GLPF_ECO57
ID GLPF_ECO57 Reviewed; 281 AA.
AC P0AER2; P11244; Q46727;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glycerol uptake facilitator protein {ECO:0000250|UniProtKB:P0AER0};
DE AltName: Full=Aquaglyceroporin;
GN Name=glpF; OrderedLocusNames=Z5472, ECs4852;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG59120.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38275.1; -; Genomic_DNA.
DR PIR; D86082; D86082.
DR PIR; D91235; D91235.
DR RefSeq; NP_312879.1; NC_002695.1.
DR RefSeq; WP_000084268.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AER2; -.
DR SMR; P0AER2; -.
DR STRING; 155864.EDL933_5256; -.
DR PRIDE; P0AER2; -.
DR EnsemblBacteria; AAG59120; AAG59120; Z5472.
DR EnsemblBacteria; BAB38275; BAB38275; ECs_4852.
DR GeneID; 66672165; -.
DR GeneID; 915039; -.
DR KEGG; ece:Z5472; -.
DR KEGG; ecs:ECs_4852; -.
DR PATRIC; fig|386585.9.peg.5074; -.
DR eggNOG; COG0580; Bacteria.
DR HOGENOM; CLU_020019_9_3_6; -.
DR OMA; MTRTGMF; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..281
FT /note="Glycerol uptake facilitator protein"
FT /id="PRO_0000064081"
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
