ABC transporter of unknown function, but aspects of its structure and mechanism of action are known (Yuan et al. 2001; Zoghbi and Altenberg 2013). Nucleotide-binding domain dimerization occurs as a result of binding to the natural nucleotide triphosphates, ATP, GTP, CTP and UTP, as well as the analog ATP-gamma-S. All the natural nucleotide triphosphates are hydrolyzed at similar rates, whereas ATP-gamma-S is not hydrolyzed. The non-hydrolyzable ATP analog AMP-PNP, frequently assumed to produce the nucleotide-bound conformation, failed to elicit nucleotide-binding domain dimerization (Fendley et al. 2016).
|Protein Name:||Uncharacterized ABC transporter ATP-binding protein MJ0796|
|Species:||Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)  |
|Number of TMSs:||1|
1: MIKLKNVTKT YKMGEEIIYA LKNVNLNIKE GEFVSIMGPS GSGKSTMLNI IGCLDKPTEG
61: EVYIDNIKTN DLDDDELTKI RRDKIGFVFQ QFNLIPLLTA LENVELPLIF KYRGAMSGEE
121: RRKRALECLK MAELEERFAN HKPNQLSGGQ QQRVAIARAL ANNPPIILAD EPTGALDSKT
181: GEKIMQLLKK LNEEDGKTVV VVTHDINVAR FGERIIYLKD GEVEREEKLR GFDDR