ID   UT_DESVH                Reviewed;         337 AA.
AC   Q72CX3;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Urea transporter DVU1160;
DE            Short=dvUT;
GN   OrderedLocusNames=DVU_1160;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, AND
RP   SUBUNIT.
RX   PubMed=19865084; DOI=10.1038/nature08558;
RA   Levin E.J., Quick M., Zhou M.;
RT   "Crystal structure of a bacterial homologue of the kidney urea
RT   transporter.";
RL   Nature 462:757-761(2009).
CC   -!- FUNCTION: Urea channel that facilitates transmembrane urea transport
CC       down a concentration gradient. {ECO:0000269|PubMed:19865084}.
CC   -!- SUBUNIT: Homotrimer; each subunit contains a pore through which urea
CC       permeates. {ECO:0000269|PubMed:19865084}.
CC   -!- INTERACTION:
CC       Q72CX3; Q72CX3: DVU_1160; NbExp=2; IntAct=EBI-15812037, EBI-15812037;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19865084};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:19865084}.
CC   -!- SIMILARITY: Belongs to the urea transporter family. {ECO:0000305}.
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DR   EMBL; AE017285; AAS95638.1; -; Genomic_DNA.
DR   RefSeq; WP_010938457.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_010379.1; NC_002937.3.
DR   PDB; 3K3F; X-ray; 2.30 A; A=2-337.
DR   PDB; 3K3G; X-ray; 2.40 A; A=2-337.
DR   PDB; 3M6E; X-ray; 2.65 A; A=2-337.
DR   PDB; 3ME1; X-ray; 3.86 A; A/B/C=3-337.
DR   PDBsum; 3K3F; -.
DR   PDBsum; 3K3G; -.
DR   PDBsum; 3M6E; -.
DR   PDBsum; 3ME1; -.
DR   AlphaFoldDB; Q72CX3; -.
DR   SMR; Q72CX3; -.
DR   DIP; DIP-60445N; -.
DR   STRING; 882.DVU_1160; -.
DR   PaxDb; Q72CX3; -.
DR   EnsemblBacteria; AAS95638; AAS95638; DVU_1160.
DR   KEGG; dvu:DVU_1160; -.
DR   PATRIC; fig|882.5.peg.1090; -.
DR   eggNOG; COG4413; Bacteria.
DR   HOGENOM; CLU_047509_0_1_7; -.
DR   OMA; CPDWATA; -.
DR   PhylomeDB; Q72CX3; -.
DR   EvolutionaryTrace; Q72CX3; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0033219; F:urea binding; IDA:UniProtKB.
DR   GO; GO:0015265; F:urea channel activity; IDA:UniProtKB.
DR   GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR   GO; GO:0071918; P:urea transmembrane transport; IDA:UniProtKB.
DR   Gene3D; 1.10.3430.10; -; 1.
DR   InterPro; IPR029020; Ammonium/urea_transptr.
DR   InterPro; IPR004937; Urea_transporter.
DR   PANTHER; PTHR10464; PTHR10464; 1.
DR   Pfam; PF03253; UT; 1.
DR   PIRSF; PIRSF016502; Urea_transporter; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..337
FT                   /note="Urea transporter DVU1160"
FT                   /id="PRO_0000430010"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        11..26
FT                   /note="Helical"
FT   INTRAMEM        31..43
FT                   /note="Helical"
FT   TRANSMEM        47..66
FT                   /note="Helical"
FT   TRANSMEM        71..93
FT                   /note="Helical"
FT   TRANSMEM        99..121
FT                   /note="Helical"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT   INTRAMEM        172..189
FT                   /note="Helical"
FT   INTRAMEM        194..205
FT                   /note="Helical"
FT   TRANSMEM        210..229
FT                   /note="Helical"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT   TRANSMEM        264..285
FT                   /note="Helical"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT   TOPO_DOM        309..337
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   SITE            294
FT                   /note="Important for channel permeability"
FT                   /evidence="ECO:0000250"
FT   HELIX           2..7
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           10..23
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           24..26
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           31..44
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           46..66
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           70..74
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   TURN            75..79
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           80..92
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           99..122
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   TURN            123..125
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           131..141
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           142..145
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           174..186
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           194..207
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           209..228
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           233..237
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   TURN            238..242
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           243..252
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   TURN            253..255
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           261..284
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           286..288
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           295..308
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   TURN            319..321
FT                   /evidence="ECO:0007829|PDB:3K3F"
FT   HELIX           325..332
FT                   /evidence="ECO:0007829|PDB:3K3F"
SQ   SEQUENCE   337 AA;  35757 MW;  BB578918E1BDC9CA CRC64;
     MFGEQLLKNP LIEFCDSVCR GCGQVMFQNN TVTGLLFFAG IFYNSTTLGV CAVLGTAAST
     LTAQLLGVDK PLVRAGLFGF NGTLAGIALP FFFNYEPAML GYVALNGAFT TIIMASLLNF
     LGKWGVPALT APFVLATWLL MFGVYKLSLF HPGALIAPAL PSVAGLADMG TVTGRTFMEG
     LFKGVGEVMF QDNIVTGVIF VVAILVNSRI SALFAVIGSL VGLCTALIMH SPETPVRLGL
     YGFNSVLCGI AMGGIFFYLN IRTFLYALGC MVLGAIATGA FSVLLSPIGM PALTWPFIVV
     TWLFLFAGSM FRNIAQVPTE KAGTPEDNLR SLAIGSR