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


2.A.66.1.10
Na -dependent cationic drug (ethidium, acriflavine, 2-N-methyl ellipticinium, berberine, norfloxacin, ciprofloxacin, rhodamine 6G, crystal violet, doxorubicin, novobiocin, enoxacin, and tetraphenylphosphonium chloride) efflux pump, NorM (Long et al. 2008).  3-d structures of the N. gonorrheae NorM transporter (96% identical to the N. miningitidis protein) have been solved complexed with three different substrates in a multidrug cavity and Cs (4HUN; Lu et al. 2013).  Lu et al. an identified an uncommon cation-π interaction in the Na+-binding site located outside the drug-binding cavity and validated the biological relevance of both the substrate- and cation-binding sites by conducting drug resistance and transport assays. Additionally, they observed a potential rearrangement of at least two transmembrane helices upon Na+-induced drug export. They suggested that Na+ triggers multidrug extrusion by inducing protein conformational changes rather than by directly competing for the substrate-binding amino acids.  However, see 2.A.66.1.32 where the opposite was concluded for a homologue that functions by drug:H+ antiport.

Accession Number:Q9JV27
Protein Name:NorM
Length:459
Molecular Weight:49941.00
Species:Neisseria meningitidis (serogroup A) [65699]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate ethidium, acriflavine, 2-N-methyl ellipticinium, Berberine, norfloxacin, Ciprofloxacin, Rhodamine 6G, Crystal violet, doxorubicin, Novobiocin, enoxacin, Tetraphenylphosphonium chloride

Cross database links:

HEGENOM: HBG479615
RefSeq: YP_002342441.1   
Entrez Gene ID: 906998   
Pfam: PF01554   
BioCyc: NMEN122587:NMA1022-MONOMER   
KEGG: nma:NMA1022   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0015297 F:antiporter activity
GO:0015238 F:drug transmembrane transporter activity
GO:0006811 P:ion transport
GO:0006855 P:drug transmembrane transport

References (1)

[1] “Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491.”  Parkhill J.et.al.   10761919
Structure:
4huk     

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:	MLLDLNRFSF SVFLKEVRLL TALALPMLLA QVAQVGIGFV DTVMAGGAGK EDLAAVALGS 
61:	SAFATVYITF MGIMAALNPM IAQLYGAGKT DEVGETGRQG IWFGLFLGVF GMVLMWAAIT 
121:	PFRNWLTLSD YVEGTMAQYM LFTSLAMPAA MVHRALHAYA SSLNRPRLIM LVSFAAFVLN 
181:	VPLNYIFVYG KFGMPALGGA GCGLATMAVF WFSALALWIY IAKENFFRPF GLTAKFGKPD 
241:	WAVFKQIWKI GAPIGLSYFL EASAFSFIVF LIAPFGEDYV AAQQVGISLS GILYMIPQSV 
301:	GSAGTVRIGF SLGRREFSRA RYISGVSLVS GWMLAVITVL SLVLFRSPLV SMYNNDPAVL 
361:	SIAATVLLFA GLFQPADFTQ CIASYALRGY KVTKVPMFIH AAAFWGCGLL PGYLLAYRFD 
421:	MGIYGFWTAL IASLTIAAIA LVWCLELCSR EMVRSHKAV