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2.A.6.1.6
The Zn2+-specific exporter, ZneABC. The ZneB MFP plays an active role in substrate efflux through metal binding and release. Its 2.8 Å structure is available (De Angelis et al., 2010).  3.0 Å  intermediate conformational structures of ZneA have been determined, revealing two Zn2+ binding sites separated by a channel, and the protein has been shown to catalyze electrogenic Zn2+:H+ antiport (Pak et al. 2013).

Accession Number:Q1LCD7
Protein Name:Membrane fusion protein (MFP-RND) heavy metal cation tricomponent efflux HmxB (CzcB-like)
Length:385
Molecular Weight:41375.00
Species:Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [266264]
Number of TMSs:1
Substrate Zn2+, H+

Cross database links:

eggNOG: COG0845
HEGENOM: HBG701618
Entrez Gene ID: 4042191   
KEGG: rme:Rmet_5330   

Gene Ontology

GO:0016020 C:membrane
GO:0046872 F:metal ion binding
GO:0055085 P:transmembrane transport

References (1)

[1] “Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems.”  De Angelis F.et.al.   20534468
Structure:
3LNN     

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)
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FASTA formatted sequence
1:	MKNKPAFPGR VVYWLAAAVI LGLGGAGVWT MRAKAEQKRA DPPVALRHEG ERLVVPAESP 
61:	LRRTLAVAPA TRETVAAPFN LPAMIEADPA KLVKVLPPLA GRIVSLNKQL GDEVKAGDVL 
121:	FTIDSADLAQ ANSDAAKARA AMTMARRNLD RQRELDKSEI AAKRDFEQAQ SDYDQAASES 
181:	QRADARLAQL GAKGGGTLQA GGGHILAVRS PINGRVVDLN AATGAYWNDT TASLMTVADL 
241:	SHVFVTANAQ EKDLGHVYVG QSATVKFDAY DDPQPGKVRY VGQILDADTR TTKVRMVFDN 
301:	PDGRLRPGMF AQATFLSQPH EGIVVPMSAI VQSGFYTRAF VEVAPWQFEP RVIKLGAQIG 
361:	DRMEVKSGLS AGDRVVVKEG VLLND