ID   AQPZ_BRUAB              Reviewed;         228 AA.
AC   P0C112; Q57AQ4; Q9LA79;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Aquaporin Z {ECO:0000255|HAMAP-Rule:MF_01146};
DE   AltName: Full=Aquaporin X;
GN   Name=aqpZ {ECO:0000255|HAMAP-Rule:MF_01146}; Synonyms=aqpX;
GN   OrderedLocusNames=BruAb1_1976;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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:0000255|HAMAP-Rule:MF_01146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01146};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29668;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01146};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29669;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01146};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01146}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01146}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01146}.
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). {ECO:0000255|HAMAP-Rule:MF_01146}.
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; AE017223; AAX75280.1; -; Genomic_DNA.
DR   RefSeq; WP_002967012.1; NC_006932.1.
DR   AlphaFoldDB; P0C112; -.
DR   SMR; P0C112; -.
DR   EnsemblBacteria; AAX75280; AAX75280; BruAb1_1976.
DR   GeneID; 3788457; -.
DR   KEGG; bmb:BruAb1_1976; -.
DR   HOGENOM; CLU_020019_3_2_5; -.
DR   Proteomes; UP000000540; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015250; F:water channel activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..228
FT                   /note="Aquaporin Z"
FT                   /id="PRO_0000063983"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   MOTIF           63..65
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   MOTIF           184..186
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            20
FT                   /note="Involved in tetramerization or stability of the
FT                   tetramer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            43
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            172
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            181
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
FT   SITE            187
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01146"
SQ   SEQUENCE   228 AA;  23145 MW;  23C64C39E4DD444A CRC64;
     MLNKLSAEFF GTFWLVFGGC GSAILAAAFP ELGIGFLGVA LAFGLTVLTM AYAVGGISGG
     HFNPAVSLGL TVAGRLPAKD LIPYWVAQVL GAIAAAAILY VIASGKDGFS AGGLASNGYG
     ELSPGGYSMM AGLLIEIILT AFFIIIILGS TSSLAPAGFA PIAIGFGLTL IHLVSIPVTN
     TSVNPARSTG VALFADRAAL SQLWLFWVAP LVGAVIGAII WKGLLGRD
//