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Database: UniProt
Entry: A0A399T124_9BACT
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ID   A0A399T124_9BACT        Unreviewed;       227 AA.
AC   A0A399T124;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Aquaporin Z {ECO:0000256|HAMAP-Rule:MF_01146};
GN   Name=aqpZ {ECO:0000256|HAMAP-Rule:MF_01146};
GN   ORFNames=D1614_05235 {ECO:0000313|EMBL:RIJ50150.1};
OS   Maribellus luteus.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Maribellus.
OX   NCBI_TaxID=2305463 {ECO:0000313|EMBL:RIJ50150.1, ECO:0000313|Proteomes:UP000265926};
RN   [1] {ECO:0000313|EMBL:RIJ50150.1, ECO:0000313|Proteomes:UP000265926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XSD2 {ECO:0000313|EMBL:RIJ50150.1,
RC   ECO:0000313|Proteomes:UP000265926};
RA   Zhou L.Y.;
RT   "Pallidiluteibacterium maritimus gen. nov., sp. nov., isolated from coastal
RT   sediment.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01146};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01146}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01146};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01146}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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:0000256|HAMAP-Rule:MF_01146}.
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC       {ECO:0000256|HAMAP-Rule:MF_01146}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01146}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RIJ50150.1}.
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DR   EMBL; QWGR01000002; RIJ50150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399T124; -.
DR   OrthoDB; 9807293at2; -.
DR   Proteomes; UP000265926; Unassembled WGS sequence.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01146};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265926};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01146};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01146};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01146};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01146}.
FT   TRANSMEM        35..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   TRANSMEM        80..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   TRANSMEM        124..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   TRANSMEM        157..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   TRANSMEM        196..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   MOTIF           62..64
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   MOTIF           182..184
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   SITE            19
FT                   /note="Involved in tetramerization or stability of the
FT                   tetramer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   SITE            42
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   SITE            170
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   SITE            179
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
FT   SITE            185
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01146"
SQ   SEQUENCE   227 AA;  23545 MW;  33BACD42EB284384 CRC64;
     MKKLVAEFIG TMWLVVGGCG SAVFAAAYPD LGIGFAGVAL AFGLTVLTMV YAIGHISGCH
     LNPAVSIGLW AGGRFDGKDL VPYIISQVLG GIVGAAILYI IITGSGKEIG SFAANGFGEH
     SPDGYSMVSG LVSEIVMTFM FLIVILGATH SKAPKGFAGI AIGLSLTLIH LISIPITNTS
     VNPARSTSQA LFVGDWALGQ LWLFWVAPII GALIAGFVYK LVSPEEK
//
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