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3.A.1.4.11
The phenylpropeneoid uptake porter, CouPSTW.  The purple photosynthetic bacterium Rhodopseudomonas palustris is able to grow photoheterotrophically under anaerobic conditions on a range of phenylpropeneoid lignin monomers, including coumarate, ferulate, caffeate, and cinnamate. RPA1789 (CouP) is the periplasmic binding-protein component of the ABC uptake system (CouPSTU).  CouP binds a range of phenylpropeneoid ligands with Kd values in the nanomolar range. The crystal structure of CouP with ferulate as the bound ligand shows H-bond interactions between the 4-OH group of the aromatic ring with His309 and Gln305. H-bonds are also made between the carboxyl group on the ferulate side chain and Arg197, Ser222, and Thr102 (Salmon et al. 2013). Within the same operon are a diguanylate cyclase (Q6N8W3) and a phenylacetate-CoA ligase (Q6N8W5).

Accession Number:Q6N8W4
Protein Name:Putative branched-chain amino acid transport system substrate-binding protein
Length:385
Molecular Weight:40884.00
Species:Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [258594]
Number of TMSs:2
Substrate

Cross database links:

Structure:
3TX6   4F8J   4FB4   4JB0   4JB2     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MTKFKLSATA IAVALALPGL SGAALAETNE ITIGITVTTT GPAAALGIPE RNALEFVAKE 
61:	IGGHPLKVIV LDDGGDPTAA TTNARRFVTE SKADVIMGSS VTPPTVAVSN VANEAQVPHI 
121:	ALAPLPITPE RAKWSVAMPQ PIPIMGKVLY EHMKKNNIKT VGYIGYSDSY GDLWFNDLKK 
181:	QGEAMGLKIV AEERFARPDT SVAGQVLKLV AANPDAILVG ASGTAAALPQ TSLRERGYKG 
241:	LIYQTHGAAS MDFIRIAGKS AEGVLMASGP VMDPEGQDDS ALTKKPGLEL NTAYEAKYGP 
301:	NSRSQFAAHS FDAFKVLERV VPVALKTAKP GTQEFREAIR KALVSEKDIA ASQGVYSFTE 
361:	TDRYGLDDRS RILLTVKDGK YVMVK