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3.A.1.135.5
The hetrodimeric ABC transporter, TM287/TM288.  The 2.9-Å crystal structure has been solved in the inward-facing state. The two nucleotide binding domains (NBDs) remain in contact through an interface involving conserved motifs that connect the two ATP hydrolysis sites.  AMP-PNP binds to a degenerate catalytic site which deviates from the consensus sequence in the same positions as the eukaryotic homologs, CFTR (TC# 3.A.1.202.1) and TAP1-TAP2 (TC# 3.A.1.209.1) (Hohl et al. 2012).  The structural basis for allosteric crosstalk (positive cooperativity) between the two ATP binding sites has been studied (Hohl et al. 2014).  The two NBDs exhibit unexpected differences and flexibility (Bukowska et al. 2015). It exports daunomycin and the nonfluorescent 2,7-bis(carboxyethyl)-5(6)-carboxyfluorescein-acetoxymethylester (BCECF-AM) (Hohl et al. 2012). Timachi et al. 2017 observed hydrolysis-independent closure of the NBD dimer, further stabilized as the consensus site nucleotide is committed to hydrolysis.

Accession Number:Q9WYC3
Protein Name:ABC transporter, ATP-binding protein
Length:577
Molecular Weight:64360.00
Species:Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [243274]
Number of TMSs:6
Substrate Daunomycin, 2,7-bis(carboxyethyl)-5(6)-carboxyfluorescein-acetoxymethylester

Cross database links:

Structure:
3QF4   4Q4A   4Q4H   4Q4J   4Q7K   6QUZ   6QV0   6QV1   6QV2      [...more]

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MKTLARYLKP YWIFAVLAPL FMVVEVICDL SQPTLLARIV DEGIARGDFS LVLKTGILML 
61:	IVALIGAVGG IGCTVFASYA SQNFGADLRR DLFRKVLSFS ISNVNRFHTS SLITRLTNDV 
121:	TQLQNLVMML LRIVVRAPLL FVGGIVMAVS INVKLSSVLI FLIPPIVLLF VWLTKKGNPL 
181:	FRKIQESTDE VNRVVRENLL GVRVVRAFRR EEYENENFRK ANESLRRSII SAFSLIVFAL 
241:	PLFIFIVNMG MIAVLWFGGV LVRNNQMEIG SIMAYTNYLM QIMFSLMMIG NILNFIVRAS 
301:	ASAKRVLEVL NEKPAIEEAD NALALPNVEG SVSFENVEFR YFENTDPVLS GVNFSVKPGS 
361:	LVAVLGETGS GKSTLMNLIP RLIDPERGRV EVDELDVRTV KLKDLRGHIS AVPQETVLFS 
421:	GTIKENLKWG REDATDDEIV EAAKIAQIHD FIISLPEGYD SRVERGGRNF SGGQKQRLSI 
481:	ARALVKKPKV LILDDCTSSV DPITEKRILD GLKRYTKGCT TFIITQKIPT ALLADKILVL 
541:	HEGKVAGFGT HKELLEHCKP YREIYESQFG NGVMNDA