ID AQPZ_ECOLI Reviewed; 231 AA.
AC P60844; P48838; P75827; Q47159;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 27-MAR-2024, entry version 160.
DE RecName: Full=Aquaporin Z {ECO:0000255|HAMAP-Rule:MF_01146};
DE AltName: Full=Bacterial nodulin-like intrinsic protein;
DE AltName: Full=Water channel AqpZ {ECO:0000305};
GN Name=aqpZ; Synonyms=bniP; OrderedLocusNames=b0875, JW0859;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / DH5-alpha;
RX PubMed=7493926; DOI=10.1074/jbc.270.49.29063;
RA Calamita G., Bishai W.R., Preston G.M., Guggino W.B., Agre P.;
RT "Molecular cloning and characterization of AqpZ, a water channel from
RT Escherichia coli.";
RL J. Biol. Chem. 270:29063-29066(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LE392;
RA Fushimi K.;
RT "Cloning and expression of a new member of aquaporin water channel family
RT of E. coli.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9137831; DOI=10.1080/15216549700202061;
RA Fushimi K., Bai L., Marumo F., Sasaki S.;
RT "Isolation of a gene encoding nodulin-like intrinsic protein of Escherichia
RT coli.";
RL Biochem. Mol. Biol. Int. 41:995-1003(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=10400575; DOI=10.1128/jb.181.14.4193-4197.1999;
RA Delamarche C., Thomas D., Rolland J.-P., Froger A., Gouranton J.,
RA Svelto M., Agre P., Calamita G.;
RT "Visualization of AqpZ-mediated water permeability in Escherichia coli by
RT cryoelectron microscopy.";
RL J. Bacteriol. 181:4193-4197(1999).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-9; CYS-20; THR-183 AND ARG-189.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=10518952; DOI=10.1006/jmbi.1999.3032;
RA Borgnia M.J., Kozono D., Calamita G., Maloney P.C., Agre P.;
RT "Functional reconstitution and characterization of AqpZ, the E. coli water
RT channel protein.";
RL J. Mol. Biol. 291:1169-1179(1999).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF MEMBRANE SELECTIVITY.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=11493683; DOI=10.1073/pnas.161299398;
RA Pohl P., Saparov S.M., Borgnia M.J., Agre P.;
RT "Highly selective water channel activity measured by voltage clamp:
RT Analysis of planar lipid bilayers reconstituted with purified AqpZ.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9624-9629(2001).
RN [10]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=10518953; DOI=10.1006/jmbi.1999.3031;
RA Ringler P., Borgnia M.J., Stahlberg H., Maloney P.C., Agre P., Engel A.;
RT "Structure of the water channel AqpZ from Escherichia coli revealed by
RT electron crystallography.";
RL J. Mol. Biol. 291:1181-1190(1999).
RN [11]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=10487750; DOI=10.1093/emboj/18.18.4981;
RA Scheuring S., Ringler P., Borgnia M.J., Stahlberg H., Mueller D.J.,
RA Agre P., Engel A.;
RT "High resolution AFM topographs of the Escherichia coli water channel
RT aquaporin Z.";
RL EMBO J. 18:4981-4987(1999).
RN [12]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=14691544; DOI=10.1371/journal.pbio.0000072;
RA Savage D.F., Egea P.F., Robles-Colmenares Y., O'Connell J.D. III,
RA Stroud R.M.;
RT "Architecture and selectivity in aquaporins: 2.5 A X-ray structure of
RT aquaporin Z.";
RL PLoS Biol. 1:334-340(2003).
RN [14]
RP REVIEW.
RX PubMed=10931322; DOI=10.1046/j.1365-2958.2000.02016.x;
RA Calamita G.;
RT "The Escherichia coli aquaporin-Z water channel.";
RL Mol. Microbiol. 37:254-262(2000).
