GNTU_ECOLI
ID GNTU_ECOLI Reviewed; 446 AA.
AC P0AC96; P46858; P76694; P76695; Q2M799;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Low-affinity gluconate transporter;
DE AltName: Full=Gluconate permease;
DE AltName: Full=Gnt-I system;
GN Name=gntU; OrderedLocusNames=b4476, JW5686;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8987614; DOI=10.1271/bbb.60.1548;
RA Yamada M., Kawai T., Izu H.;
RT "Analysis of the Escherichia coli gntT and gntU genes and comparison of the
RT products with their homologues.";
RL Biosci. Biotechnol. Biochem. 60:1548-1550(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9135111; DOI=10.1006/jmbi.1996.0913;
RA Izu H., Adachi O., Yamada M.;
RT "Gene organization and transcriptional regulation of the gntRKU operon
RT involved in gluconate uptake and catabolism of Escherichia coli.";
RL J. Mol. Biol. 267:778-793(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP CHARACTERIZATION.
RX PubMed=8655507; DOI=10.1128/jb.178.11.3260-3269.1996;
RA Tong S., Porco A., Isturiz T., Conway T.;
RT "Cloning and molecular genetic characterization of the Escherichia coli
RT gntR, gntK, and gntU genes of GntI, the main system for gluconate
RT metabolism.";
RL J. Bacteriol. 178:3260-3269(1996).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Part of the gluconate utilization system Gnt-I; low-affinity
CC intake of gluconate.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the GntP permease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58233.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA58234.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D84362; BAA12326.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58233.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U18997; AAA58234.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48183.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77857.1; -; Genomic_DNA.
DR PIR; JC4989; JC4989.
DR RefSeq; WP_000210111.1; NZ_SSZK01000008.1.
DR RefSeq; YP_026221.1; NC_000913.3.
DR AlphaFoldDB; P0AC96; -.
DR BioGRID; 4261494; 5.
DR STRING; 511145.b4476; -.
DR TCDB; 2.A.8.1.8; the gluconate:h(+) symporter (gntp) family.
DR jPOST; P0AC96; -.
DR PaxDb; P0AC96; -.
DR PRIDE; P0AC96; -.
DR DNASU; 2847760; -.
DR EnsemblBacteria; AAT48183; AAT48183; b4476.
DR EnsemblBacteria; BAE77857; BAE77857; BAE77857.
DR GeneID; 2847760; -.
DR GeneID; 66672681; -.
DR KEGG; ecj:JW5686; -.
DR KEGG; eco:b4476; -.
DR PATRIC; fig|1411691.4.peg.3293; -.
DR EchoBASE; EB2515; -.
DR eggNOG; COG2610; Bacteria.
DR HOGENOM; CLU_027949_0_2_6; -.
DR InParanoid; P0AC96; -.
DR OMA; MGGILGH; -.
DR PhylomeDB; P0AC96; -.
DR BioCyc; EcoCyc:GNTU-MON; -.
DR BioCyc; MetaCyc:GNTU-MON; -.
DR SABIO-RK; P0AC96; -.
DR PRO; PR:P0AC96; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005402; F:carbohydrate:cation symporter activity; IDA:EcoCyc.
DR GO; GO:0015128; F:gluconate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035429; P:gluconate transmembrane transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Gluconate utilization; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..446
FT /note="Low-affinity gluconate transporter"
FT /id="PRO_0000061935"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..26
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..109
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..176
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..261
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..330
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..387
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 446 AA; 46416 MW; 9BC51A785FF80A5F CRC64;
MTTLTLVLTA VGSVLLLLFL VMKARMHAFL ALMVVSMGAG LFSGMPLDKI AATMEKGMGG
TLGFLAVVVA LGAMFGKILH ETGAVDQIAV KMLKSFGHSR AHYAIGLAGL VCALPLFFEV
AIVLLISVAF SMARHTGTNL VKLVIPLFAG VAAAAAFLVP GPAPMLLASQ MNADFGWMIL
IGLCAAIPGM IIAGPLWGNF ISRYVELHIP DDISEPHLGE GKMPSFGFSL SLILLPLVLV
GLKTIAARFV PEGSTAYEWF EFIGHPFTAI LVACLVAIYG LAMRQGMPKD KVMEICGHAL
QPAGIILLVI GAGGVFKQVL VDSGVGPALG EALTGMGLPI AITCFVLAAA VRIIQGSATV
ACLTAVGLVM PVIEQLNYSG AQMAALSICI AGGSIVVSHV NDAGFWLFGK FTGATEAETL
KTWTMMETIL GTVGAIVGMI AFQLLS
