2.A.17.4.7
Di-/Tri-peptide porter. 3-d structure (PDB: 2XUT) known revealing a probable alternating access mechanism of transport (Newstead et al., 2011). A second structure shows the protein in an inward open conformation with the peptidommetic, alafosfalin, bound (Guettou et al. 2013). Appears to take up glutathione (Deutschbauer et al. 2011).
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| Accession Number: | Q8EKT7 |
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| Protein Name: | Proton/peptide symporter family protein |
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| Length: | 516 |
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| Molecular Weight: | 56705.00 |
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| Species: | Shewanella oneidensis (strain MR-1) [211586] |
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| Number of TMSs: | 14 |
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| Location1 / Topology2 / Orientation3: |
Membrane1 / Multi-pass membrane protein2 |
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| Substrate |
glutathione, tripeptide, dipeptide |
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| Entrez Gene ID: |
1167900
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| Pfam: |
PF00854
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| KEGG: |
son:SO_0002
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[1] “Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis.” Heidelberg J.F. et.al. 12368813
[2] “Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2.” Newstead S. et.al. 21131908
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1: MTTPVDAPKW PRQIPYIIAS EACERFSFYG MRNILTPFLM TALLLSIPEE LRGAVAKDVF
61: HSFVIGVYFF PLLGGWIADR FFGKYNTILW LSLIYCVGHA FLAIFEHSVQ GFYTGLFLIA
121: LGSGGIKPLV SSFMGDQFDQ SNKSLAQKAF DMFYFTINFG SFFASLSMPL LLKNFGAAVA
181: FGIPGVLMFV ATVFFWLGRK RYIHMPPEPK DPHGFLPVIR SALLTKVEGK GNIGLVLALI
241: GGVSAAYALV NIPTLGIVAG LCCAMVLVMG FVGAGASLQL ERARKSHPDA AVDGVRSVLR
301: ILVLFALVTP FWSLFDQKAS TWILQANDMV KPQWFEPAMM QALNPLLVML LIPFNNFVLY
361: PAIERMGVKL TALRKMGAGI AITGLSWIVV GTIQLMMDGG SALSIFWQIL PYALLTFGEV
421: LVSATGLEFA YSQAPKAMKG TIMSFWTLSV TVGNLWVLLA NVSVKSPTVT EQIVQTGMSV
481: TAFQMFFFAG FAILAAIVFA LYARSYQMQD HYRQAT