A85B_MYCBO
ID A85B_MYCBO Reviewed; 325 AA.
AC P0C2T2; A0A1R3XZM1; P12942; X2BIS9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Diacylglycerol acyltransferase/mycolyltransferase Ag85B;
DE Short=DGAT;
DE EC=2.3.1.122;
DE EC=2.3.1.20;
DE AltName: Full=30 kDa extracellular protein;
DE AltName: Full=Acyl-CoA:diacylglycerol acyltransferase;
DE AltName: Full=Antigen 85 complex B;
DE Short=85B;
DE Short=Ag85B;
DE AltName: Full=Extracellular alpha-antigen {ECO:0000303|PubMed:2842287};
DE AltName: Full=Fibronectin-binding protein B;
DE Short=Fbps B;
DE Flags: Precursor;
GN Name=fbpB; OrderedLocusNames=BQ2027_MB1918C;
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 41-70.
RC STRAIN=BCG / Tokyo;
RX PubMed=2842287; DOI=10.1128/jb.170.9.3847-3854.1988;
RA Matsuo K., Yamaguchi R., Yamazaki A., Tasaka H., Yamada T.;
RT "Cloning and expression of the Mycobacterium bovis BCG gene for
RT extracellular alpha antigen.";
RL J. Bacteriol. 170:3847-3854(1988).
RN [2]
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 [3]
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).
RN [4]
RP BINDING TO HUMAN FIBRONECTIN.
RC STRAIN=AN-5;
RX PubMed=8406884; DOI=10.1128/iai.61.11.4828-4834.1993;
RA Peake P., Gooley A., Britton W.J.;
RT "Mechanism of interaction of the 85B secreted protein of Mycobacterium
RT bovis with fibronectin.";
RL Infect. Immun. 61:4828-4834(1993).
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 Mycobacteria to
CC murine alveolar macrophages (AMs) (PubMed:8406884). They also help to
CC maintain the integrity of the cell wall by catalyzing the transfer of
CC mycolic acids to cell wall arabinogalactan and through the synthesis of
CC alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the
CC transfer of a mycoloyl residue from one molecule of alpha,alpha-
CC trehalose monomycolate (TMM) to another TMM, leading to the formation
CC of TDM (By similarity). {ECO:0000250, ECO:0000269|PubMed:8406884}.
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 -!- 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 -!- SUBUNIT: Three regions of this protein interact with the collagen-
CC binding domain of human fibronectin (FN1); binding is saturable and
CC competed by gelatin (which binds to the same domain) but not by heparin
CC (which binds to another domain of fibronectin) (PubMed:8406884).
CC {ECO:0000269|PubMed:8406884}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
CC {ECO:0000305}.
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DR EMBL; M21839; AAA25359.1; -; Genomic_DNA.
DR EMBL; LT708304; SIU00522.1; -; Genomic_DNA.
DR PIR; A32348; A32348.
DR RefSeq; NP_855570.1; NC_002945.3.
DR RefSeq; WP_003409456.1; NC_002945.4.
DR AlphaFoldDB; P0C2T2; -.
DR SMR; P0C2T2; -.
DR ESTHER; myctu-a85b; A85-Mycolyl-transferase.
DR EnsemblBacteria; SIU00522; SIU00522; BQ2027_MB1918C.
DR GeneID; 45425859; -.
DR PATRIC; fig|233413.5.peg.2101; -.
DR OMA; GANMPAE; -.
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 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Disulfide bond; Secreted;
KW Signal; Transferase.
FT SIGNAL 1..40
FT /evidence="ECO:0000269|PubMed:2842287"
FT CHAIN 41..325
FT /note="Diacylglycerol acyltransferase/mycolyltransferase
FT Ag85B"
FT /id="PRO_0000000217"
FT REGION 98..108
FT /note="Fibronectin-binding"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 270
FT /evidence="ECO:0000250"
FT ACT_SITE 302
FT /evidence="ECO:0000250"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272..275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302..304
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 127..132
FT /evidence="ECO:0000250"
FT CONFLICT 140
FT /note="F -> L (in Ref. 1; AAA25359)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..202
FT /note="Missing (in Ref. 1; AAA25359)"
FT /evidence="ECO:0000305"
FT CONFLICT 285..286
FT /note="NA -> KP (in Ref. 1; AAA25359)"
FT /evidence="ECO:0000305"
SQ 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
