| Organism Information |
| Organism Name | Streptomyces coelicolor strain J1929 |
| Clinical Implication | Plant pathogens |
| Domain | Bacteria |
| Phylum | Actinobacteria |
| Classification | Family: Streptomycetaceae
Suborder: Streptomycineae
Order: Actinomycetales
Subclass: Actinobacteridae
Class: Actinobacteria
Division or phylum: "Actinobacteria" |
| Taxonomic ID (NCBI) | 100226 |
| Genome Information |
| Gene Bank | AL939115.1 |
| EMBL | AL939115.1 |
| Gene Information |
| Gene Name | SCO3154 |
| NCBI Gene ID | 1098588 |
| Protein information |
| Protein Name | Pmt |
| UniProtKB/ SwissProt ID | Q9RKD3 |
| NCBI Ref Seq | NP_627370.1 |
| UniProtKB Sequence | >tr|Q9RKD3|Q9RKD3_STRCO Putative integral membrane protein OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) GN=SCO3154 PE=4 SV=1
MHSAVPYDGAVTSTASSTDTLHDQAPHDERPTWQQRLRRFGYPAGPATGDVRDRLVPPYT
SPSPRLWAFLGVSKPLTDRMIRWSAWGGPLLVALFAGVLRFWNLGSPKAVIFDETYYAKD
AWALIHRGFEVNWDKNANDLILNSGGDVPIPTDAAYVVHPPVGKYIIGLGELLFGFDPFG
WRFMTALLGTLSVLLLCRIGRRLFRSTFLGCLAGALMALDGLHFVMSRTALLDSVLMFFV
LAAFGCLVVDRDKARSRLAAALPVDEDGRVRPDAHVAETLRLGWRPWRLAAGLMLGLAAA
TKWNGLYIMAAFCVMAVLWDVGSRRVAGAHRPYRAVLRHDLGWAFLSTVPVALATYLLSW
LGWILSPSDGTGGYYRDWATKDGANSSWSWLFPDWWRSLWHYETQVLEFHTHLTSPHTYQ
SNPWSWIVLGRPVSYFYESPSAGSDGCPVDAGEKCAREVLALGTPLLWWVGCFALLYVLW
RWLFRRDWRAGAIACGVAAGYLPWFMYQERTIFLFYAVVFLPFLCLAVAMLLGAIIGRPG
CTDTRRVAGATGAGVLVLLIAWNFIYFWPLYTGTAIPMEEWRARMWLDTWV
|
| EMBL CDS | CAB59650.1 |
| Sequence length | 591 AA |
| Subcellular Location | Membrane |
| Function in Native Organism | 1) Pmt transfer the mannose sugar to PstS Protein.
2) Streptomyces coelicolor protein mannosyltransferase (Pmt) is required for glycosylation of the Apa protein. |
| String | 100226.SCO3154. |
| Additional Information | 1) PMTs are functional orthologues of the PMTs in fungi and POMTs in humans.
2) Streptomyces coelicolor Ppm and Pmt also modify the Apa protein of M.tb. |
| Glycosyltransferase Information |
| Glycosylation Type | O- (Ser/Thr) linked |
| CAZY Family | GT39 |
| EC Number (BRENDA) | 2.4.1.- |
| Mechanism of Glycan Transfer | Sequential |
| Donor Type | Nucleotide activated sugars |
| Donor Specificity | GDP-Mannose |
| Accessory GT ID | ProGT35.1 |
| Glycan Information |
| Glycan transferred | Trihexose |
| Method of Glycan Indentification | Nano-LC-ESI-MS/MS |
| Experimental_strategies | In vitro and In vivo  |
| Acceptor Subtrate Information |
| Acceptor Substrate name | PstS |
| ProGPdb ID | ProGP309 |
| Acceptor Substrate name | Apa |
| ProGPdb ID | ProGP51 |
| Litrature |
| Year Of Validation | 2009Â |
| Reference | Wehmeier, S., Varghese, A.S., Gurcha, S.S., Tissot, B., Panico, M., Hitchen, P., Morris, H.R., Besra, G.S., Dell, A. & 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), 421-433.
|
| Authors | Wehmeier, S., Varghese, A.S., Gurcha, S.S., Tissot, B., Panico, M., Hitchen, P., Morris, H.R., Besra, G.S., Dell, A. & Smith, M. C. M.
|
| Research groups | School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Aberdeen AB25 2ZD, UK.
|
| Corresponding Author | Smith, M. C. M.
|
| Contacts | School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Aberdeen AB25 2ZD, UK.
|
| Reference | Córdova-Dávalos, L. E., Espitia, C., González-Cerón, G., Arreguín-Espinosa, R., Soberón-Chávez, G., & Servín-González, L. (2014). Lipoprotein N-acyl transferase (Lnt1) is dispensable for protein O-mannosylation by Streptomyces coelicolor. FEMS microbiology letters, 350(1), 72-82.
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| Authors | Córdova-Dávalos, L. E., Espitia, C., González-Cerón, G., Arreguín-Espinosa, R., Soberón-Chávez, G., & Servín-González, L.
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| Research groups | School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Aberdeen AB25 2ZD, UK.
|
| Corresponding Author | Servín-González, L.
|
| Contacts | Department of Molecular Biology and Biotechnology, Biomedical Research Institute, National Autonomous University of Mexico, Ciudad Universitaria, Mexico City, DF, Mexico.
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