KDGT_SHIFL
ID KDGT_SHIFL Reviewed; 327 AA.
AC P0A714; P32172;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=2-keto-3-deoxygluconate permease;
DE Short=KDG permease;
GN Name=kdgT; OrderedLocusNames=SF3986, S3762;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45420.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18780.1; -; Genomic_DNA.
DR RefSeq; NP_709713.2; NC_004337.2.
DR RefSeq; WP_001166063.1; NZ_UIPU01000091.1.
DR AlphaFoldDB; P0A714; -.
DR STRING; 198214.SF3986; -.
DR EnsemblBacteria; AAN45420; AAN45420; SF3986.
DR EnsemblBacteria; AAP18780; AAP18780; S3762.
DR GeneID; 1026571; -.
DR GeneID; 66672182; -.
DR KEGG; sfl:SF3986; -.
DR KEGG; sfx:S3762; -.
DR PATRIC; fig|198214.7.peg.4698; -.
DR HOGENOM; CLU_057476_0_1_6; -.
DR OMA; ESGPFMT; -.
DR OrthoDB; 1029737at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome;
KW Sugar transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..327
FT /note="2-keto-3-deoxygluconate permease"
FT /id="PRO_0000209684"
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..41
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..162
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..223
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..288
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 327 AA; 33669 MW; 8F870CB233B35453 CRC64;
MQIKRSIEKI 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
