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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).

Accession Number:Q8XC86
Protein Name:EspB
Length:312
Molecular Weight:32631.00
Species:Escherichia coli O157:H7 [83334]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate protein polypeptide chain

Cross database links:

RefSeq: NP_290254.1    NP_312581.1   
Entrez Gene ID: 915476    960867   
BioCyc: ECOL83334:ECS4554-MONOMER   
KEGG: ece:Z5105    ecs:ECs4554   

References (2)

[1] “Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.”  Perna N.T.et.al.   11206551
[2] “Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.”  Hayashi T.et.al.   11258796

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MNTIDNTQVT MVNSASESTT GASSAVAASA LSIDSSLLTD GKVDICKLML EIQKLLGKMV 
61:	TLLQDYQQKQ LAQSYQIQQA VFESQNKAIE EKKAAATAAL VGGIISSALG ILGSFAAMNN 
121:	AAKGAGEIAE KASSASSKAA GAASEVANKA LVKATESVAD VAEEASSAMQ KAMATTTKAA 
181:	SRASGVADDV AKASDFAEDL ADAAEKTSRI NKLLNSVDKL TNTTAFVAVT SLAEGTKTLP 
241:	TTISESVKST HEVNEQRAKS LENFQQGNLE LYKQDVRRTQ DDITTRLRDI TSAVRDLLEV 
301:	QNRMGQSGRL AG