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3.A.1.3.10
Cystine/cysteine/diaminopimelate transporter, CysXYZ; these proteins are also designated FliY/YecS/YecC.  Note, another transporter is designated CysZ in E. coli (TC# 2.A.121.1.1).  CysXYZ also transports the toxic amino acid analogues, L-selenaproline (SCA; L-selenazolidine-4-carboxylic acid) and L-selenocystine (SeCys) (Deutch et al. 2014). FliY binds L-cystine, L-cysteine, and D-cysteine with micromolar affinities, but binding of the L- and D-enantiomers induced different conformational changes in FliY, where the L- enantiomer/SBP complex interacted more efficiently with the YecSC transporter. YecSC has low basal ATPase activity that is moderately stimulated by apo-FliY, more strongly by D-cysteine-bound FliY, and maximally by L-cysteine- or L-cystine-bound FliY (Sabrialabe et al. 2020). FliY may exist in a conformational equilibrium between an open, unliganded form that does not bind to the YecSC transporter and closed, unliganded and closed, liganded forms that bind this transporter with variable affinities but equally stimulate its ATPase activity. These findings differ from previous observations for similar ABC transporters, highlighting the extent of mechanistic diversity in this large protein family (Sabrialabe et al. 2020).

Accession Number:P0AEM9
Protein Name:Cystine-binding periplasmic protein FLIY aka CysX aka B1920
Length:266
Molecular Weight:29039.00
Species:Escherichia coli [83333]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Periplasm1
Substrate DAP, Cystine

Cross database links:

DIP: DIP-47980N
RefSeq: AP_002535.1    NP_416430.1   
Entrez Gene ID: 948833   
Pfam: PF00497   
BioCyc: EcoCyc:G7039-MONOMER    ECOL168927:B1920-MONOMER   
KEGG: ecj:JW1905    eco:b1920   

Gene Ontology

GO:0030288 C:outer membrane-bounded periplasmic space
GO:0005215 F:transporter activity
GO:0006810 P:transport

References (7)

[1] “Escherichia coli fliAZY operon.”  Mytelka D.S.et.al.   8550423
[2] “A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map.”  Itoh T.et.al.   9097040
[3] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[4] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[5] “Amino acid composition and N-terminal sequence of purified cystine binding protein of Escherichia coli.”  Butler J.D.et.al.   8450713
[6] “Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.”  Link A.J.et.al.   9298646
[7] “Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli.”  Quadroni M.et.al.   8774726

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FASTA formatted sequence
1:	MKLAHLGRQA LMGVMAVALV AGMSVKSFAD EGLLNKVKER GTLLVGLEGT YPPFSFQGDD 
61:	GKLTGFEVEF AQQLAKHLGV EASLKPTKWD GMLASLDSKR IDVVINQVTI SDERKKKYDF 
121:	STPYTISGIQ ALVKKGNEGT IKTADDLKGK KVGVGLGTNY EEWLRQNVQG VDVRTYDDDP 
181:	TKYQDLRVGR IDAILVDRLA ALDLVKKTND TLAVTGEAFS RQESGVALRK GNEDLLKAVN 
241:	DAIAEMQKDG TLQALSEKWF GADVTK