2.A.68.1.2 The drug resistance permease, MtrF (Folster and Shafer, 2005). The 3-d structure is known (Su et al. 2015). MtrF is a bowl-shaped dimer with a solvent-filled basin extending from the cytoplasm to halfway
across the membrane bilayer (Su et al. 2015). Each subunit of the transporter contains nine transmembrane helices and
two hairpins, posing a plausible pathway for substrate transport. A combination of the crystal
structure and biochemical functional assays suggests that MtrF is an antibiotic efflux pump
mediating bacterial resistance to sulfonamide antimetabolite drugs (Su et al. 2015). MtrF and YdaH, (TC#2.A.68.1.4) and the dicarboxylate transporter, INDY (TC#2.a.47.5.2) have been shown to have the same 3-d fold (Vergara-Jaque et al. 2015), confirming the assignment of these two families to the same superfamily (Prakash et al. 2003).
|
Accession Number: | Q5F721 |
Protein Name: | Antibiotic resistance efflux pump component |
Length: | 522 |
Molecular Weight: | 56178.00 |
Species: | Neisseria gonorrhoeae (strain ATCC 700825/FA 1090) [242231] |
Number of TMSs: | 12 |
Location1 / Topology2 / Orientation3: |
Mitochondrion inner membrane1 / Multi-pass membrane protein2 |
Substrate |
drug |
---|
1: MSQTDARRSG RFLRTVEWLG NMLPHPVTLF IIFIVLLLIA SAVGAYFGLS VPDPRPVGAK
61: GRADDGLIHV VSLLDADGLI KILTHTVKNF TGFAPLGTVL VSLLGVGIAE KSGLISALMR
121: LLLTKSPRKL TTFMVVFTGI LSNTASELGY VVLIPLSAVI FHSLGRHPLA GLAAAFAGVS
181: GGYSANLFLG TIDPLLAGIT QQAAQIIHPD YVVGPEANWF FMAASTFVIA LIGYFVTEKI
241: VEPQLGPYQS DLSQEEKDIR HSNEITPLEY KGLIWAGVVF VALSALLAWS IVPADGILRH
301: PETGLVAGSP FLKSIVVFIF LLFALPGIVY GRITRSLRGE REVVNAMAES MSTLGLYLVI
361: IFFAAQFVAF FNWTNIGQYI AVKGAVFLKE VGLGGSVLFI GFILICAFIN LMIGSASAQW
421: AVTAPIFVPM LMLAGYAPEV IQAAYRIGDS VTNIITPMMS YFGLIMATVI KYKKDAGVGT
481: LISMMLPYSA FFLIAWIALF CIWVFVLGLP VGPGTPTFYP VP