ID A0A0F7H743_SERFO Unreviewed; 318 AA.
AC A0A0F7H743;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=WN53_02820 {ECO:0000313|EMBL:AKG68152.1};
OS Serratia fonticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG68152.1, ECO:0000313|Proteomes:UP000034699};
RN [1] {ECO:0000313|EMBL:AKG68152.1, ECO:0000313|Proteomes:UP000034699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG68152.1,
RC ECO:0000313|Proteomes:UP000034699};
RA Chan K.-G., Ee R.;
RT "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011254; AKG68152.1; -; Genomic_DNA.
DR RefSeq; WP_024484334.1; NZ_CP011254.1.
DR AlphaFoldDB; A0A0F7H743; -.
DR STRING; 47917.AV650_25550; -.
DR GeneID; 30319088; -.
DR KEGG; sfw:WN53_02820; -.
DR PATRIC; fig|47917.8.peg.583; -.
DR Proteomes; UP000034699; Chromosome.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000034699};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 49..67
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 79..96
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 102..124
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 247..268
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
FT TRANSMEM 274..296
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00070"
SQ SEQUENCE 318 AA; 31714 MW; 7097A0276EAD55B2 CRC64;
MKIKATIEKI PGGMMVVPLV LGAMINTFAP QALDIGGFTT ALFKNGAAPL IGAFLLCMGA
GISFKAAPQA LLQGGTITLT KLLVAMALGL GVEHLFGAEG IFGLTGVAII AAMSNSNGGL
YAALVGEFGN ERDVGAISIL SLNDGPFFTM IALGAAGMAN IPLMALVAVL VPLLVGMMLG
NLDHQMRDFL TKGGPILIPF FAFALGAGIN LEILLQGGMA GVLLGVLTTF VGGFFNIRAD
RLVGGSGIAG AAASSTAGNA VATPLAIAQA DPSLASVAAA AAPLIAASVI TTAILTPILS
SWVAKRNAAK GAALKETA
//
