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


1.A.8.3.1
Aquaporin Z water channel (aqpZ gene expression is under sigma S control; induced at the onset of stationary phase) (Mallo and Ashby, 2006).  The high resolution 3-d structure is available (PDB 1RC2) revealing two re-entrant coil-helix domains from the selectivity filter (Savage et al. 2003).

Accession Number:P60844
Protein Name:Aquaporin Z AQPZ aka BNIP aka B0875
Length:231
Molecular Weight:23703.00
Species:Escherichia coli [83333]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate water

Cross database links:

Genevestigator: P60844
EchoBASE: EB1283
EcoGene: EG13270
eggNOG: COG0580
HEGENOM: HBG705794
DIP: DIP-35499N
RefSeq: AP_001506.1    NP_415396.1   
Entrez Gene ID: 945497   
Pfam: PF00230   
Drugbank: Drugbank Link   
BioCyc: EcoCyc:AQPZ-MONOMER    ECOL168927:B0875-MONOMER   
KEGG: ecj:JW0859    eco:b0875   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0015250 F:water channel activity
GO:0009992 P:cellular water homeostasis
GO:0006970 P:response to osmotic stress
GO:0055085 P:transmembrane transport
GO:0006833 P:water transport

References (13)

[1] “Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli.”  Calamita G.et.al.   7493926
[2] “Isolation of a gene encoding nodulin-like intrinsic protein of Escherichia coli.”  Fushimi K.et.al.   9137831
[3] “A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.”  Oshima T.et.al.   8905232
[4] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[5] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[6] “Visualization of AqpZ-mediated water permeability in Escherichia coli by cryoelectron microscopy.”  Delamarche C.et.al.   10400575
[7] “Functional reconstitution and characterization of AqpZ, the E. coli water channel protein.”  Borgnia M.J.et.al.   10518952
[8] “Highly selective water channel activity measured by voltage clamp: Analysis of planar lipid bilayers reconstituted with purified AqpZ.”  Pohl P.et.al.   11493683
[9] “Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography.”  Ringler P.et.al.   10518953
[10] “High resolution AFM topographs of the Escherichia coli water channel aquaporin Z.”  Scheuring S.et.al.   10487750
[11] “Global topology analysis of the Escherichia coli inner membrane proteome.”  Daley D.O.et.al.   15919996
[12] “Architecture and selectivity in aquaporins: 2.5 A X-ray structure of aquaporin Z.”  Savage D.F.et.al.   14691544
[13] “The Escherichia coli aquaporin-Z water channel.”  Calamita G.et.al.   10931322
Structure:
1RC2   2ABM   2O9D   2O9E   2O9F   2O9G   3NK5   3NKA   3NKC      [...more]

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:	MFRKLAAECF GTFWLVFGGC GSAVLAAGFP ELGIGFAGVA LAFGLTVLTM AFAVGHISGG 
61:	HFNPAVTIGL WAGGRFPAKE VVGYVIAQVV GGIVAAALLY LIASGKTGFD AAASGFASNG 
121:	YGEHSPGGYS MLSALVVELV LSAGFLLVIH GATDKFAPAG FAPIAIGLAL TLIHLISIPV 
181:	TNTSVNPARS TAVAIFQGGW ALEQLWFFWV VPIVGGIIGG LIYRTLLEKR D