A85B_MYCS2
ID A85B_MYCS2 Reviewed; 325 AA.
AC A0QU51;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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;
DE AltName: Full=Fibronectin-binding protein B;
DE Short=Fbps B;
DE Flags: Precursor;
GN Name=fbpB; OrderedLocusNames=MSMEG_2078, MSMEI_2033;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=22610443; DOI=10.1074/jbc.m112.346544;
RA Plocinska R., Purushotham G., Sarva K., Vadrevu I.S., Pandeeti E.V.,
RA Arora N., Plocinski P., Madiraju M.V., Rajagopalan M.;
RT "Septal localization of the Mycobacterium tuberculosis MtrB sensor kinase
RT promotes MtrA regulon expression.";
RL J. Biol. Chem. 287:23887-23899(2012).
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. They also help to maintain the integrity of the cell wall
CC by catalyzing the transfer of mycolic acids to cell wall
CC arabinogalactan and through the synthesis of alpha,alpha-trehalose
CC dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl
CC residue from one molecule of alpha,alpha-trehalose monomycolate (TMM)
CC to another TMM, leading to the formation of TDM (By similarity).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Expression depends on the two-component regulatory system
CC MtrA/MtrB. {ECO:0000269|PubMed:22610443}.
CC -!- SIMILARITY: Belongs to the mycobacterial A85 antigen family.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK75892.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38504.1; -; Genomic_DNA.
DR RefSeq; WP_003893447.1; NZ_SIJM01000021.1.
DR RefSeq; YP_886439.1; NC_008596.1.
DR AlphaFoldDB; A0QU51; -.
DR SMR; A0QU51; -.
DR STRING; 246196.MSMEI_2033; -.
DR ESTHER; mycs2-a0qu51; A85-Mycolyl-transferase.
DR PRIDE; A0QU51; -.
DR EnsemblBacteria; ABK75892; ABK75892; MSMEG_2078.
DR EnsemblBacteria; AFP38504; AFP38504; MSMEI_2033.
DR GeneID; 66733506; -.
DR KEGG; msg:MSMEI_2033; -.
DR KEGG; msm:MSMEG_2078; -.
DR PATRIC; fig|246196.19.peg.2054; -.
DR eggNOG; COG0627; Bacteria.
DR OMA; SEAWIRN; -.
DR OrthoDB; 1828423at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 2: Evidence at transcript level;
KW Acyltransferase; Disulfide bond; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..325
FT /note="Diacylglycerol acyltransferase/mycolyltransferase
FT Ag85B"
FT /id="PRO_0000421121"
FT REGION 98..108
FT /note="Fibronectin-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT ACT_SITE 304
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 274..277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 304..306
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 127..132
FT /evidence="ECO:0000250"
SQ SEQUENCE 325 AA; 35190 MW; D0F4EA32E445270B CRC64;
MTFIDKIRGH WARRMTVAAV AALLLPGLVG VVGGSATAGA FSRPGLPVEY LMVPSPSMGR
DIKVQFQSGG PGSHAVYLLD GLRAQDDFNG WDINTNAFEM FLDSGLSVVM PVGGQSSFYS
DWYQPACGNN GCVTYKWETF LTSELPEWLA ANRDVAATGN AAIGLSMAGS AALILAAYHP
DRFIYAGSMS GFLNPSEGWW PFLINISMGD AGGYKANDMW GPTEDPNSAW KRNDPMVQIP
RLVANNTRIW VYCGNGQPNE LGGGDLPATF LEGLTIRTNE TFRDNYIAAG GNNGVFNFPN
NGTHNWAYWG RELQAMVPDL QRVLG
