ProGP347 (Spermidine/putrescine-binding protein (PotD))

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ProGP ID ProGP347 (Spermidine/putrescine-binding protein (PotD))
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 Information
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 NC_000913.2
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
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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
Year of Identification2011
Year of Identification Month Wise2011.1.21
Year of Validation 2011
ReferenceSchwarz, 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(1), pp.45-54.
Corresponding Author Markus Aebi
ContactDepartment of Biology, Institute of Microbiology, ETH Zürich, Wolfgang-Pauli-Strasse 10, Zürich, Switzerland.
ReferenceSugiyama, S., Matsuo, Y., Vassylyev, D.G., Matsushima, M., Morikawa, K., Maenaka, K., Kashiwagi, K. and Igarashi, K., 1996. The 1.8‐Å X‐ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding. Protein science, 5(10), pp.1984-1990.
Corresponding Author Kosuke Morikawa
ContactProtein Engineering Research Institute, Osaka, Japan.
ReferenceSugiyama, 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 (∗). Journal of Biological Chemistry, 271(16), pp.9519-9525.
Corresponding Author Kosuke Morikawa
ContactProtein Engineering Research Institute, Osaka, Japan.
ReferenceSchwarz, F., Lizak, C., Fan, Y.Y., Fleurkens, S., Kowarik, M. and Aebi, M. (201Relaxed 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., 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., 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 Sugiyama, S., Vassylyev, D.G., Matsushima, M., Kashiwagi, K., Igarashi, K. Morikawa, K.
Research GroupProtein Engineering Research Institute, Suita, Osaka, Japan
ContactProtein Engineering Research Institute, Suita, Osaka, Japan