A85A_MYCTO
ID A85A_MYCTO Reviewed; 338 AA.
AC P9WQP2; D6MJP3; F2GDG3; P0A4V2; P17944; P17996;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
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; Synonyms=mpt44; OrderedLocusNames=MT3911;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 (By 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 {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK48277.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK48277.1; ALT_INIT; Genomic_DNA.
DR PIR; H70887; H70887.
DR RefSeq; WP_003900759.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQP2; -.
DR SMR; P9WQP2; -.
DR EnsemblBacteria; AAK48277; AAK48277; MT3911.
DR GeneID; 45427805; -.
DR KEGG; mtc:MT3911; -.
DR PATRIC; fig|83331.31.peg.4208; -.
DR HOGENOM; CLU_026624_3_1_11; -.
DR Proteomes; UP000001020; 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 InterPro; IPR006311; TAT_signal.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell wall; Cytoplasm; Disulfide bond; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..43
FT /note="Tat-type signal"
FT /evidence="ECO:0000255"
FT CHAIN 44..338
FT /note="Diacylglycerol acyltransferase/mycolyltransferase
FT Ag85A"
FT /id="PRO_0000426741"
FT REGION 101..111
FT /note="Fibronectin-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 273
FT /evidence="ECO:0000250"
FT ACT_SITE 305
FT /evidence="ECO:0000250"
FT BINDING 85..86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275..278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 305..307
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 130..135
FT /evidence="ECO:0000250"
SQ SEQUENCE 338 AA; 35686 MW; 57B1CF95D07D52C0 CRC64;
MQLVDRVRGA VTGMSRRLVV GAVGAALVSG LVGAVGGTAT AGAFSRPGLP VEYLQVPSPS
MGRDIKVQFQ SGGANSPALY LLDGLRAQDD FSGWDINTPA FEWYDQSGLS VVMPVGGQSS
FYSDWYQPAC GKAGCQTYKW ETFLTSELPG WLQANRHVKP TGSAVVGLSM AASSALTLAI
YHPQQFVYAG AMSGLLDPSQ AMGPTLIGLA MGDAGGYKAS DMWGPKEDPA WQRNDPLLNV
GKLIANNTRV WVYCGNGKPS DLGGNNLPAK FLEGFVRTSN IKFQDAYNAG GGHNGVFDFP
DSGTHSWEYW GAQLNAMKPD LQRALGATPN TGPAPQGA
