A1KQD8 (A85A_MYCBP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Diacylglycerol acyltransferase/mycolyltransferase Ag85A
Short name=DGAT
EC=2.3.1.122
EC=2.3.1.20

Alternative name(s):
Acyl-CoA:diacylglycerol acyltransferase
Antigen 85 complex A
Short name=85A
Short name=Ag85A
Fibronectin-binding protein A
Short name=Fbps A

Gene names

Name:	fbpA
Synonyms:	mpt44
Ordered Locus Names:	BCG_3866c

Organism

Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP]

Taxonomic identifier

410289 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis › Mycobacterium bovis BCG

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan, and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. FbpA mediates triacylglycerol (TAG) formation with long-chain acyl-CoA as the acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as the acyl acceptor. It has a preference for C26:0-CoA over C18:1-CoA By similarity.
Catalytic activity	Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol. 2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose + alpha,alpha'-trehalose 6,6'-bismycolate.
Subunit structure	Homodimer By similarity.
Subcellular location	Secreted › cell wall. Cytoplasm.
Sequence similarities	Belongs to the mycobacterial A85 antigen family.

Ontologies

Keywords
Cellular component	Cell wall Cytoplasm Secreted
Domain	Signal
Molecular function	Acyltransferase Transferase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Cellular_component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	diacylglycerol O-acyltransferase activity Inferred from electronic annotation. Source: EC trehalose O-mycolyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 42	42	By similarity
	Chain	43 – 338	296	Diacylglycerol acyltransferase/mycolyltransferase Ag85A		PRO_0000285177
Regions
	Region	85 – 86	2	Substrate binding By similarity
	Region	101 – 111	11	Fibronectin-binding
	Region	275 – 278	4	Substrate binding By similarity
	Region	305 – 307	3	Substrate binding By similarity
Sites
	Active site	169	1	Nucleophile By similarity
	Active site	273	1	By similarity
	Active site	305	1	By similarity
	Binding site	169	1	Substrate By similarity
	Binding site	197	1	Substrate By similarity
	Binding site	282	1	Substrate By similarity
Amino acid modifications
	Disulfide bond	130 ↔ 135		By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1KQD8 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 57B1CF95D07D52C0	FASTA	338	35,686
	10 20 30 40 50 60 MQLVDRVRGA VTGMSRRLVV GAVGAALVSG LVGAVGGTAT AGAFSRPGLP VEYLQVPSPS 70 80 90 100 110 120 MGRDIKVQFQ SGGANSPALY LLDGLRAQDD FSGWDINTPA FEWYDQSGLS VVMPVGGQSS 130 140 150 160 170 180 FYSDWYQPAC GKAGCQTYKW ETFLTSELPG WLQANRHVKP TGSAVVGLSM AASSALTLAI 190 200 210 220 230 240 YHPQQFVYAG AMSGLLDPSQ AMGPTLIGLA MGDAGGYKAS DMWGPKEDPA WQRNDPLLNV 250 260 270 280 290 300 GKLIANNTRV WVYCGNGKPS DLGGNNLPAK FLEGFVRTSN IKFQDAYNAG GGHNGVFDFP 310 320 330 DSGTHSWEYW GAQLNAMKPD LQRALGATPN TGPAPQGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the 32 kDa-protein gene (antigen 85 A) of Mycobacterium bovis BCG." de Wit L., de la Cuvellerie A., Ooms J., Content J. Nucleic Acids Res. 18:3995-3995(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Pasteur 1173P2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X53034 Genomic DNA. Translation: CAA37206.1. AM408590 Genomic DNA. Translation: CAL73856.1.
PIR	S10326.
RefSeq	YP_979945.1. NC_008769.1.
3D structure databases
ProteinModelPortal	A1KQD8.
SMR	A1KQD8. Positions 43-330.
ModBase	Search...
Protein-protein interaction databases
STRING	410289.BCG_3866c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL73856; CAL73856; BCG_3866c.
GeneID	4696523.
KEGG	mbb:BCG_3866c.
PATRIC	18018927. VBIMycBov80988_4198.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0627.
HOGENOM	HOG000049505.
OMA	GGHNAVW.
Enzyme and pathway databases
BioCyc	MBOV410289:GJW7-3917-MONOMER.
Family and domain databases
InterPro	IPR000801. Esterase_put. IPR006311. TAT_signal. [Graphical view]
Pfam	PF00756. Esterase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A85A_MYCBP

Accession

Primary (citable) accession number: A1KQD8
Secondary accession number(s): P0A4V3, P17944, P17996

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program