RefSeq; WP_010909014.1; NC_002677.1.
DR AlphaFoldDB; Q05862; -.
DR SMR; Q05862; -.
DR STRING; 272631.ML2655; -.
DR ESTHER; mycle-a85c; A85-Mycolyl-transferase.
DR EnsemblBacteria; CAC32187; CAC32187; CAC32187.
DR KEGG; mle:ML2655; -.
DR PATRIC; fig|272631.5.peg.5102; -.
DR Leproma; ML2655; -.
DR eggNOG; COG0627; Bacteria.
DR HOGENOM; CLU_026624_3_1_11; -.
DR OMA; WNQQLMA; -.
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; Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..333
FT /note="Diacylglycerol acyltransferase/mycolyltransferase
FT Ag85C"
FT /id="PRO_0000000225"
FT REGION 102..112
FT /note="Fibronectin-binding"
FT ACT_SITE 170
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 274
FT /evidence="ECO:0000250"
FT ACT_SITE 306
FT /evidence="ECO:0000250"
FT BINDING 86..87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276..279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 306..308
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 36392 MW; 50EADF1F731E8EC2 CRC64;
MKFLQQMRKL FGLAAKFPAR LTIAVIGTAL LAGLVGVVGD TAIAVAFSKP GLPVEYLQVP
SPSMGHDIKI QFQGGGQHAV YLLDGLRAQE DYNGWDINTP AFEEYYHSGL SVIMPVGGQS
SFYSNWYQPS QGNGQHYTYK WETFLTQEMP SWLQANKNVL PTGNAAVGLS MSGSSALILA
SYYPQQFPYA ASLSGFLNPS EGWWPTMIGL AMNDSGGYNA NSMWGPSTDP AWKRNDPMVQ
IPRLVANNTR IWVYCGNGAP NELGGDNIPA KFLESLTLST NEIFQNTYAA SGGRNGVFNF
PPNGTHSWPY WNQQLVAMKP DIQQILNGSN NNA
