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).
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| Accession Number: | Q1LCD7 |
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| Protein Name: | Membrane fusion protein (MFP-RND) heavy metal cation tricomponent efflux HmxB (CzcB-like) |
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| Length: | 385 |
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| Molecular Weight: | 41375.00 |
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| Species: | Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [266264] |
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| Number of TMSs: | 1 |
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| Substrate |
zinc(2+), hydron |
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| Entrez Gene ID: |
4042191
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| KEGG: |
rme:Rmet_5330
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[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
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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