GNTT_ECOLI
ID GNTT_ECOLI Reviewed; 438 AA.
AC P39835; Q2M780; Q6BF35;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=High-affinity gluconate transporter;
DE AltName: Full=Gluconate permease;
DE AltName: Full=Gnt-I system;
GN Name=gntT; Synonyms=gntM, usgA, yhgC; OrderedLocusNames=b3415, JW5690;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [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 [3]
RP SEQUENCE REVISION TO 55-58.
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 [4]
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 [5]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 381-437.
RX PubMed=2845225; DOI=10.1111/j.1365-2958.1988.tb00053.x;
RA Pugsley A.P., Dubreuil C.;
RT "Molecular characterization of malQ, the structural gene for the
RT Escherichia coli enzyme amylomaltase.";
RL Mol. Microbiol. 2:473-479(1988).
RN [6]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [7]
RP CHARACTERIZATION.
RX PubMed=3040894; DOI=10.1099/00221287-132-11-3209;
RA Isturiz T., Palmero E., Vitelli-Flores J.;
RT "Mutations affecting gluconate catabolism in Escherichia coli. Genetic
RT mapping of the locus for the thermosensitive gluconokinase.";
RL J. Gen. Microbiol. 132:3209-3219(1986).
RN [8]
RP CHARACTERIZATION.
RX PubMed=9045817; DOI=10.1128/jb.179.5.1584-1590.1997;
RA Porco A., Peekhaus N., Bausch C., Tong S., Isturiz T., Conway T.;
RT "Molecular genetic characterization of the Escherichia coli gntT gene of
RT GntI, the main system for gluconate metabolism.";
RL J. Bacteriol. 179:1584-1590(1997).
RN [9]
RP SUBCELLULAR LOCATION.
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; high-affinity
CC intake of gluconate.
CC -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the GntP permease family. {ECO:0000305}.
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DR EMBL; U18997; AAA58213.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48179.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77876.1; -; Genomic_DNA.
DR EMBL; M32793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JC4988; JC4988.
DR RefSeq; WP_001131758.1; NZ_STEB01000004.1.
DR RefSeq; YP_026217.1; NC_000913.3.
DR AlphaFoldDB; P39835; -.
DR BioGRID; 4261217; 20.
DR STRING; 511145.b3415; -.
DR TCDB; 2.A.8.1.4; the gluconate:h(+) symporter (gntp) family.
DR PaxDb; P39835; -.
DR PRIDE; P39835; -.
DR DNASU; 947924; -.
DR EnsemblBacteria; AAT48179; AAT48179; b3415.
DR EnsemblBacteria; BAE77876; BAE77876; BAE77876.
DR GeneID; 66672703; -.
DR GeneID; 947924; -.
DR KEGG; ecj:JW5690; -.
DR KEGG; eco:b3415; -.
DR PATRIC; fig|1411691.4.peg.3313; -.
DR EchoBASE; EB2282; -.
DR eggNOG; COG2610; Bacteria.
DR HOGENOM; CLU_027949_0_0_6; -.
DR InParanoid; P39835; -.
DR OMA; MVLPKGH; -.
DR PhylomeDB; P39835; -.
DR BioCyc; EcoCyc:GNTT-MON; -.
DR BioCyc; MetaCyc:GNTT-MON; -.
DR UniPathway; UPA00792; -.
DR PRO; PR:P39835; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015128; F:gluconate transmembrane transporter activity; IMP:EcoliWiki.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0035429; P:gluconate transmembrane transport; IMP:EcoliWiki.
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..438
FT /note="High-affinity gluconate transporter"
FT /id="PRO_0000061934"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 55..58
FT /note="GGTL -> ADV (in Ref. 1; AAA58213)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="S -> A (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 420..421
FT /note="ET -> VS (in Ref. 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 45967 MW; C142882C557E894C CRC64;
MPLVIVAIGV ILLLLLMIRF KMNGFIALVL VALAVGLMQG MPLDKVIGSI KAGVGGTLGS
LALIMGFGAM LGKMLADCGG AQRIATTLIA KFGKKHIQWA VVLTGFTVGF ALFYEVGFVL
MLPLVFTIAA SANIPLLYVG VPMAAALSVT HGFLPPHPGP TAIATIFNAD MGKTLLYGTI
LAIPTVILAG PVYARVLKGI DKPIPEGLYS AKTFSEEEMP SFGVSVWTSL VPVVLMAMRA
IAEMILPKGH AFLPVAEFLG DPVMATLIAV LIAMFTFGLN RGRSMDQIND TLVSSIKIIA
MMLLIIGGGG AFKQVLVDSG VDKYIASMMH ETNISPLLMA WSIAAVLRIA LGSATVAAIT
AGGIAAPLIA TTGVSPELMV IAVGSGSVIF SHVNDPGFWL FKEYFNLTIG ETIKSWSMLE
TIISVCGLVG CLLLNMVI
