GLPT_ECOLI
ID GLPT_ECOLI Reviewed; 452 AA.
AC P08194;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Glycerol-3-phosphate transporter;
DE Short=G-3-P transporter;
DE AltName: Full=G-3-P permease;
GN Name=glpT; OrderedLocusNames=b2240, JW2234;
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;
RX PubMed=3329281; DOI=10.1111/j.1365-2958.1987.tb01931.x;
RA Eiglmeier K., Boos W., Cole S.;
RT "Nucleotide sequence and transcriptional startpoint of the glpT gene of
RT Escherichia coli: extensive sequence homology of the glycerol-3-phosphate
RT transport protein with components of the hexose-6-phosphate transport
RT system.";
RL Mol. Microbiol. 1:251-258(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(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 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 TOPOLOGY.
RX PubMed=3141744; DOI=10.1111/j.1365-2958.1988.tb00074.x;
RA Goett P., Boos W.;
RT "The transmembrane topology of the sn-glycerol-3-phosphate permease of
RT Escherichia coli analysed by phoA and lacZ protein fusions.";
RL Mol. Microbiol. 2:655-663(1988).
RN [6]
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 5-451.
RX PubMed=12893936; DOI=10.1126/science.1087619;
RA Huang Y., Lemieux M.J., Song J., Auer M., Wang D.-N.;
RT "Structure and mechanism of the glycerol-3-phosphate transporter from
RT Escherichia coli.";
RL Science 301:616-620(2003).
CC -!- FUNCTION: Responsible for glycerol-3-phosphate uptake.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family. {ECO:0000305}.
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DR EMBL; Y00536; CAA68598.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75300.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16059.1; -; Genomic_DNA.
DR PIR; S00868; JNECGT.
DR RefSeq; NP_416743.1; NC_000913.3.
DR RefSeq; WP_000948731.1; NZ_LN832404.1.
DR PDB; 1PW4; X-ray; 3.30 A; A=3-448.
DR PDBsum; 1PW4; -.
DR AlphaFoldDB; P08194; -.
DR SMR; P08194; -.
DR BioGRID; 4261310; 178.
DR IntAct; P08194; 1.
DR STRING; 511145.b2240; -.
DR TCDB; 2.A.1.4.3; the major facilitator superfamily (mfs).
DR jPOST; P08194; -.
DR PaxDb; P08194; -.
DR PRIDE; P08194; -.
DR EnsemblBacteria; AAC75300; AAC75300; b2240.
DR EnsemblBacteria; BAA16059; BAA16059; BAA16059.
DR GeneID; 946704; -.
DR KEGG; ecj:JW2234; -.
DR KEGG; eco:b2240; -.
DR PATRIC; fig|1411691.4.peg.4499; -.
DR EchoBASE; EB0396; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_001265_31_0_6; -.
DR InParanoid; P08194; -.
DR OMA; AMPYLID; -.
DR PhylomeDB; P08194; -.
DR BioCyc; EcoCyc:GLPT-MON; -.
DR BioCyc; MetaCyc:GLPT-MON; -.
DR EvolutionaryTrace; P08194; -.
DR PRO; PR:P08194; -.
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:0061513; F:glucose 6-phosphate:inorganic phosphate antiporter activity; IBA:GO_Central.
DR GO; GO:0015169; F:glycerol-3-phosphate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015527; F:glycerol-phosphate:inorganic phosphate antiporter activity; IDA:EcoCyc.
DR GO; GO:0015315; F:organophosphate:inorganic phosphate antiporter activity; IMP:EcoCyc.
DR GO; GO:0015760; P:glucose-6-phosphate transport; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0015793; P:glycerol transmembrane transport; IDA:EcoCyc.
DR GO; GO:0015794; P:glycerol-3-phosphate transmembrane transport; IDA:EcoCyc.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR005267; G3P_transporter.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR021159; Sugar-P_transporter_CS.
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 TIGRFAMs; TIGR00712; glpT; 1.
DR PROSITE; PS00942; GLPT; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Glycerol metabolism;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..452
FT /note="Glycerol-3-phosphate transporter"
FT /id="PRO_0000199878"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT TRANSMEM 37..57
FT /note="Helical; Name=1"
FT TOPO_DOM 58..63
FT /note="Periplasmic"
FT TRANSMEM 64..84
FT /note="Helical; Name=2"
FT TOPO_DOM 85..93
FT /note="Cytoplasmic"
FT TRANSMEM 94..112
FT /note="Helical; Name=3"
FT TOPO_DOM 113..120
FT /note="Periplasmic"
FT TRANSMEM 121..141
FT /note="Helical; Name=4"
FT TOPO_DOM 142..160
FT /note="Cytoplasmic"
FT TRANSMEM 161..180
FT /note="Helical; Name=5"
FT TOPO_DOM 181..189
FT /note="Periplasmic"
FT TRANSMEM 190..207
FT /note="Helical; Name=6"
FT TOPO_DOM 208..261
FT /note="Cytoplasmic"
FT TRANSMEM 262..282
FT /note="Helical; Name=7"
FT TOPO_DOM 283..287
FT /note="Periplasmic"
FT TRANSMEM 288..308
FT /note="Helical; Name=8"
FT TOPO_DOM 309..321
FT /note="Cytoplasmic"
FT TRANSMEM 322..341
FT /note="Helical; Name=9"
FT TOPO_DOM 342..346
FT /note="Periplasmic"
FT TRANSMEM 347..368
FT /note="Helical; Name=10"
FT TOPO_DOM 369..387
FT /note="Cytoplasmic"
FT TRANSMEM 388..409
FT /note="Helical; Name=11"
FT TOPO_DOM 410..414
FT /note="Periplasmic"
FT TRANSMEM 415..435
FT /note="Helical; Name=12"
FT TOPO_DOM 436..452
FT /note="Cytoplasmic"
FT HELIX 20..45
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 65..89
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 92..112
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:1PW4"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:1PW4"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 153..169
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 191..207
FT /evidence="ECO:0007829|PDB:1PW4"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1PW4"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 253..279
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 288..315
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 321..338
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 347..361
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 380..409
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 414..443
FT /evidence="ECO:0007829|PDB:1PW4"
FT HELIX 444..448
FT /evidence="ECO:0007829|PDB:1PW4"
SQ SEQUENCE 452 AA; 50310 MW; 0DE70D08D40AD445 CRC64;
MLSIFKPAPH KARLPAAEID PTYRRLRWQI FLGIFFGYAA YYLVRKNFAL AMPYLVEQGF
SRGDLGFALS GISIAYGFSK FIMGSVSDRS NPRVFLPAGL ILAAAVMLFM GFVPWATSSI
AVMFVLLFLC GWFQGMGWPP CGRTMVHWWS QKERGGIVSV WNCAHNVGGG IPPLLFLLGM
AWFNDWHAAL YMPAFCAILV ALFAFAMMRD TPQSCGLPPI EEYKNDYPDD YNEKAEQELT
AKQIFMQYVL PNKLLWYIAI ANVFVYLLRY GILDWSPTYL KEVKHFALDK SSWAYFLYEY
AGIPGTLLCG WMSDKVFRGN RGATGVFFMT LVTIATIVYW MNPAGNPTVD MICMIVIGFL
IYGPVMLIGL HALELAPKKA AGTAAGFTGL FGYLGGSVAA SAIVGYTVDF FGWDGGFMVM
IGGSILAVIL LIVVMIGEKR RHEQLLQERN GG
