ID D9Z530_ECOLX Unreviewed; 322 AA.
AC D9Z530;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=2-keto-3-deoxygluconate permease {ECO:0000256|HAMAP-Rule:MF_00070};
DE Short=KDG permease {ECO:0000256|HAMAP-Rule:MF_00070};
GN Name=kdgT {ECO:0000256|HAMAP-Rule:MF_00070,
GN ECO:0000313|EMBL:ADL13980.1};
OS Escherichia coli.
OG Plasmid pEC_L46 {ECO:0000313|EMBL:ADL14105.1}, and
OG Plasmid pEC_L8 {ECO:0000313|EMBL:ADL13980.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ADL13980.1};
RN [1] {ECO:0000313|EMBL:ADL13980.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L46 {ECO:0000313|EMBL:ADL14105.1}, and L8
RC {ECO:0000313|EMBL:ADL13980.1};
RC PLASMID=pEC_L46 {ECO:0000313|EMBL:ADL14105.1}, and pEC_L8
RC {ECO:0000313|EMBL:ADL13980.1};
RX PubMed=20585456; DOI=10.1371/journal.pone.0011202;
RA Smet A., Van Nieuwerburgh F., Vandekerckhove T.T., Martel A., Deforce D.,
RA Butaye P., Haesebrouck F.;
RT "Complete nucleotide sequence of CTX-M-15-plasmids from clinical
RT Escherichia coli isolates: insertional events of transposons and insertion
RT sequences.";
RL PLoS ONE 5:E11202-E11202(2010).
CC -!- FUNCTION: Catalyzes the proton-dependent uptake of 2-keto-3-
CC deoxygluconate (KDG) into the cell. {ECO:0000256|HAMAP-Rule:MF_00070}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-gluconate(in) + H(+)(in) = 2-dehydro-3-
CC deoxy-D-gluconate(out) + H(+)(out); Xref=Rhea:RHEA:29943,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57990; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00070};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00070};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00070}.
CC -!- SIMILARITY: Belongs to the KdgT transporter family.
CC {ECO:0000256|ARBA:ARBA00006430, ECO:0000256|HAMAP-Rule:MF_00070}.
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DR EMBL; GU371928; ADL13980.1; -; Genomic_DNA.
DR EMBL; GU371929; ADL14105.1; -; Genomic_DNA.
DR RefSeq; YP_003829086.1; NC_014384.1.
DR RefSeq; YP_003829211.1; NC_014385.1.
DR AlphaFoldDB; D9Z530; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015649; F:2-keto-3-deoxygluconate:proton symporter activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00070; KdgT; 1.
DR InterPro; IPR004684; 2keto-3dGluconate_permease.
DR InterPro; IPR018395; 2keto-3dGluconate_permease_sub.
DR NCBIfam; TIGR00793; kdgT; 1.
DR Pfam; PF03812; KdgT; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00070};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00070};
KW Plasmid {ECO:0000313|EMBL:ADL13980.1};
KW Sugar transport {ECO:0000256|HAMAP-Rule:MF_00070};
KW Symport {ECO:0000256|HAMAP-Rule:MF_00070};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00070};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00070};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00070}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 36..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 79..97
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 257..276
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 288..312
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
SQ SEQUENCE 322 AA; 33175 MW; BD6E2C4DEE9EA1E8 CRC64;
MMNIKKTVEK IPGGMMLAPL FLGAVLHTFW PGTGKYFGSF TNGMITGVVP ILAVWLFCMG
ASIKISATGT VLKKSGTLVA TKIATAWVCA FVFAQLLPEG GMVKTGFFAG LSVLAIVAAM
DMTNAGLYAS LMQEYGTKEE AGASVLISLE SGPLMTMIIL GSAGQATFEP EHLAGVLIPF
LVGFLLGNLD PELRELFSRA TKSLIPFFAF ALGNTINLGV IIDTGLLGIL MALAVIVITG
VPLIIMDIML GKGRGTAGIA ASSTAGAAVA TPLLVAEIAP DFAEAAPAAT TLVASCVVIT
AIVVPVITAL WAKHGASRVR AT
//
