ProGP351

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ProGP ID ProGP351
Validation Status Characterized
Organism Information
Organism NameEscherichia coli K12/DH5alpha
Domain Bacteria
Classification Family: Enterobacteriaceae
Order: "Enterobacteriales"
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 83333
Genome Sequence(s)
GenBank U00096.2
EMBL U00096
Organism Additional Information Escherichia coli (Gram-negative) is the predominant facultative organism in the human intestine. It is responsible for a number of diseases like urinary tract infections, gastroenteritis (diarrhoea), meningitis, traveler's diarrhea and hemorrhagic colitis. There are a myriad of serotypes of pathogenic E. coli. Adhesion to the host cells is an important step in its pathogenesis. However, most strains are harmless and normal flora residing in the gut.
Gene Information
Gene NamepotD (b1123)
NCBI Gene ID 945682
GenBank Gene Sequence 945682
Protein Information
Protein NameSpermidine/putrescine-binding protein (PotD)
UniProtKB/SwissProt ID P0AFK9
NCBI RefSeq NP_415641.1
EMBL-CDSAAC74207.1
UniProtKB Sequence >sp|P0AFK9|POTD_ECOLI Spermidine/putrescine-binding periplasmic protein OS=Escherichia coli (strain K12) GN=potD PE=1 SV=1 MKKWSRHLLAAGALALGMSAAHADDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYE SNETMYAKLKTYKDGAYDLVVPSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLNKPFD PNNDYSIPYIWGATAIGVNGDAVDPKSVTSWADLWKPEYKGSLLLTDDAREVFQMALRKL GYSGNTTDPKEIEAAYNELKKLMPNVAAFNSDNPANPYMEGEVNLGMIWNGSAFVARQAG TPIDVVWPKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAA RKLLSPEVANDKTLYPDAETIKNGEWQNDVGAASSIYEEYYQKLKAGR
Sequence length 348 AA
Subcellular LocationPeriplasm
Function It is a component of the polyamine transport system specifically binding either spermidine or putrescine.
Protein Structure
PDB ID 1POT, 1POY
Glycosylation Status
Glycosylation Type N (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN26, N62
Experimentally Validated Glycosite(s ) in Mature ProteinN26, N62
Glycosite(s) Annotated Protein Sequence >sp|P0AFK9|POTD_ECOLI Spermidine/putrescine-binding periplasmic protein OS=Escherichia coli (strain K12) GN=potD PE=1 SV=1 MKKWSRHLLAAGALALGMSAAHADDN*(26)NTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYE SN*(62)ETMYAKLKTYKDGAYDLVVPSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLNKPFD PNNDYSIPYIWGATAIGVNGDAVDPKSVTSWADLWKPEYKGSLLLTDDAREVFQMALRKL GYSGNTTDPKEIEAAYNELKKLMPNVAAFNSDNPANPYMEGEVNLGMIWNGSAFVARQAG TPIDVVWPKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAA RKLLSPEVANDKTLYPDAETIKNGEWQNDVGAASSIYEEYYQKLKAGR
Sequence Around Glycosites (21 AA) LGMSAAHADDNNTLYFYNWTE
IKVIYSTYESNETMYAKLKTY
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionSBA (soybean agglutinin) lectin-agarose affinity chromatography
Technique(s) used for Glycosylated Residue(s) Detection Site-directed mutagenesis (N26Q, N62Q)
Glycan Information
Glycan Annotation Linkage: Bac-Asn.
GalNAc-α-GalNAc-α-GalNAc-α-GalNAc-α-GalNAc-1,3-Bac, where Bac is bacillosamine, 2,4-diacetamido-2,4,6-trideoxyglucopyranose.
Technique(s) used for Glycan Identification MALDI-MS/MS (matrix-assisted laser desorption/ionization tandem mass spectrometry).
Literature
Additional CommentEngineered glycoprotein. Native PotD protein is unglycosylated. It is glycosylated using Campylobacter lari glycosylation machinery (encoded by its pgl gene cluster) reconstituted in E. coli.
Sequon features: The enzyme ClPglB has a predominant specificity for the sequon D/E-X'-N-X"-S/T (where X' and X" stand for any amino acid except proline) which is efficiently glycosylated. It has also a relaxed specificity toward sequences like DANSG and NNNST. Hence ClPglB can glycosylate sequons lacking D at -2 position but with low efficiency.
UniProtKB ID for ClPglB is B9KDD4.
Year of Identification2011
Year of Identification Month Wise2011.1.21
Year of Validation 2011
Reference Sugiyama, S., Matsuo, Y., Maenaka, K., Vassylyev, D.G., Matsushima, M., Kashiwagi, K., Igarashi, K. and Morikawa, K. (1996) The 1.8-A X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding. Protein Sci, 5, 1984-1990. [PubMed: 8897598]
Author Sugiyama, S., Matsuo, Y., Maenaka, K., Vassylyev, D.G., Matsushima, M., Kashiwagi, K., Igarashi, K. Morikawa, K.
Research GroupProtein Engineering Research Institute, Osaka, Japan.
Corresponding Author Morikawa, K.
ContactProtein Engineering Research Institute, Osaka, Japan.
Reference Sugiyama, S., Matsuo, Y., Maenaka, K., Vassylyev, D.G., Matsushima, M., Kashiwagi, K., Igarashi, K. and Morikawa, K. (1996) The 1.8-A X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding. Protein Sci, 5, 1984-1990. [PubMed: 8897598]
Author Sugiyama, S., Matsuo, Y., Maenaka, K., Vassylyev, D.G., Matsushima, M., Kashiwagi, K., Igarashi, K. Morikawa, K.
Research GroupProtein Engineering Research Institute, Osaka, Japan.
Corresponding Author Morikawa, K.
ContactProtein Engineering Research Institute, Osaka, Japan.
Reference1) Schwarz, F., Lizak, C., Fan, Y.Y., Fleurkens, S., Kowarik, M. and Aebi, M. (2011) Relaxed acceptor site specificity of bacterial oligosaccharyltransferase in vivo. Glycobiology, 21, 45-54. [PubMed: 20847188]
Author Schwarz, F., Lizak, C., Fan, Y.Y., Fleurkens, S., Kowarik, M. and Aebi, M.
Research GroupDepartment of Biology, Institute of Microbiology, ETH Zürich, Wolfgang-Pauli-Strasse 10, Zürich, Switzerland.
Corresponding Author Aebi, M.
ContactDepartment of Biology, Institute of Microbiology, ETH Zürich, Wolfgang-Pauli-Strasse 10, Zürich, Switzerland.
Reference Sugiyama, S., Vassylyev, D.G., Matsushima, M., Kashiwagi, K., Igarashi, K. and Morikawa, K. (1996) Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli. J Biol Chem, 271, 9519-9525. [PubMed: 8621624]
Author Morikawa, K.
Research GroupProtein Engineering Research Institute, Suita, Osaka, Japan
Corresponding Author Sugiyama, S., Vassylyev, D.G., Matsushima, M., Kashiwagi, K., Igarashi, K. Morikawa, K.
ContactProtein Engineering Research Institute, Suita, Osaka, Japan