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2.A.1.2.5
Multidrug (14- and 15-membered macrolides, lincosamides, streptogramins, tetracyclines, daunomycin, ethidium bromide, etc.):H+ antiporter, LmrP. Two proton translocation pathways have been proposed (Bapna et al., 2007), but Schaedler and van Veen, 2010 have provided evidence that a flexible cation binding site in LmrP is associated with variable proton coupling. Basic residues R260 and K357 affect the conformational dynamics of LmrP (Wang and van Veen, 2012).  Basic residues, R260 and K357 control the conformational dynamics of the protein (Wang and van Veen 2012).  Also specifically catalyzes Ca2+:3H+ antiport with an affinity of 7 μM (Zhang et al. 2012). Two carboxylates (Asp-235 and Glu-327) are critical for Ca2+ binding.  Protonation drives major conformational switches (Masureel et al. 2013). The system exhibits plasticity in proton interactions, which is a consequence of the flexibility in the location of key residues that are responsible for proton/multidrug antiport (Nair et al. 2016).  

Accession Number:Q48658
Protein Name:LmrP
Length:408
Molecular Weight:44995.00
Species:Lactococcus lactis [1358]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate Macrolides, Lincosamide, Streptogramin, tetracycline, Daunomycin, ethidium bromide, H+

Cross database links:

RefSeq: YP_001033686.1   
Entrez Gene ID: 4797726   
Pfam: PF07690   

Gene Ontology

GO:0055085 P:transmembrane transport

References (1)

[1] “The Lactococcal lmrP gene encodes a proton motive force-dependent drug transporter.”  Bolhuis H.et.al.   7592810

External Searches:

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MKEFWNLDKN LQLRLGIVFL GAFSYGTVFS SMTIYYNQYL GSAITGILLA LSAVATFVAG 
61:	ILAGFFADRN GRKPVMVFGT IIQLLGAALA IASNLPGHVN PWSTFIAFLL ISFGYNFVIT 
121:	AGNAMIIDAS NAENRKVVFM LDYWAQNLSV ILGAALGAWL FRPAFEALLV ILLLTVLVSF 
181:	FLTTFVMTET FKPTVKVDEK AENIFQAYKT VLQDKTYMIF MGANIATTFI IMQFDNFLPV 
241:	HLSNSFKTIT FWGFEIYGQR MLTIYLILAC VLVVLLMTTL NRLTKDWSHQ KGFIWGSLFM 
301:	AIGMIFSFLT TTFTPIFIAG IVYTLGEIVY TPSVQTLGAD LMNPEKIGSY NGVAAIKMPI 
361:	ASILAGLLVS ISPMIKAIGV SLVLALTEVL AIILVLVAVN RHQKTKLN