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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:Q1LCD9
Protein Name:Heavy metal cation tricomponent efflux outer membrane porin ZneC (CzcC-like)
Length:511
Molecular Weight:53838.00
Species:Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [266264]
Number of TMSs:3
Substrate Zn2+, H+

Cross database links:

eggNOG: COG1538
HEGENOM: HBG759011
Entrez Gene ID: 4042189   
Pfam: PF02321   
KEGG: rme:Rmet_5328   

Gene Ontology

GO:0016020 C:membrane
GO:0008289 F:lipid binding
GO:0005215 F:transporter activity

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:	MAKITSISVA TLLALATAGC AVGPDFQRPA APETDRYTAT TLPAETASAS TPDGQAQRFA 
61:	PGQDVPAQWW TMFGSSELNA LVDAALRANP DLQAMEAALR VAQENVAAQR GAFFPSVDAS 
121:	YTPSRQKIAQ IIASPLSDNS DLFTLHTAQL SVSYVPDVFG GTRRQVESGV AQADVARFQW 
181:	QAAYLTLTSN VVNAAIQEAS LRAQIRATQD VIALSTRQLE AVRKQQRLGQ VGAAEVAAQE 
241:	ATLAQAEAAL PPLDRQLAQQ RNLLAALTGR LPSDAVPQQF EFEALTLPGT LPLSLPSRLV 
301:	GQRPDIRAAE AQMHAASAQI GVATAARLPN ITLTAALGSS SQAIGDLFTA GTGFWGISAG 
361:	LMQPIFKGGM LLHQQRAAEA AYKQASAQYR STVLTAYQGV ADALHAIEAD ARGLRTASDA 
421:	ERAAYRSFNI AQAQWKAGQI GYPAVMLAEQ TYRQSAITLV QARASRYSDT VGLMQALGGS 
481:	WEDEPGKTPE NQSDSKPAAA PEAVGKAQGN G