1.C.36.1.1
IIITCP protein complex EspB/EspD (SctBE). The topology of and EspD interaction sites in EspB have been defined (Luo and Donnenberg, 2011). EspD inserts into the membrane with its two helical hairpins traversing the membrane with the N- and C-termini on the extraluminal surface, forming 2.5 diameter pores (Chatterjee et al. 2015). EspD (SctE) plays a dominant role in pore formation as it assembles into an oligomeric state, regardless of pH, membrane contact, or the presence of EspB (SctB). Subsequently, EspB subunits integrate into EspD homo-oligomers to create EspB-EspD hetero-oligomers that adopt a transmembrane orientation to create a functional pore complex (Gershberg et al. 2024).
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| Accession Number: | O69413 |
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| Protein Name: | EspD |
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| Length: | 374 |
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| Molecular Weight: | 39093.00 |
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| Species: | Escherichia coli [562] |
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| Number of TMSs: | 2 |
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| Location1 / Topology2 / Orientation3: |
Cell inner membrane1 / Multi-pass membrane protein2 |
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| Substrate |
protein polypeptide chain |
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[1] “Pas, a novel protein required for protein secretion and attaching and effacing activities of enterohemorrhagic Escherichia coli.” Kresse A.U. et.al. 9721271
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1: MLNVNNDTLS VTSGVNTASG TSGITQSETG LSLDLQLVKS MNSSAGWTES SPLPTPPAGH
61: SLVTPSAAED VLSKLFGGIS GEVTSRTEEA EPQRTSYPYL SQVNTVDPQQ MMMMVTLLSL
121: DTSAQKVSSL KNSNEIYMDG QTKALENKTQ EYKKQLEEQQ KAEEKSQKSK IVGQVFGWLG
181: VALTAVAAVF NPALWAVVAI GATAMALQTA VDVMGENAPQ GLKTAAQVFG GISMAASILT
241: AGVGGVSSLL PKFGNVANKI GSSVVKVVEK AAEALVKNVF AKISTVAEGV TNGIRSAGTT
301: ALNNEAAQLQ MLSQLAAFAV QNLTRQSESL GESAKLELDK AASELQNQAS YLQSVSQLMS
361: DSARVNSRIV SGRI