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3.A.1.103.2
Heteropolysaccharide O-antigen exporter, Wzm/Wzt (Feng et al., 2004). The C-terminal cytoplasmic domain of Wzt (an IgG-like β-sandwich) determines the specificity of the transporter for either O8 or O9a O-PS (Cuthbertson et al., 2007). The transporter structure reveals a continuous transmembrane channel in a nucleotide-free state (Caffalette et al. 2019). Upon ATP binding, large structural changes within the nucleotide-binding and transmembrane regions push conserved hydrophobic residues at the substrate entry site towards the periplasm and provide a model for polysaccharide translocation. With ATP bound, the transporter forms a large transmembrane channel with openings toward the membrane and periplasm. The channel's periplasmic exit is sealed by detergent molecules that block solvent permeation. Molecular dynamics simulation data suggest that, in a biological membrane, lipid molecules occupy this periplasmic exit and prevent water flux in the transporter's resting state (Caffalette et al. 2019).

Accession Number:Q6E7E8
Protein Name:Wzt(C)
Length:324
Molecular Weight:36614.00
Species:Escherichia coli. [562]
Location1 / Topology2 / Orientation3: Secreted1
Substrate Heteropolysaccharide O-antigen

Cross database links:

Pfam: PF00005   

Gene Ontology

GO:0005524 F:ATP binding
GO:0016887 F:ATPase activity

References (1)

[1] “Synthesis of the heteropolysaccharide O antigen of Escherichia coli O52 requires an ABC transporter: structural and genetic evidence.”  Feng L.et.al.   15231783

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FASTA formatted sequence
1:	MKNEKIIELK NVGLVYREKK TLFTYDEYEA LTNITFDVYR GETLGIIGRN GAGKSTLLRV 
61:	LAGIIKPDSG QITIHSNSIS LMALQAGFDP NLSGRQNTIF SGMVLGHRLS YIKSIIEDIK 
121:	VYSELNEFFE KPIKNYSSGM LARLGFSIAM YTTPEVLLID EVLGVGDVTF AEKAQKSIRE 
181:	KIKSDTTVVI VSHDEHQLKL LSDRLVCIEN GVVLDEGPRD SVYNKYNLIM KLTSYGLKLL 
241:	EYKNTETVAF KVGDINPTAE YSDVNFNIDV DVVSVSFKTT TSDWERVSIK DNSFWLRLNH 
301:	NKIYKIKFKD TKDHDGVFEL SVGY