ProGP190

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ProGP ID ProGP190
Validation Status Characterized
Organism Information
Organism NameMycobacterium tuberculosis H37Rv
Domain Bacteria
Classification Family: Mycobacteriaceae
Suborder: Corynebacterineae
Order: Actinomycetales
Subclass: Actinobacteridae
Class: Actinobacteria
Division or phylum: "Actinobacteria"
Taxonomic ID (NCBI) 1773
Genome Sequence(s)
GenBank BX842573.1
EMBL BX842573
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 NamesodC (Rv0432)
NCBI Gene ID 886358
GenBank Gene Sequence 886358
Protein Information
Protein NameSuperoxide dismutase [Cu-Zn]
UniProtKB/SwissProt ID P0A608
NCBI RefSeq NP_214946.1
EMBL-CDSCAB06572.1
UniProtKB Sequence >sp|P0A608|SODC_MYCTU Superoxide dismutase [Cu-Zn] OS=Mycobacterium tuberculosis GN=sodC PE=1 SV=1 MPKPADHRNHAAVSTSVLSALFLGAGAALLSACSSPQHASTVPGTTPSIWTGSPAPSGLS GHDEESPGAQSLTSTLTAPDGTKVATAKFEFANGYATVTIATTGVGKLTPGFHGLHIHQV GKCEPNSVAPTGGAPGNFLSAGGHYHVPGHTGTPASGDLASLQVRGDGSAMLVTTTDAFT MDDLLSGAKTAIIIHAGADNFANIPPERYVQVNGTPGPDETTLTTGDAGKRVACGVIGSG
Sequence length 240 AA
Subcellular LocationAssociated 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 1PZS
Glycosylation Status
Glycosylation Type O- (Ser/Thr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinT45, T46, S48, T51, S53, S57
Experimentally Validated Glycosite(s ) in Mature ProteinT45, 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 GHDEESPGAQSLTSTLTAPDGTKVATAKFEFANGYATVTIATTGVGKLTPGFHGLHIHQV GKCEPNSVAPTGGAPGNFLSAGGHYHVPGHTGTPASGDLASLQVRGDGSAMLVTTTDAFT MDDLLSGAKTAIIIHAGADNFANIPPERYVQVNGTPGPDETTLTTGDAGKRVACGVIGSG
Sequence Around Glycosites (21 AA) SPQHASTVPGTTPSIWTGSPA
PQHASTVPGTTPSIWTGSPAP
HASTVPGTTPSIWTGSPAPSG
TVPGTTPSIWTGSPAPSGLSG
PGTTPSIWTGSPAPSGLSGHD
PSIWTGSPAPSGLSGHDEESP
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionConcanavalin 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: αMan-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 NameProtein O mannosyltransferase
OST ProGT IDProGT10
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.
Accessory Gene(s)Progt IDProGT10.1
Additional CommentSec-mediated translocation influences the O-mannosylation. Ppm1 does not discriminate between polyprenol substrates with variable chain lengths and saturation of the isoprene units.
Literature
Year of Identification2000
Year of Identification Month Wise2000.5.19
Year of Validation 2009
ReferenceSartain, 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]
Author Sartain, M.J. and Belisle, J.T
Research GroupDepartment of Microbiology, Immunology, and Pathology, Mycobacteria Research Laboratories, Colorado State University, Fort Collins, CO 80523, USA.
Corresponding Author Belisle, J.T
ContactDepartment of Microbiology, Immunology, and Pathology, Mycobacteria Research Laboratories, Colorado State University, Fort Collins, CO 80523, USA.
Reference 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]
Author Scherman, H., Kaur, D., Pham, H., Skovierova, H., Jackson, M. Brennan, P.J.
Research GroupDepartment of Microbiology, Colorado State University, Fort Collins, Colorado 80523-1682, USA
Corresponding Author Brennan, P.J.
ContactDepartment of Microbiology, Colorado State University, Fort Collins, Colorado 80523-1682, USA
ReferenceSpagnolo, L., Toro, I., DOrazio, M., ONeill, 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]
Author Spagnolo, L., Toro, I., DOrazio, M., ONeill, P., Pedersen, J.Z., Carugo, O., Rotilio, G., Battistoni, A. Djinovic-Carugo, K.
Research GroupStructural Biology Laboratory, ELETTRA, Sincrotrone Trieste, Italy.
ContactStructural Biology Laboratory, ELETTRA, Sincrotrone Trieste, Italy.
ReferenceHerrmann, 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]
Author Herrmann, J.L., Delahay, R., Gallagher, A., Robertson, B. Young, D.
Research GroupDepartment of Infectious Diseases and Microbiology, Imperial College School of Medicine, St. Marys Campus, Norfolk Place, W2 1PG, London, UK
Corresponding Author Young, D.
ContactDepartment of Infectious Diseases and Microbiology, Imperial College School of Medicine, St. Marys Campus, Norfolk Place, W2 1PG, London, UK