KDGT2_SALTY
ID KDGT2_SALTY Reviewed; 317 AA.
AC Q8ZQZ4;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=2-keto-3-deoxygluconate permease 2;
DE Short=KDG permease 2;
GN Name=kdgT2; OrderedLocusNames=STM0651;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KdgT transporter family. {ECO:0000305}.
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DR EMBL; AE006468; AAL19602.1; -; Genomic_DNA.
DR RefSeq; NP_459643.1; NC_003197.2.
DR RefSeq; WP_000694477.1; NC_003197.2.
DR AlphaFoldDB; Q8ZQZ4; -.
DR STRING; 99287.STM0651; -.
DR PaxDb; Q8ZQZ4; -.
DR EnsemblBacteria; AAL19602; AAL19602; STM0651.
DR GeneID; 1252171; -.
DR KEGG; stm:STM0651; -.
DR PATRIC; fig|99287.12.peg.687; -.
DR HOGENOM; CLU_057476_0_0_6; -.
DR OMA; QYGDARD; -.
DR PhylomeDB; Q8ZQZ4; -.
DR BioCyc; SENT99287:STM0651-MON; -.
DR Proteomes; UP000001014; 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 Pfam; PF03812; KdgT; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Sugar transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..317
FT /note="2-keto-3-deoxygluconate permease 2"
FT /id="PRO_0000209683"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..34
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..104
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..157
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..213
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..281
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 317 AA; 32366 MW; 5030EC93A043ADAA 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 NPAAAGG