CC -!- FUNCTION: Channel that permits osmotically driven movement of water in
CC both directions. It is involved in the osmoregulation and in the
CC maintenance of cell turgor during volume expansion in rapidly growing
CC cells. It mediates rapid entry or exit of water in response to abrupt
CC changes in osmolarity. {ECO:0000269|PubMed:10400575,
CC ECO:0000269|PubMed:10518952, ECO:0000269|PubMed:11493683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377;
CC Evidence={ECO:0000269|PubMed:10400575, ECO:0000269|PubMed:10518952,
CC ECO:0000269|PubMed:11493683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29668;
CC Evidence={ECO:0000269|PubMed:10400575, ECO:0000269|PubMed:10518952,
CC ECO:0000269|PubMed:11493683};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29669;
CC Evidence={ECO:0000269|PubMed:10400575, ECO:0000269|PubMed:10518952,
CC ECO:0000269|PubMed:11493683};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10487750,
CC ECO:0000269|PubMed:10518952, ECO:0000269|PubMed:10518953}.
CC -!- INTERACTION:
CC P60844; P60844: aqpZ; NbExp=4; IntAct=EBI-957663, EBI-957663;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10487750,
CC ECO:0000269|PubMed:10518952}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10487750, ECO:0000269|PubMed:10518952}.
CC -!- INDUCTION: By extracellular hypoosmotic conditions, especially during
CC the mid-logarithmic phase of growth.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA).
CC -!- MISCELLANEOUS: It is a remarkably rigid tetramer that does not
CC dissociate even when solubilized in SDS. {ECO:0000305|PubMed:10518952}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000255|HAMAP-Rule:MF_01146, ECO:0000305}.
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DR EMBL; U38664; AAC43518.1; -; Genomic_DNA.
DR EMBL; D49469; BAA08441.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73962.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35589.1; -; Genomic_DNA.
DR PIR; C64826; C64826.
DR RefSeq; NP_415396.1; NC_000913.3.
DR RefSeq; WP_001298299.1; NZ_SSZK01000002.1.
DR PDB; 1RC2; X-ray; 2.50 A; A/B=1-231.
DR PDB; 2ABM; X-ray; 3.20 A; A/B/C/D/E/F/G/H=1-231.
DR PDB; 2O9D; X-ray; 2.30 A; A/B=1-231.
DR PDB; 2O9E; X-ray; 2.20 A; A=1-231.
DR PDB; 2O9F; X-ray; 2.55 A; A/B=1-231.
DR PDB; 2O9G; X-ray; 1.90 A; A=1-231.
DR PDB; 3NK5; X-ray; 2.40 A; A/B=1-231.
DR PDB; 3NKA; X-ray; 2.50 A; A/B=1-231.
DR PDB; 3NKC; X-ray; 3.10 A; A/B=1-231.
DR PDB; 8H1D; NMR; -; A=1-231.
DR PDBsum; 1RC2; -.
DR PDBsum; 2ABM; -.
DR PDBsum; 2O9D; -.
DR PDBsum; 2O9E; -.
DR PDBsum; 2O9F; -.
DR PDBsum; 2O9G; -.
DR PDBsum; 3NK5; -.
DR PDBsum; 3NKA; -.
DR PDBsum; 3NKC; -.
DR PDBsum; 8H1D; -.
DR AlphaFoldDB; P60844; -.
DR SMR; P60844; -.
DR BioGRID; 4260000; 107.
DR DIP; DIP-35499N; -.
DR STRING; 511145.b0875; -.
DR DrugBank; DB07349; (1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE.
DR DrugBank; DB03152; B-2-Octylglucoside.
DR DrugBank; DB07923; octyl alpha-L-altropyranoside.
DR DrugBank; DB07924; octyl beta-D-galactopyranoside.
DR TCDB; 1.A.8.3.1; the major intrinsic protein (mip) family.
DR PaxDb; 511145-b0875; -.
DR EnsemblBacteria; AAC73962; AAC73962; b0875.
DR GeneID; 75170949; -.
DR GeneID; 945497; -.
