GLPF_ECOLI
ID GLPF_ECOLI Reviewed; 281 AA.
AC P0AER0; P11244; Q2M8M3; Q46727;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Glycerol uptake facilitator protein;
DE AltName: Full=Aquaglyceroporin;
DE AltName: Full=Glycerol facilitator {ECO:0000303|PubMed:6998951};
GN Name=glpF {ECO:0000303|PubMed:6998951}; OrderedLocusNames=b3927, JW3898;
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=2544860;
RA Muramatsu S., Mizuno T.;
RT "Nucleotide sequence of the region encompassing the glpKF operon and its
RT upstream region containing a bent DNA sequence of Escherichia coli.";
RL Nucleic Acids Res. 17:4378-4378(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=1372899; DOI=10.1016/s0021-9258(18)42670-1;
RA Weissenborn D.L., Wittekindt N., Larson T.J.;
RT "Structure and regulation of the glpFK operon encoding glycerol diffusion
RT facilitator and glycerol kinase of Escherichia coli K-12.";
RL J. Biol. Chem. 267:6122-6131(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33694 / HB101;
RA Chun B.W., Yang M.S.;
RT "Escherichia coli HB101 nucleotide sequence of the glycerol diffusion
RT facilitator protein gene.";
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [5]
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 [6]
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 [7]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=6998951; DOI=10.1128/jb.144.1.274-278.1980;
RA Heller K.B., Lin E.C., Wilson T.H.;
RT "Substrate specificity and transport properties of the glycerol facilitator
RT of Escherichia coli.";
RL J. Bacteriol. 144:274-278(1980).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=7512955; DOI=10.1016/s0021-9258(17)32653-4;
RA Maurel C., Reizer J., Schroeder J.I., Chrispeels M.J., Saier M.H. Jr.;
RT "Functional characterization of the Escherichia coli glycerol facilitator,
RT GlpF, in Xenopus oocytes.";
RL J. Biol. Chem. 269:11869-11872(1994).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9150238; DOI=10.1128/jb.179.10.3365-3367.1997;
RA Sanders O.I., Rensing C., Kuroda M., Mitra B., Rosen B.P.;
RT "Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia
RT coli.";
RL J. Bacteriol. 179:3365-3367(1997).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNITS, AND MUTAGENESIS OF 236-PRO-LEU-237.
RX PubMed=11226336; DOI=10.1073/pnas.051628098;
RA Borgnia M.J., Agre P.;
RT "Reconstitution and functional comparison of purified GlpF and AqpZ, the
RT glycerol and water channels from Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2888-2893(2001).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14970228; DOI=10.1074/jbc.m400037200;
RA Meng Y.L., Liu Z., Rosen B.P.;
RT "As(III) and Sb(III) uptake by GlpF and efflux by ArsB in Escherichia
RT coli.";
RL J. Biol. Chem. 279:18334-18341(2004).
RN [12]
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).
RN [13]
RP REVIEW ON THE MEMBRANE STRUCTURE.
RX PubMed=11101882; DOI=10.1038/81914;
RA Unger V.M.;
RT "Fraternal twins: AQP1 and GlpF.";
RL Nat. Struct. Biol. 7:1082-1084(2000).
RN [14] {ECO:0007744|PDB:1FX8}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLYCEROL, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11039922; DOI=10.1126/science.290.5491.481;
RA Fu D., Libson A., Miercke L.J., Weitzman C., Nollert P., Krucinski J.,
RA Stroud R.M.;
RT "Structure of a glycerol-conducting channel and the basis for its
RT selectivity.";
RL Science 290:481-486(2000).
RN [15] {ECO:0007744|PDB:1LDA, ECO:0007744|PDB:1LDF, ECO:0007744|PDB:1LDI}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF WILD-TYPE AND OF MUTANT
RP PHE-48/THR-200 IN COMPLEX WITH GLYCEROL, SELECTIVITY OF THE WATER CHANNEL,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11964478; DOI=10.1126/science.1067778;
RA Tajkhorshid E., Nollert P., Jensen M.O., Miercke L.J., O'Connell J.D. III,
RA Stroud R.M., Schulten K.;
RT "Control of the selectivity of the aquaporin water channel family by global
RT orientational tuning.";
RL Science 296:525-530(2002).
CC -!- FUNCTION: Mediates glycerol diffusion across the cytoplasmic membrane
CC via a pore-type mechanism (PubMed:6998951, PubMed:7512955,
CC PubMed:11039922, PubMed:11226336). Is highly permeable to glycerol, but
CC less well permeated by water (PubMed:11226336). Does not transport ions
CC (PubMed:7512955). It may also have limited permeability to various
CC other substrates, including xylitol, erythritol, D-arabitol, L-
CC arabitol, ribitol, D-galactitol, D-mannitol, D-sorbitol, urea, glycine,
CC D/L-glyceraldehyde and the trivalent inorganic forms of arsenic and
CC antimony (PubMed:6998951, PubMed:9150238, PubMed:14970228).
