P0C5B9 (A85B_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Antigen 85-B

Alternative name(s):
30 kDa extracellular protein
Antigen 85 complex B
Short name=85B
Short name=Ag85B
Extracellular alpha-antigen
Fibronectin-binding protein B
Mycolyl transferase 85B
EC=2.3.1.-

Gene names

Name:	fbpB
Ordered Locus Names:	Rv1886c, MT1934
ORF Names:	MTCY180.32

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Proteins of the antigen 85 complex are responsible for the high affinity of mycobacteria to fibronectin. Possesses a mycolyltransferase activity required for the biogenesis of trehalose dimycolate (cord factor), a dominant structure necessary for maintaining cell wall integrity.
Subcellular location	Secreted.
Miscellaneous	Was identified as a high-confidence drug target.
Sequence similarities	Belongs to the mycobacterial A85 antigen family.
Sequence caution	The sequence AAK46207.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Acyltransferase Transferase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	growth of symbiont in host cell Inferred from mutant phenotype. Source: MTBBASE response to antibiotic Inferred from direct assay. Source: MTBBASE response to host immune response Inferred from expression pattern. Source: MTBBASE
Cellular component	cell wall Inferred from direct assay Ref.2. Source: MTBBASE extracellular region Inferred from direct assay. Source: MTBBASE plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	protein binding Inferred from physical interaction. Source: MTBBASE transferase activity, transferring acyl groups other than amino-acyl groups Inferred from direct assay. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 40

40

Potential

Chain

41 – 325

285

Antigen 85-B

PRO_0000000222

Regions

Region

98 – 108

11

Fibronectin-binding By similarity

Sites

Active site

166

1

Acyl-ester intermediate

Active site

302

1

Probable

Amino acid modifications

Disulfide bond

127 ↔ 132

Ref.6

Secondary structure

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325

Helix Strand Turn

Details...

Beta strand

48 – 55

8

Turn

56 – 59

4

Beta strand

60 – 67

8

Beta strand

75 – 79

5

Beta strand

86 – 88

3

Helix

90 – 94

5

Helix

97 – 101

5

Beta strand

107 – 111

5

Beta strand

126 – 128

3

Beta strand

131 – 133

3

Helix

137 – 142

6

Helix

144 – 153

10

Beta strand

157 – 165

9

Helix

167 – 178

12

Turn

180 – 182

3

Beta strand

183 – 190

8

Helix

200 – 210

11

Helix

216 – 220

5

Helix

227 – 230

4

Turn

233 – 236

4

Helix

237 – 242

6

Beta strand

246 – 250

5

Helix

264 – 286

23

Beta strand

291 – 295

5

Helix

304 – 322

19

Sequences

	Sequence		Length	Mass (Da)
	P0C5B9 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: B993B5442FD5567D	FASTA	325	34,581
	10 20 30 40 50 60 MTDVSRKIRA WGRRLMIGTA AAVVLPGLVG LAGGAATAGA FSRPGLPVEY LQVPSPSMGR 70 80 90 100 110 120 DIKVQFQSGG NNSPAVYLLD GLRAQDDYNG WDINTPAFEW YYQSGLSIVM PVGGQSSFYS 130 140 150 160 170 180 DWYSPACGKA GCQTYKWETF LTSELPQWLS ANRAVKPTGS AAIGLSMAGS SAMILAAYHP 190 200 210 220 230 240 QQFIYAGSLS ALLDPSQGMG PSLIGLAMGD AGGYKAADMW GPSSDPAWER NDPTQQIPKL 250 260 270 280 290 300 VANNTRLWVY CGNGTPNELG GANIPAEFLE NFVRSSNLKF QDAYNAAGGH NAVFNFPPNG 310 320 THSWEYWGAQ LNAMKGDLQS SLGAG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the 85B-protein gene of Mycobacterium bovis BCG and Mycobacterium tuberculosis." de Wit L., Palou M., Content J. DNA Seq. 4:267-270(1994) [PubMed: 7987013] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35801 / TMC 107 / Erdman.
[2]	"Novel insights into the genetics, biochemistry, and immunocytochemistry of the 30-kilodalton major extracellular protein of Mycobacterium tuberculosis." Harth G., Lee B.Y., Wang J., Clemens D.L., Horwitz M.A. Infect. Immun. 64:3038-3047(1996) [PubMed: 8757831] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35801 / TMC 107 / Erdman.
[3]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[4]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[5]	"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis." Raman K., Yeturu K., Chandra N. BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract] Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
[6]	"An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory protein (Antigen 85B), a mycolyl transferase." Anderson D.H., Harth G., Horwitz M.A., Eisenberg D. J. Mol. Biol. 307:671-681(2001) [PubMed: 11254389] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 41-325, DISULFIDE BOND.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X62398 Genomic DNA. Translation: CAA44269.1.
U38939 Genomic DNA. Translation: AAC44294.1.
BX842578 Genomic DNA. Translation: CAB10044.1.
AE000516 Genomic DNA. Translation: AAK46207.1. Different initiation.

PIR

C70516.

RefSeq

NP_216402.1. NC_000962.2.
NP_336393.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F0N	X-ray	1.80	A	41-325	[»]
1F0P	X-ray	1.90	A	41-325	[»]

ProteinModelPortal

P0C5B9.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000001837; EBMYCP00000001837; EBMYCG00000001835.
EBMYCT00000072943; EBMYCP00000071002; EBMYCG00000072938.

GeneID

885785.
923641.

GenomeReviews

Gene locus MT1934 in contig AE000516_GR.
Gene locus Rv1886c in contig AL123456_GR.

KEGG

mtc:MT1934.
mtu:Rv1886c.

PATRIC

18126018. VBIMycTub22151_2121.

TIGR

MT1934.

Organism-specific databases

TubercuList

Rv1886c.

Phylogenomic databases

GeneTree

EBGT00050000015316.

HOGENOM

HBG564791.

OMA

MSGSSAM.

Enzyme and pathway databases

BioCyc

MetaCyc:RV1886C-MONOMER.

Family and domain databases

InterPro

IPR000801. Esterase_put.
[Graphical view]

Pfam

PF00756. Esterase. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

A85B_MYCTU

Accession

Primary (citable) accession number: P0C5B9
Secondary accession number(s): P31952, Q9RMI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program