DGOT_ECOL6
ID DGOT_ECOL6 Reviewed; 430 AA.
AC P0AA77; P31457;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=D-galactonate transporter {ECO:0000250|UniProtKB:P0AA76};
DE AltName: Full=D-galactonate/H(+) symporter {ECO:0000250|UniProtKB:P0AA76};
GN Name=dgoT; OrderedLocusNames=c4612;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Involved in D-galactonate metabolism (By similarity).
CC Catalyzes the proton-dependent uptake of galactonate into the cell (By
CC similarity). {ECO:0000250|UniProtKB:P0AA76}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactonate(in) + H(+)(in) = D-galactonate(out) + H(+)(out);
CC Xref=Rhea:RHEA:29835, ChEBI:CHEBI:12931, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000250|UniProtKB:P0AA76};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29837;
CC Evidence={ECO:0000250|UniProtKB:P0AA76};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AA76}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0AA76}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Phthalate
CC permease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN83047.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN83047.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P0AA77; -.
DR SMR; P0AA77; -.
DR STRING; 199310.c4612; -.
DR EnsemblBacteria; AAN83047; AAN83047; c4612.
DR KEGG; ecc:c4612; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_001265_5_1_6; -.
DR OMA; RVVTTWF; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..430
FT /note="D-galactonate transporter"
FT /id="PRO_0000121378"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 18..39
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 40..50
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 51..74
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 75..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 82..100
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 101..103
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 104..125
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 126..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 142..164
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 165..168
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 169..190
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 191..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 242..267
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 268..276
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 298..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 315..333
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 334..336
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 337..354
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 355..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 374..395
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 396..400
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TRANSMEM 401..423
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT TOPO_DOM 424..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT BINDING 29
FT /ligand="D-galactonate"
FT /ligand_id="ChEBI:CHEBI:12931"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT BINDING 32
FT /ligand="D-galactonate"
FT /ligand_id="ChEBI:CHEBI:12931"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT BINDING 64
FT /ligand="D-galactonate"
FT /ligand_id="ChEBI:CHEBI:12931"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT BINDING 358
FT /ligand="D-galactonate"
FT /ligand_id="ChEBI:CHEBI:12931"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT SITE 31
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
FT SITE 118
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P0AA76"
SQ SEQUENCE 430 AA; 47077 MW; 86B1902777F2E461 CRC64;
MDIPVNAAKP GRRRYLTLVM IFITVVICYV DRANLAVASA HIQEEFGITK AEMGYVFSAF
AWLYTLCQIP GGWFLDRVGS RVTYFIAIFG WSVATLFQGF ATGLMSLIGL RAITGIFEAP
AFPTNNRMVT SWFPEHERAS AVGFYTSGQF VGLAFLTPLL IWIQEMLSWH WVFIVTGGIG
IIWSLIWFKV YQPPRLTKGI SKAELDYIRD GGGLVDGDAP VKKEARQPLT AKDWKLVFHR
KLIGVYLGQF AVASTLWFFL TWFPNYLTQE KGITALKAGF MTTVPFLAAF VGVLLSGWVA
DLLVRKGFSL GFARKTPIIC GLLISTCIMG ANYTNDPMMI MCLMALAFFG NGFASITWSL
VSSLAPMRLI GLTGGVFNFA GGLGGITVPL VVGYLAQGYG FAPALVYISA VALIGALSYI
LLVGDVKRVG