CC {ECO:0000269|PubMed:11039922, ECO:0000269|PubMed:11226336,
CC ECO:0000269|PubMed:14970228, ECO:0000269|PubMed:6998951,
CC ECO:0000269|PubMed:7512955, ECO:0000269|PubMed:9150238}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol(in) = glycerol(out); Xref=Rhea:RHEA:29675,
CC ChEBI:CHEBI:17754; Evidence={ECO:0000269|PubMed:11039922,
CC ECO:0000269|PubMed:11226336, ECO:0000269|PubMed:6998951,
CC ECO:0000269|PubMed:7512955};
CC -!- ACTIVITY REGULATION: Transport of glycerol is blocked by mercuric ions
CC (Hg(2+)) but not N-ethylmaleimide. {ECO:0000269|PubMed:7512955}.
CC -!- SUBUNIT: Homotetramer (PubMed:11039922, PubMed:11226336). Exists in
CC multiple oligomeric states (PubMed:11226336). Is predominantly
CC disassociated in the less dense fractions (PubMed:11226336). Tetramers
CC are stabilized while in the membrane and during affinity purification
CC (PubMed:11226336). {ECO:0000269|PubMed:11039922,
CC ECO:0000269|PubMed:11226336}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11039922,
CC ECO:0000269|PubMed:11964478, ECO:0000269|PubMed:15919996}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11039922,
CC ECO:0000269|PubMed:11964478}.
CC -!- INDUCTION: Expression is regulated by the HTH-type transcriptional
CC regulator GlpR and by the cAMP-cAMP receptor protein (CRP) complex.
CC {ECO:0000269|PubMed:1372899}.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA). {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutant grows on glucose but not on glycerol
CC (PubMed:9150238). Disruption of the gene greatly reduces the level of
CC uptake of both arsenite and antimonite (PubMed:9150238,
CC PubMed:14970228). {ECO:0000269|PubMed:14970228,
CC ECO:0000269|PubMed:9150238}.
CC -!- MISCELLANEOUS: The remarkable property of effective water conductance
CC combined with a strict exclusion of all ions including protons is
CC mediated by two conserved asparagines which force a central water
CC molecule to serve strictly as a hydrogen bond donor to its neighboring
CC water molecules. Assisted by the electrostatic potential generated by
CC two half-membrane spanning loops, this dictates opposite orientations
CC of water molecules in the two halves of the channel, and thus prevents
CC the formation of a 'proton wire', while permitting rapid water
CC diffusion. {ECO:0000269|PubMed:11964478}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X15054; CAA33153.1; -; Genomic_DNA.
DR EMBL; M55990; AAA23886.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03059.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76909.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77383.1; -; Genomic_DNA.
DR EMBL; U13915; AAA21363.1; -; Genomic_DNA.
DR PIR; A42157; XMECGF.
DR RefSeq; NP_418362.1; NC_000913.3.
DR RefSeq; WP_000084268.1; NZ_STEB01000017.1.
DR PDB; 1FX8; X-ray; 2.20 A; A=1-281.
DR PDB; 1LDA; X-ray; 2.80 A; A=1-281.
DR PDB; 1LDF; X-ray; 2.10 A; A=1-281.
DR PDB; 1LDI; X-ray; 2.70 A; A=1-281.
DR PDBsum; 1FX8; -.
DR PDBsum; 1LDA; -.
DR PDBsum; 1LDF; -.
DR PDBsum; 1LDI; -.
DR AlphaFoldDB; P0AER0; -.
DR SMR; P0AER0; -.
DR BioGRID; 4263410; 234.
DR DIP; DIP-47976N; -.
DR IntAct; P0AER0; 1.
DR STRING; 511145.b3927; -.
DR DrugBank; DB09462; Glycerin.
DR TCDB; 1.A.8.1.1; the major intrinsic protein (mip) family.
DR PaxDb; P0AER0; -.
DR PRIDE; P0AER0; -.
DR EnsemblBacteria; AAC76909; AAC76909; b3927.
DR EnsemblBacteria; BAE77383; BAE77383; BAE77383.
DR GeneID; 66672165; -.
DR GeneID; 948422; -.
DR KEGG; ecj:JW3898; -.
DR KEGG; eco:b3927; -.
DR PATRIC; fig|1411691.4.peg.2778; -.
DR EchoBASE; EB0391; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_9_3_6; -.
DR InParanoid; P0AER0; -.
DR OMA; MTRTGMF; -.
DR PhylomeDB; P0AER0; -.
DR BioCyc; EcoCyc:GLPF-MON; -.
DR BioCyc; MetaCyc:GLPF-MON; -.
DR EvolutionaryTrace; P0AER0; -.
DR PRO; PR:P0AER0; -.
