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: | Q1LCD8 |
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| Protein Name: | Heavy metal cation tricomponent efflux pump ZneA(CzcA-like) |
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| Length: | 1039 |
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| Molecular Weight: | 113590.00 |
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| Species: | Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [266264] |
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| Number of TMSs: | 12 |
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| Substrate |
zinc(2+), hydron |
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1: MIERLVTLCF NRRGIVALVF AMVALYGWYA WKQLPLEAYP DIADTTSQVV TQVNGLAAEE
61: VEQQITIPLE REIMGVPGMH VMRSKSTFGL SLITVVFKDG AEDYWSRQRL QERINGVSLP
121: YGAQPSLDPL TSPIGEIYRY TLVSKTRDLR ELSELQFWKV IPRLKQVAGV VDVANFGGLT
181: TQFMLEFDPV MLSKYNISLN QITQAISENN ANAGGSILNR GEQGLVVRGV GLIRNLDDLG
241: NIVVTQKNGV PVLVKDLGRV VLGNPQRHGI LGMDRNPDTI QGITLLLKNE NPSVVMEGVH
301: AAVRDLNDNI LPKDVKVVPY IDRSNLVDAT VHTVGKTLME GMFLVSLVLL LFLGSPRAAI
361: IVAVTIPLSL LMAFILMHHF KIPANLLSLG AIDFGIIVDG AIVVMENILR RREEDAEKEL
421: HGRDIMQSVL QVARPIFFGM IVIITAYLPL FAFQRIEYKL FSPMAFAVGF ALFGALLVAL
481: LLIPGLAYWA YRKPRKVFHN PALVWLAPRY ESVLNRLVGS TRTAIGIAVA TLVGVMILGA
541: TIGRDFLPYL DEGSIWLQVT LPPGISLEKA GQMADNLRAA TMEFPEVEHV VTQVGRNDEG
601: TDPFSPSHIE TAVTLHPYST WTSGRDKQQL IEAMATRFRD LPGTQVGFSQ PMIDGVLDKL
661: AGAHSDLVVK VYGNDFAETR QVATAITRLL KTVPGAQDVI IDQEPPLPQV RIDVDRAAAA
721: RLGINVADVM ALIQTGIGGS PVTQVFVEDR SYNVVARFIG SSRNDPEAIG NLTLTAANGA
781: HVALAQVAHI RLAEGETTIT REMNKRHLTV RLNLRGRDLS TFLEEARMRI DKEVPYDRTH
841: IQVAWGGQFE NQQRAQARLA VILPMVLALM FVLLFGEFKN LRQPALILMA VPLATLGGLV
901: ALHLRGMTLN VSSAVGFIAL FGVAVLNAII MIANLNRWRD TSGVSLKEAV VRGAGERMRP
961: VLMTATVAAL GLIPAALAHG LGSDVQRPLA TVVVGGLITA TALTLVLLPA LYYLIETRAA
1021: KQVREEPPVQ FGPTSEGDL