KDGT_ECO5E
ID KDGT_ECO5E Reviewed; 327 AA.
AC B5YZ47;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 60.
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};
GN OrderedLocusNames=ECH74115_5364;
OS Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=444450;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC4115 / EHEC;
RX PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
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; CP001164; ACI38399.1; -; Genomic_DNA.
DR RefSeq; WP_001166037.1; NC_011353.1.
DR AlphaFoldDB; B5YZ47; -.
DR KEGG; ecf:ECH74115_5364; -.
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_1000092361"
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; 33695 MW; 8142EB4EE74141B0 CRC64;
MQIKRLIEKI 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