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:UniProtKB.
DR GO; GO:0015254; F:glycerol channel activity; IDA:EcoCyc.
DR GO; GO:0015168; F:glycerol transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0071288; P:cellular response to mercury ion; IDA:UniProtKB.
DR GO; GO:0015793; P:glycerol transmembrane transport; IDA:UniProtKB.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..281
FT /note="Glycerol uptake facilitator protein"
FT /id="PRO_0000064080"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TRANSMEM 6..34
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TOPO_DOM 35..39
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TRANSMEM 40..60
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TOPO_DOM 61..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11039922"
FT INTRAMEM 64..67
FT /evidence="ECO:0000269|PubMed:11039922"
FT INTRAMEM 68..78
FT /note="Helical; Name=M3"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TOPO_DOM 79..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TRANSMEM 85..108
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TOPO_DOM 109..143
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TRANSMEM 144..169
FT /note="Helical; Name=M5"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TOPO_DOM 170..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TRANSMEM 178..194
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TOPO_DOM 195..198
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:11039922"
FT INTRAMEM 199..202
FT /evidence="ECO:0000269|PubMed:11039922"
FT INTRAMEM 203..216
FT /note="Helical; Name=M7"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TOPO_DOM 217..231
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TRANSMEM 232..254
FT /note="Helical; Name=M8"
FT /evidence="ECO:0000269|PubMed:11039922"
FT TOPO_DOM 255..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11039922"
FT MOTIF 68..70
FT /note="NPA 1"
FT /evidence="ECO:0000305"
FT MOTIF 203..205
FT /note="NPA 2"
FT /evidence="ECO:0000305"
FT BINDING 66..68
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11039922,
FT ECO:0000269|PubMed:11964478, ECO:0007744|PDB:1FX8,
FT ECO:0007744|PDB:1LDF"
FT BINDING 138
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11039922,
FT ECO:0000269|PubMed:11964478, ECO:0007744|PDB:1FX8"
FT BINDING 199..201
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11039922,
FT ECO:0007744|PDB:1FX8"
FT BINDING 203
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11039922,
FT ECO:0000269|PubMed:11964478, ECO:0007744|PDB:1FX8,
FT ECO:0007744|PDB:1LDF"
FT BINDING 206
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11039922,
FT ECO:0007744|PDB:1FX8"
FT SITE 48
FT /note="Substrate discrimination"
FT /evidence="ECO:0000305|PubMed:11101882"
FT SITE 200
FT /note="Substrate discrimination"
FT /evidence="ECO:0000305|PubMed:11101882"
FT SITE 206
FT /note="Substrate discrimination"
FT /evidence="ECO:0000305|PubMed:11101882"
FT VARIANT 126
FT /note="V -> I (in strain: HB101)"
FT VARIANT 160
FT /note="M -> I (in strain: HB101)"
FT VARIANT 239
FT /note="G -> S (in strain: HB101)"
FT MUTAGEN 236..237
FT /note="PL->FW: No detectable water or glycerol
FT permeability."
FT /evidence="ECO:0000269|PubMed:11226336"
FT CONFLICT 168
FT /note="D -> V (in Ref. 1; CAA33153)"
FT /evidence="ECO:0000305"
FT HELIX 7..34
FT /evidence="ECO:0007829|PDB:1LDF"
FT HELIX 41..63
FT /evidence="ECO:0007829|PDB:1LDF"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:1LDF"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1LDF"
FT HELIX 86..118
FT /evidence="ECO:0007829|PDB:1LDF"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1LDF"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1LDF"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1LDF"
FT HELIX 145..167
FT /evidence="ECO:0007829|PDB:1LDF"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1LDF"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1LDF"
FT HELIX 179..198
FT /evidence="ECO:0007829|PDB:1LDF"
FT HELIX 204..216
FT /evidence="ECO:0007829|PDB:1LDF"
FT TURN 217..221
FT /evidence="ECO:0007829|PDB:1LDF"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:1LDF"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1LDI"
FT HELIX 234..254
FT /evidence="ECO:0007829|PDB:1LDF"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1LDF"
SQ SEQUENCE 281 AA; 29780 MW; 94E8D2B79B6E6568 CRC64;
MSQTSTLKGQ CIAEFLGTGL LIFFGVGCVA ALKVAGASFG QWEISVIWGL GVAMAIYLTA
GVSGAHLNPA VTIALWLFAC FDKRKVIPFI VSQVAGAFCA AALVYGLYYN LFFDFEQTHH
IVRGSVESVD LAGTFSTYPN PHINFVQAFA VEMVITAILM GLILALTDDG NGVPRGPLAP
LLIGLLIAVI GASMGPLTGF AMNPARDFGP KVFAWLAGWG NVAFTGGRDI PYFLVPLFGP
IVGAIVGAFA YRKLIGRHLP CDICVVEEKE TTTPSEQKAS L
