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KDGT_ENT38
ID   KDGT_ENT38              Reviewed;         331 AA.
AC   A4W5M3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=Ent638_0314;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP59003.1; -; Genomic_DNA.
DR   RefSeq; WP_011915576.1; NC_009436.1.
DR   AlphaFoldDB; A4W5M3; -.
DR   STRING; 399742.Ent638_0314; -.
DR   EnsemblBacteria; ABP59003; ABP59003; Ent638_0314.
DR   KEGG; ent:Ent638_0314; -.
DR   eggNOG; ENOG502Z7JT; Bacteria.
DR   HOGENOM; CLU_057476_0_1_6; -.
DR   OMA; YASLMNQ; -.
DR   OrthoDB; 1029737at2; -.
DR   Proteomes; UP000000230; Chromosome.
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..331
FT                   /note="2-keto-3-deoxygluconate permease"
FT                   /id="PRO_1000057467"
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        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00070"
FT   TRANSMEM        141..161
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        200..220
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   331 AA;  34030 MW;  43BEEA30D39D259D CRC64;
     MKIKATIERI PGGMMLVPLV LGAILNTLAP NTGAYFGGFT KGMISGTVPI LAVWFFCIGA
     SINLRATGTV LRKSGTLVLT KIAVAWVVAM GCAMFIPENG IQTGFFAGLS VLAIVSAMDM
     TNGGLYASLM NQYGTKEESG AFVLMSLESG PLVTMLILGS AGLASFEPHH FVGAVLPFLI
     GFALGNLDTD LRDFFSKATP VLIPFFGFAL GNTINLNVIM DTGLLGIVLG VAVIIITGIP
     LIIADRVIGG GNGTAGVAAS SAAGAAVANP MIIAQINPSF EPVAASATAL VAASVIVTAI
     LVPIITALYA KRYGNIPKAD VEPQPVESLH H
 
 
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