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Database: UniProt
Entry: A0A0T7RQT7_SALET
LinkDB: A0A0T7RQT7_SALET
Original site: A0A0T7RQT7_SALET 
ID   A0A0T7RQT7_SALET        Unreviewed;       322 AA.
AC   A0A0T7RQT7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-SEP-2017, entry version 15.
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:CFW72143.1};
GN   ORFNames=ERS008215_01108 {ECO:0000313|EMBL:CFW72143.1};
OS   Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=58097 {ECO:0000313|EMBL:CFW72143.1, ECO:0000313|Proteomes:UP000048853};
RN   [1] {ECO:0000313|EMBL:CFW72143.1, ECO:0000313|Proteomes:UP000048853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A31126 {ECO:0000313|EMBL:CFW72143.1,
RC   ECO:0000313|Proteomes:UP000048853};
RA   Murphy D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The 2-keto-3-deoxygluconate permease transports the
CC       degraded pectin products into the bacterial cell, where they serve
CC       as carbon and energy sources. This is a hydrogen coupled transport
CC       system. {ECO:0000256|HAMAP-Rule:MF_00070}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00070}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00070}.
CC   -!- SIMILARITY: Belongs to the KdgT transporter family.
CC       {ECO:0000256|HAMAP-Rule:MF_00070}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00070}.
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DR   EMBL; CGIA01000002; CFW72143.1; -; Genomic_DNA.
DR   EnsemblBacteria; CFW72143; CFW72143; ERS008215_01108.
DR   Proteomes; UP000048853; Unassembled WGS sequence.
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   GO; GO:0005351; F:sugar:proton symporter activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00070; KdgT; 1.
DR   InterPro; IPR004684; 2keto-3dGluconate_permease.
DR   Pfam; PF03812; KdgT; 1.
DR   ProDom; PD024513; 2keto-3dGluconate_permease; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Complete proteome {ECO:0000313|Proteomes:UP000048853};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Sugar transport {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Symport {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00070};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00070}.
FT   TRANSMEM     12     29       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM     35     61       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM     73     94       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM    162    181       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM    188    208       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM    214    234       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM    246    268       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
FT   TRANSMEM    280    302       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00070}.
SQ   SEQUENCE   322 AA;  32774 MW;  A94613FEEA3030EC CRC64;
     MKIKKTLERF PGGMMVVPLI IGALFKTFAP EALEIGGFVT SISHGAMAIL GMFLVCMGAD
     IQFKAAPKAL KKGAAITFAK FASGVIIGIL VGKFCGPDGL LGLSALAIIS AMTNSNSGLY
     AALVGEYGDE TDGGAIAVIS LNDGPFFTML ALGSAGMVSI PFMNLVAVII PIIIGMILGN
     LDEDMRKFLK QGSVVTIPFF AFGLGYGIDF ARLITAGSSG ILLGLMTVAI GGFFNIFADR
     LTGGSGVAGA AVSTTSGNAV ATPAAIALLD PHFTDLASTA AAQVAASTII TALCAPFLTV
     WIKKRYDRKL NPAAAGGXXA GG
//
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