GLPF_ECOL6
ID GLPF_ECOL6 Reviewed; 281 AA.
AC P0AER1; P11244; Q46727;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Glycerol uptake facilitator protein {ECO:0000250|UniProtKB:P0AER0};
DE AltName: Full=Aquaglyceroporin;
GN Name=glpF; OrderedLocusNames=c4879;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Mediates glycerol diffusion across the cytoplasmic membrane
CC via a pore-type mechanism. {ECO:0000250|UniProtKB:P0AER0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol(in) = glycerol(out); Xref=Rhea:RHEA:29675,
CC ChEBI:CHEBI:17754; Evidence={ECO:0000250|UniProtKB:P0AER0};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AER0}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AER0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0AER0}.
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 -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AE014075; AAN83307.1; -; Genomic_DNA.
DR RefSeq; WP_000084268.1; NC_004431.1.
DR AlphaFoldDB; P0AER1; -.
DR SMR; P0AER1; -.
DR STRING; 199310.c4879; -.
DR EnsemblBacteria; AAN83307; AAN83307; c4879.
DR GeneID; 66672165; -.
DR KEGG; ecc:c4879; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_9_3_6; -.
DR OMA; MTRTGMF; -.
DR BioCyc; ECOL199310:C4879-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..281
FT /note="Glycerol uptake facilitator protein"
FT /id="PRO_0000064082"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 6..34
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 35..39
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 40..60
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 61..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 64..67
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 68..78
FT /note="Helical; Name=M3"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 79..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 85..108
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 109..143
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 144..169
FT /note="Helical; Name=M5"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 170..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 178..194
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 195..198
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 199..202
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 203..216
FT /note="Helical; Name=M7"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 217..231
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 232..254
FT /note="Helical; Name=M8"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 255..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
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 SITE 48
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT SITE 200
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT SITE 206
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
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
