Total Record - 1

Print this rrecord

 
ProGlyProt ID
BC154
Organism Information
Organism Name
Mycobacterium tuberculosis H37Rv
Domain
Bacteria
Classification
Family: Mycobacteriaceae
Suborder: Corynebacterineae
Order: Actinomycetales
Subclass: Actinobacteridae
Class: Actinobacteria
Division or phylum: "Actinobacteria"
Taxonomic ID (NCBI)
 
 
Genome Sequence(s)
GenBank
EMBL
Organism Additional Information
It is the causative agent of human tuberculosis. The pathogenesis is influenced by its lipoglycans and glycolipids (having a wide range of immunomodulatory activities), and a variety of its virulence factors and antigens.
 
 
Gene Information
Gene Name
sodC (Rv0432)
NCBI Gene ID
GenBank Gene Sequence
 
 
Protein Information
Protein Name
Superoxide dismutase [Cu-Zn]
UniProtKB/SwissProt ID
NCBI RefSeq
EMBL-CDS
UniProtKB Sequence
Sequence length
240 AA
Subcellular Location
Associated with cell envelope (or membrane)
Function
One of two Mtb superoxide dismutases (SODs) and is a membrane-associated lipoprotein of the Cu, Zn-dependent SOD family. Contributes to the survival of Mtb in activated macrophages, suggesting a role in the defense against the oxidative burst produced in vivo. EC= 1.15.1.1
 
 
Protein Structure
PDB ID
 
 
Glycosylation Status
Glycosylation Type
O (Ser/Thr) linked
Experimentally Validated Glycosite(s) in Full Length Protein
T45, T46, S48, T51, S53, S57
Experimentally Validated Glycosite(s ) in Mature Protein
T45, T46, S48, T51, S53, S57
Glycosite(s) Annotated Protein Sequence
>sp|P0A608|SODC_MYCTU Superoxide dismutase [Cu-Zn] OS=Mycobacterium tuberculosis
GN=sodC PE=1 SV=1 MPKPADHRNHAAVSTSVLSALFLGAGAALLSACSSPQHASTVPGT*(45)T*(46
)
PS*(48)IWT*(51)GS*(53)PAPS*(57)GLS GHDEESPGAQSLTSTLTAPDGTKVATAKFE
FANGYATVTIATTGVGKLTPGFHGLHIHQV GKCEPNSVAPTGGAPGNFLSAGGHYHVPGHTGTPASGDLASLQV
RGDGSAMLVTTTDAFT MDDLLSGAKTAIIIHAGADNFANIPPERYVQVNGTPGPDETTLTTGDAGKRVACGVIGSG
Sequence Around Glycosites (21 AA)
SPQHASTVPGTTPSIWTGSPA
PQHASTVPGTTPSIWTGSPAP
HASTVPGTTPSIWTGSPAPSG
TVPGTTPSIWTGSPAPSGLSG
PGTTPSIWTGSPAPSGLSGHD
PSIWTGSPAPSGLSGHDEESP
Glycosite Sequence Logo
Glycosite Sequence Logo
Technique(s) used for Glycosylation Detection
Concanavalin A (ConA)-binding
Technique(s) used for Glycosylated Residue(s) Detection
LC-ESI-MS/MS (liquid chromatography-electrospray-ionization-tandem mass spectrometry) and site-directed mutagenesis (Thr to Ala)
Protein Glycosylation- Implication
Glycosylation of this enzyme modulates proteolytic cleavage within the unstructured SodC N-terminus and influences SodC localization and stability.
 
 
Glycan Information
Glycan Annotation
Linkages: ╬▒Man-Thr/Ser.
Variable modifications with one to three hexose (mannose) units on each site. The total number of hexose units present is in the range of 6-10. The most dominant SodC glycoform was modified with nine hexose units.
Technique(s) used for Glycan Identification
ESI-MS/MS (electrospray ionization tandem mass spctrometry)
 
 
Protein Glycosylation linked (PGL) gene(s)
OST Gene Name
pmt/rv1002c
OST NCBI Gene ID
OST GenBank Gene Sequence
OST Protein Name
Protein O mannosyltransferase
OST UniProtKB/ SwissProt ID
OST NCBI RefSeq
OST EMBL-CDS
OST UniProtKB Sequence
OST EC Number (BRENDA)
OST Genome Context
Characterized Accessory Gene(s)
Polyprenol-phosphate-mannose (PPM) synthase, Ppm1, is present. A second type of Ppm synthase (Rv3779 gene product) exclusive to slow-growing mycobacteria, is a membrane glycosyltransferase. It mannosylates polyprenyl-phosphates directly from GDP-mannose.
PGL Additional Links
 
 
Literature
Reference(s)
1) Sartain, M.J. and Belisle, J.T. (2009) N-Terminal clustering of the O-glycosylation sites in the Mycobacterium tuberculosis lipoprotein SodC. Glycobiology, 19, 38-51. [PubMed: 18842962]
2) Scherman, H., Kaur, D., Pham, H., Skovierova, H., Jackson, M. and Brennan, P.J. (2009) Identification of a polyprenylphosphomannosyl synthase involved in the synthesis of mycobacterial mannosides. J Bacteriol, 191, 6769-6772. [PubMed: 19717608]
3) Spagnolo, L., Toro, I., D'Orazio, M., O'Neill, P., Pedersen, J.Z., Carugo, O., Rotilio, G., Battistoni, A. and Djinovic-Carugo, K. (2004) Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site. J Biol Chem, 279, 33447-33455. [PubMed: 15155722]
3) Herrmann, J.L., Delahay, R., Gallagher, A., Robertson, B. and Young, D. (2000) Analysis of post-translational modification of mycobacterial proteins using a cassette expression system. FEBS Lett, 473, 358-362. [PubMed: 10818240]
Additional Comments
Sec-mediated translocation influences the O-mannosylation. Ppm1 does not discriminate between polyprenol substrates with variable chain lengths and saturation of the isoprene units.
Year of Identification
2000
Year of Validation
2009
 
 
Copyright @ 2011 IMTECH
This site is best viewed in Mozilla Firefox, Internet Explorer 6 and above at screen resolution of 1024 x 768 and above.