P0A4V4 (A85C_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Antigen 85-C

Alternative name(s):
Antigen 85 complex C
Short name=85C
Short name=Ag85C
Fibronectin-binding protein C
Mycolyl transferase 85C
EC=2.3.1.-

Gene names

Name:	fbpC
Synonyms:	mpt45
Ordered Locus Names:	Rv0129c, MT0137
ORF Names:	MTCI5.03c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	340 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 AAK44361.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycolipid biosynthetic process Inferred from direct assay. Source: MTBBASE lipid transport Inferred from mutant phenotype. Source: MTBBASE mycolate cell wall layer assembly Inferred from direct assay. Source: MTBBASE response to antibiotic Inferred from expression pattern. Source: MTBBASE
Cellular component	cell wall Inferred from direct assay. Source: MTBBASE extracellular region Inferred from direct assay. Source: MTBBASE
Molecular function	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 – 46

46

Potential

Chain

47 – 340

294

Antigen 85-C

PRO_0000000226

Regions

Region

102 – 112

11

Fibronectin-binding

Sites

Active site

170

1

Acyl-ester intermediate

Active site

274

1

Active site

306

1

Experimental info

Sequence conflict

21

1

L → V in CAA40506. Ref.1

Secondary structure

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340

Helix Strand Turn

Details...

Beta strand

54 – 61

8

Turn

62 – 65

4

Beta strand

66 – 73

8

Beta strand

76 – 82

7

Beta strand

90 – 92

3

Helix

94 – 98

5

Helix

101 – 105

5

Beta strand

108 – 115

8

Beta strand

127 – 129

3

Turn

131 – 134

4

Helix

141 – 146

6

Helix

148 – 157

10

Beta strand

161 – 163

3

Beta strand

165 – 169

5

Helix

172 – 182

11

Turn

184 – 186

3

Beta strand

188 – 194

7

Helix

204 – 214

11

Helix

220 – 224

5

Helix

230 – 234

5

Turn

237 – 240

4

Helix

241 – 246

6

Beta strand

250 – 254

5

Beta strand

259 – 263

5

Helix

268 – 290

23

Beta strand

295 – 299

5

Helix

308 – 327

20

Sequences

	Sequence		Length	Mass (Da)
	P0A4V4 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 2D868C438D697988	FASTA	340	36,771
	10 20 30 40 50 60 MTFFEQVRRL RSAATTLPRR LAIAAMGAVL VYGLVGTFGG PATAGAFSRP GLPVEYLQVP 70 80 90 100 110 120 SASMGRDIKV QFQGGGPHAV YLLDGLRAQD DYNGWDINTP AFEEYYQSGL SVIMPVGGQS 130 140 150 160 170 180 SFYTDWYQPS QSNGQNYTYK WETFLTREMP AWLQANKGVS PTGNAAVGLS MSGGSALILA 190 200 210 220 230 240 AYYPQQFPYA ASLSGFLNPS EGWWPTLIGL AMNDSGGYNA NSMWGPSSDP AWKRNDPMVQ 250 260 270 280 290 300 IPRLVANNTR IWVYCGNGTP SDLGGDNIPA KFLEGLTLRT NQTFRDTYAA DGGRNGVFNF 310 320 330 340 PPNGTHSWPY WNEQLVAMKA DIQHVLNGAT PPAAPAAPAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genes coding for the antigen 85 complexes of Mycobacterium tuberculosis and Mycobacterium bovis BCG are members of a gene family: cloning, sequence determination, and genomic organization of the gene coding for antigen 85-C of M. tuberculosis." Content J., la Cuvellerie A., de Wit L., Vincent-Levy-Frebault V., Ooms J., de Bruyn J. Infect. Immun. 59:3205-3212(1991) [PubMed: 1715324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35801 / TMC 107 / Erdman.
[2]	"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.
[3]	"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.
[4]	"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].
[5]	"Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines." Ronning D.R., Klabunde T., Besra G.S., Vissa V.D., Belisle J.T., Sacchettini J.C. Nat. Struct. Biol. 7:141-146(2000) [PubMed: 10655617] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 47-328.
[6]	"Mycobacterium tuberculosis antigen 85A and 85C structures confirm binding orientation and conserved substrate specificity." Ronning D.R., Vissa V., Besra G.S., Belisle J.T., Sacchettini J.C. J. Biol. Chem. 279:36771-36777(2004) [PubMed: 15192106] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 47-340 IN COMPLEX WITH SUBSTRATE ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X57229 Genomic DNA. Translation: CAA40506.1.
BX842572 Genomic DNA. Translation: CAE55244.1.
AE000516 Genomic DNA. Translation: AAK44361.1. Different initiation.

PIR

D70615.

RefSeq

NP_334547.1. NC_002755.2.
YP_177694.1. NC_000962.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DQY	X-ray	1.83	A	47-328	[»]
1DQZ	X-ray	1.50	A/B	49-328	[»]
1VA5	X-ray	2.02	A/B	47-340	[»]
3HRH	X-ray	2.30	A/B	47-340	[»]

ProteinModelPortal

P0A4V4.

SMR

P0A4V4. Positions 47-328.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000001074; EBMYCP00000001074; EBMYCG00000001074.
EBMYCT00000072923; EBMYCP00000070982; EBMYCG00000072918.

GeneID

886885.
923001.

GenomeReviews

Gene locus MT0137 in contig AE000516_GR.
Gene locus Rv0129c in contig AL123456_GR.

KEGG

mtc:MT0137.
mtu:Rv0129c.

PATRIC

18122028. VBIMycTub22151_0149.

TIGR

MT0137.

Organism-specific databases

TubercuList

Rv0129c.

Phylogenomic databases

GeneTree

EBGT00050000015316.

HOGENOM

HBG564791.

OMA

YLDVFSP.

Enzyme and pathway databases

BioCyc

MetaCyc:RV0129C-MONOMER.

Family and domain databases

InterPro

IPR000801. Esterase_put.
[Graphical view]

Pfam

PF00756. Esterase. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

A85C_MYCTU

Accession

Primary (citable) accession number: P0A4V4
Secondary accession number(s): P31953, P96806

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program