ID   A85C_MYCBO              Reviewed;         340 AA.
AC   P0A4V5; A0A1R3XUE5; P31953; P96806; X2BE42;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=mpt45; OrderedLocusNames=BQ2027_MB0134C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIT98556.1; -; Genomic_DNA.
DR   RefSeq; NP_853801.1; NC_002945.3.
DR   RefSeq; WP_003400908.1; NC_002945.4.
DR   AlphaFoldDB; P0A4V5; -.
DR   SMR; P0A4V5; -.
DR   ESTHER; myctu-a85c; A85-Mycolyl-transferase.
DR   GeneID; 45424095; -.
DR   PATRIC; fig|233413.5.peg.151; -.
DR   OMA; WNQQLMA; -.
DR   Proteomes; UP000001419; 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; Secreted; Signal; Transferase.
FT   SIGNAL          1..45
FT                   /evidence="ECO:0000255"
FT   CHAIN           46..340
FT                   /note="Diacylglycerol acyltransferase/mycolyltransferase
FT                   Ag85C"
FT                   /id="PRO_0000000224"
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   340 AA;  36771 MW;  2D868C438D697988 CRC64;
     MTFFEQVRRL RSAATTLPRR LAIAAMGAVL VYGLVGTFGG PATAGAFSRP GLPVEYLQVP
     SASMGRDIKV QFQGGGPHAV YLLDGLRAQD DYNGWDINTP AFEEYYQSGL SVIMPVGGQS
     SFYTDWYQPS QSNGQNYTYK WETFLTREMP AWLQANKGVS PTGNAAVGLS MSGGSALILA
     AYYPQQFPYA ASLSGFLNPS EGWWPTLIGL AMNDSGGYNA NSMWGPSSDP AWKRNDPMVQ
     IPRLVANNTR IWVYCGNGTP SDLGGDNIPA KFLEGLTLRT NQTFRDTYAA DGGRNGVFNF
     PPNGTHSWPY WNEQLVAMKA DIQHVLNGAT PPAAPAAPAA