ProGP189 (Superoxide dismutase [Cu-Zn])

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ProGP ID ProGP189 (Superoxide dismutase [Cu-Zn])
Validation Status Characterized
Organism Information
Organism NameMycobacterium tuberculosis H37Rv
Domain Bacteria
Classification Phylum : Actinobacteria
Class : Actinomycetia
Orders : Corynebacteriales
Family : Mycobacteriaceae
Genus : Mycobacterium
Species : tuberculosis
Strain : H37Rv
Taxonomic ID (NCBI) 1773
Genome Information
GenBank AL123456.3
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 NC_000962
Protein Information
Protein NameSuperoxide dismutase [Cu-Zn]
UniProtKB/SwissProt ID P9WGE9
NCBI RefSeq NP_214946.1
EMBL-CDSCCP43163
UniProtKB Sequence >sp|P9WGE9|SODC_MYCTU Superoxide dismutase [Cu-Zn] OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 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
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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 IDProGT12
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(1), pp.38-51.
Corresponding Author John T Belisle
ContactDepartment of Microbiology, Immunology, and Pathology, Mycobacteria Research Laboratories, Colorado State University, Fort Collins, CO 80523, USA.
ReferenceScherman, H., Kaur, D., Pham, H., Škovierová, H., Jackson, M. and Brennan, P.J., 2009. Identification of a polyprenylphosphomannosyl synthase involved in the synthesis of mycobacterial mannosides. Journal of bacteriology, 191(21), pp.6769-6772.
Corresponding Author Hataichanok Scherman
ContactDepartment of Microbiology, Colorado State University, Fort Collins, Colorado 80523-1682, USA.
ReferenceSpagnolo, L., Törö, I., D'orazio, M., O'Neill, P., Pedersen, J.Z., Carugo, O., Rotilio, G., Battistoni, A. and Djinović-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. Journal of Biological Chemistry, 279(32), pp.33447-33455.
Corresponding Author Kristina Djinovi?-Carugo
Andrea Battistoni
ContactStructural Biology Laboratory, ELETTRA, Sincrotrone Trieste, Italy.
Department of Biology, University of Rome Tor Vergata and Istituto Nazionale per la Fisica della Materia, Via della Ricerca Scientifica, 00133 Rome, 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 Letters, 473(3), pp.358-362.
Corresponding Author Jean Louis Herrmann
ContactDepartment of Infectious Diseases and Microbiology, Imperial College School of Medicine, St. Mary's Campus, Norfolk Place, W2 1PG, London, UK. jlh@chu-stlouis.fr