GNTP_ECO57
ID GNTP_ECO57 Reviewed; 447 AA.
AC P0AC95; P39373;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=High-affinity gluconate transporter;
DE AltName: Full=Gluconate permease 3;
DE AltName: Full=Gnt-III system;
GN Name=gntP; OrderedLocusNames=Z5919, ECs5280;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: High-affinity gluconate transporter with fairly broad
CC specificity, including low affinity for glucuronate, several
CC disaccharides, and some hexoses, but not glucose. {ECO:0000250}.
CC -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GntP permease family. {ECO:0000305}.
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DR EMBL; AE005174; AAG59503.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38703.1; -; Genomic_DNA.
DR PIR; C86130; C86130.
DR PIR; H91288; H91288.
DR RefSeq; NP_313307.1; NC_002695.1.
DR RefSeq; WP_000558251.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AC95; -.
DR STRING; 155864.EDL933_5656; -.
DR EnsemblBacteria; AAG59503; AAG59503; Z5919.
DR EnsemblBacteria; BAB38703; BAB38703; ECs_5280.
DR GeneID; 66671796; -.
DR GeneID; 913673; -.
DR KEGG; ece:Z5919; -.
DR KEGG; ecs:ECs_5280; -.
DR PATRIC; fig|386585.9.peg.5517; -.
DR eggNOG; COG2610; Bacteria.
DR HOGENOM; CLU_027949_0_0_6; -.
DR OMA; NTITLMY; -.
DR UniPathway; UPA00792; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0015128; F:gluconate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003474; Glcn_transporter.
DR PANTHER; PTHR30354; PTHR30354; 1.
DR Pfam; PF02447; GntP_permease; 1.
DR PIRSF; PIRSF002746; Gluconate_transporter; 1.
DR TIGRFAMs; TIGR00791; gntP; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Gluconate utilization; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..447
FT /note="High-affinity gluconate transporter"
FT /id="PRO_0000061933"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..28
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..103
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..175
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..260
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..329
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..374
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 447 AA; 47138 MW; 03B3AD16A61330E9 CRC64;
MHVLNILWVV FGIGLMLVLN LKFKINSMVA LLVAALSVGM LAGMDLMSLL HTMKAGFGNT
LGELAIIVVF GAVIGKLMVD SGAAHQIAHT LLARLGLRYV QLSVIIIGLI FGLAMFYEVA
FIMLAPLVIV IAAEAKIPFL KLAIPAVAAA TTAHSLFPPQ PGPVALVNAY GADMGMVYIY
GVLVTIPSVI CAGLILPKFL GNLERPTPSF LKADQPVDMN NLPSFGVSIL VPLIPAIIMI
STTIANIWLV KDTPAWEVVN FIGSSPIAMF IAMVVAFVLF GTARGHDMQW VMNAFESAVK
SIAMVILIIG AGGVLKQTII DTGIGDTIGM LMSHGNISPY IMAWLITVLI RLATGQGVVS
AMTAAGIISA AILDPATGQL VGVNPALLVL ATAAGSNTLT HINDASFWLF KGYFDLSVKD
TLKTWGLLEL VNSVVGLIIV LIISMVA
