ID   KDGT_ECOBW              Reviewed;         327 AA.
AC   C5A077;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=2-keto-3-deoxygluconate permease {ECO:0000255|HAMAP-Rule:MF_00070};
DE            Short=KDG permease {ECO:0000255|HAMAP-Rule:MF_00070};
GN   Name=kdgT {ECO:0000255|HAMAP-Rule:MF_00070}; OrderedLocusNames=BWG_3579;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
CC   -!- FUNCTION: The 2-keto-3-deoxygluconate permease transports the degraded
CC       pectin products into the bacterial cell, where they serve as carbon and
CC       energy sources. This is a hydrogen coupled transport system.
CC       {ECO:0000255|HAMAP-Rule:MF_00070}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00070}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00070}.
CC   -!- SIMILARITY: Belongs to the KdgT transporter family. {ECO:0000255|HAMAP-
CC       Rule:MF_00070}.
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DR   EMBL; CP001396; ACR61769.1; -; Genomic_DNA.
DR   RefSeq; WP_001166063.1; NC_012759.1.
DR   AlphaFoldDB; C5A077; -.
DR   GeneID; 66672182; -.
DR   KEGG; ebw:BWG_3579; -.
DR   HOGENOM; CLU_057476_0_1_6; -.
DR   OMA; ESGPFMT; -.
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: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   Pfam; PF03812; KdgT; 1.
DR   TIGRFAMs; TIGR00793; kdgT; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Sugar transport; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..327
FT                   /note="2-keto-3-deoxygluconate permease"
FT                   /id="PRO_1000202441"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
SQ   SEQUENCE   327 AA;  33669 MW;  8F870CB233B35453 CRC64;
     MQIKRSIEKI PGGMMLVPLF LGALCHTFSP GAGKYFGSFT NGMITGTVPI LAVWFFCMGA
     SIKLSATGTV LRKSGTLVVT KIAVAWVVAA IASRIIPEHG VEVGFFAGLS TLALVAAMDM
     TNGGLYASIM QQYGTKEEAG AFVLMSLESG PLMTMIILGT AGIASFEPHV FVGAVLPFLV
     GFALGNLDPE LREFFSKAVQ TLIPFFAFAL GNTIDLTVIA QTGLLGILLG VAVIIVTGIP
     LIIADKLIGG GDGTAGIAAS SSAGAAVATP VLIAEMVPAF KPMAPAATSL VATAVIVTSI
     LVPILTSIWS RKVKARAAKI EILGTVK