TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


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:Q8DQF7
Protein Name:Uncharacterized protein
Length:419
Molecular Weight:45277.00
Species:Streptococcus pneumoniae (strain ATCC BAA-255 / R6) [171101]
Number of TMSs:4
Substrate

Cross database links:

Structure:
5XU1     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
Window Size: Angle:  
FASTA formatted sequence
1:	MQNLKFAFSS IMAHKMRSLL TMIGIIIGVS SVVVIMALGD SLSRQVNKDM TKSQKNISVF 
61:	FSPKKSKDGS FTQKQSAFTV SGKEEEVPVE PPKPQESWVQ EAAKLKGVDS YYVTNSTNAI 
121:	LTYQDKKVEN ANLTGGNRTY MDAVKNEIIA GRSLREQDFK EFASVILLDE ELSISLFESP 
181:	QEAINKVVEV NGFSYRVIGV YTSPEAKRSK IYGFGGLPIT TNISLAANFN IDEIASIVFR 
241:	VNDTSLTPTL GPELARKMTE LAGLQQGEYQ VADESVVFAE IQQSFSFMTT IISSIAGISL 
301:	FVGGTGVMNI MLVSVTERTR EIGLRKALGA TRANILIQFL IESMILTLLG GLIGLTIASG 
361:	LTALAGLLLQ GLIEGIEVGV SIPVALFSLA VSASVGMIFG VLPANKASKL DPIEALRYE