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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:Q6N8W0
Protein Name:Branched-chain amino acid transport system permease protein
Length:346
Molecular Weight:36304.00
Species:Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [258594]
Number of TMSs:9
Substrate

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FASTA formatted sequence
1:	MNTTILLFLV QDGITNGAIY ALLGLALVLV FAVTRVILIP QGEFITFGAL TYATLSAGGV 
61:	PGTAQLALMM GLVAFGFELF SARKSLHVAK VMRAALIYIA FPAIVLALAT WLPAHKPGVA 
121:	VNIALSLLIV AAIGLFLYRI AFQPLAHTSV LVLLIASVGC HLALQGFGLV FFGAEGLRGP 
181:	PLSDVALSVG PLLFTGQSLA VYGITLALMA ALWLFFGYTR YGKALRATAV NRLGARLVGI 
241:	RTSLSGQIAF LLASVIGAIS GILIVPITTL YYDTGFLIGL KGFVAAIIGG LVSYPLTAIA 
301:	AIVVGIVESF SSFYASNYKE VIVFTLILPV LVLRSLATPA VEEEKD