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3.A.1.122.20
MacAB-MFP complex of 3 subunits involved in the resistance of antibiotics and antimicrobial peptides. Yang et al. 2018 reported the crystal structures of Spr0694-0695 (MacAB) at 3.3 Å and Spr0693 (MFP; TC# 8.A.1) at 3.0 Å resolution, revealing a MacAB-like efflux pump. The dimeric MacAB adopts a non-canonical fold, the transmembrane domain of which consists of a dimer with eight tightly packed TMSs (4 per subunit) with an extracellular domain between the first and second helices, whereas Spr0693 (the MFP) forms a nanotube channel docked onto the ABC transporter. Structural analyses, combined with ATPase activity and antimicrobial susceptibility assays, enabled the proposal of a putative substrate-entrance tunnel with lateral access controlled by a guard helix (Yang et al. 2018).

Accession Number:Q8DQF8
Protein Name:Uncharacterized protein
Length:233
Molecular Weight:25742.00
Species:Streptococcus pneumoniae (strain ATCC BAA-255 / R6) [171101]
Substrate

Cross database links:

Structure:
5XU1     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MKQLISLKNI FRSYRNGDQE LQVLKNINLE VNEGEFVAIM GPSGSGKSTL MNTIGMLDTP 
61:	TSGEYYLEGQ EVAGLGEKQL AKVRNQQIGF VFQQFFLLSK LNALQNVELP LIYAGVSSSK 
121:	RRKLAEEYLD KVELTERSHH LPSELSGGQK QRVAIARALV NNPSIILADE PTGALDTKTG 
181:	NQIMQLLVDL NKEGKTIIMV THEPEIAAYA KRQIVIRDGV ISSDSAQLGK EEN