ProGP309 (PstS (40 kDa))
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| ProGP ID | ProGP309 (PstS (40 kDa)) |
| Validation Status | Uncharacterized |
| Organism Information | |
| Organism Name | Streptomyces coelicolor J1929 |
| Domain | Bacteria |
| Classification | Phylum : Actinobacteria Class : Actinomycetia Orders : Streptomycetales Family : Streptomycetaceae Genus : Streptomyces Species : coelicolor Strain : J1929 |
| Taxonomic ID (NCBI) | 1902 |
| Genome Information | |
| GenBank | AL939119.1 |
| EMBL | AL939119 |
| Organism Additional Information | Streptomyces coelicolor is a filamentous bacterium responsible for the production of most natural antibiotics for human and veterinary use. |
| Gene Information | |
| Gene Name | pstS (SCO4142) |
| NCBI Gene ID | 1099582 |
| GenBank Gene Sequence | NC_003888.3 |
| Protein Information | |
| Protein Name | PstS (40 kDa) |
| UniProtKB/SwissProt ID | Q9KZV9 |
| NCBI RefSeq | WP_003974827.1 |
| EMBL-CDS | CAB88475.1 |
| UniProtKB Sequence | >tr|Q9KZV9|Q9KZV9_STRCO Phosphate-binding protein OS=Streptomyces coelicolor GN=SCO4142 PE=4 SV=1 MNRRALALGALAVSGALALTACGSDDTGGNSGSDSSSAAANSNIKCDDAKGQLQASGSSA QKNAIDAWVKQYVAACNGVQINYNPTGSGAGITAFTQGQTAFAGSDSALKPDEIEASKKV CKDGQAIDLPMVGGPIAVGFNVTGVDSLVLDAPTMAKIFDSKITNWNDEAIKKLNPDAKL PDLKIQAFHRSDESGTTDNFTKYLKAAAPDDWKYEGGKSWEAKGGQSAQGSSGLAGQVKQ TPGAISYFELSYAKDGIKTVDVKTAAAEPVKATVENATAAIGAAKVVGTGKDLALELDYT PDAAGAYPLVLVTYEIACDKGNKADTLPATKSFLNYMASEDGQGLLADAGYAPMPTEIIT KVRETISGLS |
| Sequence length | 370 AA |
| Subcellular Location | Secreted |
| Function | Phosphate binding protein involved in high affinity phosphate uptake. |
| Glycosylation Status | |
| Technique(s) used for Glycosylation Detection | Pro-Q Emerald Glycoprotein staining (that uses periodate oxidation) and Con-A sepharose affinity chromatography. |
| Glycan Information | |
| Glycan Annotation | Trihexose (mannose). |
| Protein Glycosylation linked (PGL) gene(s) | |
| OST ProGT ID | ProGT35 |
| Accessory Gene(s)Progt ID | ProGT35.1 |
| Additional Comment | Both Pmt (putative protein O-mannosyltransferase) and Ppm1 (polyprenol phosphate mannose synthase) are required for glycosylation. Ppm1 transfers mannose to endogenous polyprenol phosphate in membrane preparations. Ppm1 catalyzes mannose transfer. |
| Literature | |
| Year of Identification | 2009 |
| Year of Identification Month Wise | 2009.3 |
| Reference | Wehmeier, S., Varghese, A.S., Gurcha, S.S., Tissot, B., Panico, M., Hitchen, P., Morris, H.R., Besra, G.S., Dell, A. and Smith, M.C.M., 2009. Glycosylation of the phosphate binding protein, PstS, in Streptomyces coelicolor by a pathway that resembles protein O‐mannosylation in eukaryotes. Molecular microbiology, 71(2), pp.421-433. |
| Corresponding Author | M. C. M. Smith |
| Contact | School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Aberdeen AB25 2ZD, UK |