LGOT_ECOLI
ID LGOT_ECOLI Reviewed; 453 AA.
AC P39398; P39397; Q2M5W0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Probable L-galactonate transporter;
DE AltName: Full=Galactonate:H(+) symporter;
GN Name=lgoT; Synonyms=yjiZ, yjjL; OrderedLocusNames=b4356, JW4319;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
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 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 [4]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND 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).
RN [5]
RP FUNCTION, ROLE IN L-GALACTONATE UTILIZATION, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RX PubMed=17088549; DOI=10.1073/pnas.0603364103;
RA Reed J.L., Patel T.R., Chen K.H., Joyce A.R., Applebee M.K., Herring C.D.,
RA Bui O.T., Knight E.M., Fong S.S., Palsson B.O.;
RT "Systems approach to refining genome annotation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17480-17484(2006).
CC -!- FUNCTION: Probably responsible for the transport of L-galactonate from
CC the periplasm across the inner membrane. Is essential for growth on L-
CC galactonate as the sole carbon source. {ECO:0000269|PubMed:17088549}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-galactonate(in) = H(+)(out) + L-galactonate(out);
CC Xref=Rhea:RHEA:28823, ChEBI:CHEBI:15378, ChEBI:CHEBI:53071;
CC Evidence={ECO:0000305|PubMed:17088549};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28825;
CC Evidence={ECO:0000305|PubMed:17088549};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Highly up-regulated during growth on L-galactonate.
CC {ECO:0000269|PubMed:17088549}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on L-
CC galactonate as sole carbon source. {ECO:0000269|PubMed:17088549}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Phthalate
CC permease family. {ECO:0000305}.
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DR EMBL; U14003; AAA97254.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U14003; AAA97253.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC77312.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78346.1; -; Genomic_DNA.
DR PIR; F65250; F65250.
DR PIR; S56583; S56583.
DR RefSeq; NP_418776.1; NC_000913.3.
DR RefSeq; WP_000410113.1; NZ_LN832404.1.
DR AlphaFoldDB; P39398; -.
DR SMR; P39398; -.
DR BioGRID; 4262773; 125.
DR DIP; DIP-12656N; -.
DR IntAct; P39398; 1.
DR STRING; 511145.b4356; -.
DR TCDB; 2.A.1.14.33; the major facilitator superfamily (mfs).
DR PaxDb; P39398; -.
DR PRIDE; P39398; -.
DR EnsemblBacteria; AAC77312; AAC77312; b4356.
DR EnsemblBacteria; BAE78346; BAE78346; BAE78346.
DR GeneID; 948879; -.
DR KEGG; ecj:JW4319; -.
DR KEGG; eco:b4356; -.
DR PATRIC; fig|1411691.4.peg.2330; -.
DR EchoBASE; EB2473; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_001265_5_1_6; -.
DR InParanoid; P39398; -.
DR OMA; LDRFCSK; -.
DR PhylomeDB; P39398; -.
DR BioCyc; EcoCyc:YJIZ-MON; -.
DR BioCyc; MetaCyc:YJIZ-MON; -.
DR PRO; PR:P39398; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042873; P:aldonate transmembrane transport; IMP:EcoCyc.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000849; Sugar_P_transporter.
DR Pfam; PF07690; MFS_1; 1.
DR PIRSF; PIRSF002808; Hexose_phosphate_transp; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..453
FT /note="Probable L-galactonate transporter"
FT /id="PRO_0000121391"
FT TOPO_DOM 1..42
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..107
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..295
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..359
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..422
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 49440 MW; 43156D106B7FCFFA CRC64;
MEKENITIDP RSSFTPSSSA DIPVPPDGLV QRSTRIKRIQ TTAMLLLFFA AVINYLDRSS
LSVANLTIRE ELGLSATEIG ALLSVFSLAY GIAQLPCGPL LDRKGPRLML GLGMFFWSLF
QAMSGMVHNF TQFVLVRIGM GIGEAPMNPC GVKVINDWFN IKERGRPMGF FNAASTIGVA
VSPPILAAMM LVMGWRGMFI TIGVLGIFLA IGWYMLYRNR EHVELTAVEQ AYLNAGSVNA
RRDPLSFAEW RSLFRNRTMW GMMLGFSGIN YTAWLYLAWL PGYLQTAYNL DLKSTGLMAA
IPFLFGAAGM LVNGYVTDWL VKGGMAPIKS RKICIIAGMF CSAAFTLIVP QATTSMTAVL
LIGMALFCIH FAGTSCWGLI HVAVASRMTA SVGSIQNFAS FICASFAPII TGFIVDTTHS
FRLALIICGC VTAAGALAYI FLVRQPINDP RKD
