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P0A618 (MPT53_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Soluble secreted antigen MPT53
Gene names
Name:mpt53
Synonyms:mpb53
Ordered Locus Names:Rv2878c, MT2946
ORF Names:MTCY274.09c
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Disulfide oxidoreductase that catalyzes the oxidation of reduced, unfolded secreted proteins to form disulfide bonds. Despite a weak homology to thioredoxin this cannot serve as a substrate for thioredoxin reductase. Ref.4

Subcellular location

Secreted.

Sequence similarities

Belongs to the thioredoxin family.

Sequence caution

The sequence AAK47271.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRedox-active center
Signal
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from direct assay Ref.4. Source: MTBBASE

   Cellular componentextracellular region

Inferred from direct assay. Source: MTBBASE

   Molecular functionoxidoreductase activity

Inferred from direct assay Ref.4. Source: MTBBASE

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838 Ref.1
Chain39 – 173135Soluble secreted antigen MPT53
PRO_0000034290

Amino acid modifications

Disulfide bond73 ↔ 76Redox-active By similarity

Secondary structure

............................ 173
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A618 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: E67C435C368636D9

FASTA17318,383
        10         20         30         40         50         60 
MSLRLVSPIK AFADGIVAVA IAVVLMFGLA NTPRAVAADE RLQFTATTLS GAPFDGASLQ 

        70         80         90        100        110        120 
GKPAVLWFWT PWCPFCNAEA PSLSQVAAAN PAVTFVGIAT RADVGAMQSF VSKYNLNFTN 

       130        140        150        160        170 
LNDADGVIWA RYNVPWQPAF VFYRADGTST FVNNPTAAMS QDELSGRVAA LTS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, expression and significance of MPT53 for identification of secreted proteins of Mycobacterium tuberculosis."
Wiker H.G., Michell S.L., Hewinson R.G., Spierings E., Nagai S., Harboe M.
Microb. Pathog. 26:207-219(1999) [PubMed: 10089161] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-68.
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis."
Goulding C.W., Apostol M.I., Gleiter S., Parseghian A., Bardwell J., Gennaro M., Eisenberg D.
J. Biol. Chem. 279:3516-3524(2004) [PubMed: 14597624] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 38-173, FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09725 Genomic DNA. Translation: CAA70890.1.
BX842581 Genomic DNA. Translation: CAA98354.1.
AE000516 Genomic DNA. Translation: AAK47271.1. Different initiation.
PIRA70924.
RefSeqNP_217394.1. NC_000962.2.
NP_337457.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LU4X-ray1.12A38-173[»]
ProteinModelPortalP0A618.
SMRP0A618. Positions 38-171.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000003096; EBMYCP00000003096; EBMYCG00000003094.
EBMYCT00000069970; EBMYCP00000068029; EBMYCG00000069965.
GeneID887184.
925317.
GenomeReviewsGene locus MT2946 in contig AE000516_GR.
Gene locus Rv2878c in contig AL123456_GR.
KEGGmtc:MT2946.
mtu:Rv2878c.
PATRIC18128250. VBIMycTub22151_3224.
TIGRMT2946.

Organism-specific databases

TubercuListRv2878c.

Phylogenomic databases

GeneTreeEBGT00050000015916.
HOGENOMHBG565170.
OMAFVNNPTS.
ProtClustDBCLSK792139.

Family and domain databases

InterProIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMPT53_MYCTU
AccessionPrimary (citable) accession number: P0A618
Secondary accession number(s): Q10804
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families