DR KEGG; ecj:JW0859; -.
DR KEGG; eco:b0875; -.
DR PATRIC; fig|1411691.4.peg.1402; -.
DR EchoBASE; EB1283; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_3_2_6; -.
DR InParanoid; P60844; -.
DR OMA; KMFWRAV; -.
DR OrthoDB; 9807293at2; -.
DR PhylomeDB; P60844; -.
DR BioCyc; EcoCyc:AQPZ-MONOMER; -.
DR BioCyc; MetaCyc:AQPZ-MONOMER; -.
DR EvolutionaryTrace; P60844; -.
DR PRO; PR:P60844; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0015250; F:water channel activity; IDA:EcoCyc.
DR GO; GO:0009992; P:intracellular water homeostasis; IMP:EcoCyc.
DR GO; GO:0006970; P:response to osmotic stress; IMP:EcoCyc.
DR GO; GO:0006833; P:water transport; IDA:EcoCyc.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR HAMAP; MF_01146; Aquaporin_Z; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR023743; Aquaporin_Z.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR NCBIfam; TIGR00861; MIP; 1.
DR PANTHER; PTHR19139:SF199; AQUAPORIN; 1.
DR PANTHER; PTHR19139; AQUAPORIN TRANSPORTER; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; Aquaporin-like; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..231
FT /note="Aquaporin Z"
FT /id="PRO_0000063989"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..33
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..130
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..201
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 63..65
FT /note="NPA 1"
FT MOTIF 186..188
FT /note="NPA 2"
FT SITE 20
FT /note="Involved in tetramerization or stability of the
FT tetramer"
FT SITE 43
FT /note="Selectivity filter"
FT SITE 174
FT /note="Selectivity filter"
FT SITE 183
FT /note="Selectivity filter"
FT SITE 189
FT /note="Selectivity filter"
FT MUTAGEN 9
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:10518952"
FT MUTAGEN 20
FT /note="C->S: Loss of oligomerization; no alteration of
FT water permeability."
FT /evidence="ECO:0000269|PubMed:10518952"
FT MUTAGEN 183
FT /note="T->C: No effect."
FT /evidence="ECO:0000269|PubMed:10518952"
FT MUTAGEN 189
FT /note="R->V,S: Loss of function."
FT /evidence="ECO:0000269|PubMed:10518952"
FT CONFLICT 14
FT /note="W -> C (in Ref. 2; BAA08441)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="A -> P (in Ref. 2; BAA08441)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="L -> V (in Ref. 1; AAC43518)"
FT /evidence="ECO:0000305"
FT HELIX 1..25
FT /evidence="ECO:0007829|PDB:2O9G"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:2O9G"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2O9G"
FT HELIX 35..58
FT /evidence="ECO:0007829|PDB:2O9G"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:2O9G"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2O9G"
FT HELIX 81..103
FT /evidence="ECO:0007829|PDB:2O9G"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:2O9G"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2O9F"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2O9G"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2O9F"
FT HELIX 131..152
FT /evidence="ECO:0007829|PDB:2O9G"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:8H1D"
FT HELIX 162..181
FT /evidence="ECO:0007829|PDB:2O9G"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:2O9G"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:2O9G"
FT HELIX 205..226
FT /evidence="ECO:0007829|PDB:2O9G"
SQ SEQUENCE 231 AA; 23703 MW; 3BDE1A932D45CF14 CRC64;
MFRKLAAECF GTFWLVFGGC GSAVLAAGFP ELGIGFAGVA LAFGLTVLTM AFAVGHISGG
HFNPAVTIGL WAGGRFPAKE VVGYVIAQVV GGIVAAALLY LIASGKTGFD AAASGFASNG
YGEHSPGGYS MLSALVVELV LSAGFLLVIH GATDKFAPAG FAPIAIGLAL TLIHLISIPV
TNTSVNPARS TAVAIFQGGW ALEQLWFFWV VPIVGGIIGG LIYRTLLEKR D
//
