A85C_MYCTO
ID A85C_MYCTO Reviewed; 340 AA.
AC P9WQN8; L0T2K1; P0A4V4; P31953; P96806;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
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=MT0137;
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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK44361.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK44361.1; ALT_INIT; Genomic_DNA.
DR PIR; D70615; D70615.
DR RefSeq; WP_003400908.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQN8; -.
DR SMR; P9WQN8; -.
DR ESTHER; myctu-a85c; A85-Mycolyl-transferase.
DR EnsemblBacteria; AAK44361; AAK44361; MT0137.
DR GeneID; 45424095; -.
DR KEGG; mtc:MT0137; -.
DR PATRIC; fig|83331.31.peg.148; -.
DR HOGENOM; CLU_026624_3_1_11; -.
DR BRENDA; 2.3.1.122; 3445.
DR Proteomes; UP000001020; 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_0000426743"
FT REGION 102..112
FT /note="Fibronectin-binding"
FT /evidence="ECO:0000250"
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 283
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
