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Database: UniProt
Entry: W0PH17_9BURK
LinkDB: W0PH17_9BURK
Original site: W0PH17_9BURK 
ID   W0PH17_9BURK            Unreviewed;       340 AA.
AC   W0PH17;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   07-JUN-2017, entry version 12.
DE   SubName: Full=2-keto-3-deoxygluconate permease {ECO:0000313|EMBL:AHG65776.1};
GN   Name=kdgT {ECO:0000313|EMBL:AHG65776.1};
GN   ORFNames=MIM_c37190 {ECO:0000313|EMBL:AHG65776.1};
OS   Advenella mimigardefordensis DPN7.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae.
OX   NCBI_TaxID=1247726 {ECO:0000313|EMBL:AHG65776.1, ECO:0000313|Proteomes:UP000019095};
RN   [1] {ECO:0000313|EMBL:AHG65776.1, ECO:0000313|Proteomes:UP000019095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPN7 {ECO:0000313|EMBL:AHG65776.1,
RC   ECO:0000313|Proteomes:UP000019095};
RX   PubMed=24739217; DOI=10.1099/mic.0.078279-0;
RA   Wubbeler J.H., Hiessl S., Schuldes J., Thurmer A., Daniel R.,
RA   Steinbuchel A.;
RT   "Unravelling the complete genome sequence of Advenella
RT   mimigardefordensis strain DPN7T and novel insights in the catabolism
RT   of the xenobiotic polythioester precursor 3,3'-dithiodipropionate.";
RL   Microbiology 160:1401-1416(2014).
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DR   EMBL; CP003915; AHG65776.1; -; Genomic_DNA.
DR   EnsemblBacteria; AHG65776; AHG65776; MIM_c37190.
DR   KEGG; amim:MIM_c37190; -.
DR   PATRIC; fig|1247726.3.peg.4108; -.
DR   KO; K02526; -.
DR   Proteomes; UP000019095; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015649; F:2-keto-3-deoxygluconate:proton symporter activity; IEA:InterPro.
DR   InterPro; IPR004684; 2keto-3dGluconate_permease.
DR   Pfam; PF03812; KdgT; 1.
DR   ProDom; PD024513; 2keto-3dGluconate_permease; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000019095};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019095};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     20     36       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     42     65       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     77    102       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    108    131       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    143    162       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    168    191       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    203    222       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    228    247       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    259    280       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    292    314       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   340 AA;  35097 MW;  B44CD7C38FE0D773 CRC64;
     MTQERSLFPM FQTMQKIPGG LMLIPLILGS ILGTFAPEAL DIGSFTTALF KNSALPLIAL
     LIFATGTQVN MRTGGPILAT AGTILFCKTI IPASLIVLLG SFVGIDGVWG ISILALLAAF
     DNSNGGLWLA FTGQYGDARD RGAYVASAVN DGPFFSLLFL GASGLGDIPV IALVAALVPF
     LLGVLVGNLD VQWRKVLDPV PNIVIPFFAF ALGTGINLSA IVSGGTTGII LGFLISPITG
     FLVYMGYKII LRRGGKSGIG FAAGTTAGNA IATPAIVAAA DPRFQVYVET ATAQVAACVL
     ISSIMAPLLA SYFLKKAGEL KPVDAGISDI DTSAGEPVKL
//
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