GLPF_PSEAE
ID GLPF_PSEAE Reviewed; 279 AA.
AC Q51389;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glycerol uptake facilitator protein {ECO:0000250|UniProtKB:P0AER0};
DE AltName: Full=Glycerol diffusion facilitator;
GN Name=glpF; OrderedLocusNames=PA3581;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9141691; DOI=10.1099/00221287-143-4-1287;
RA Schweizer H.P., Jump R., Po C.;
RT "Structure and gene-polypeptide relationships of the region encoding
RT glycerol diffusion facilitator (glpF) and glycerol kinase (glpK) of
RT Pseudomonas aeruginosa.";
RL Microbiology 143:1287-1297(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 -!- 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}.
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; U49666; AAB57803.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06969.1; -; Genomic_DNA.
DR PIR; G83196; G83196.
DR RefSeq; NP_252271.1; NC_002516.2.
DR RefSeq; WP_003092166.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q51389; -.
DR SMR; Q51389; -.
DR STRING; 287.DR97_4358; -.
DR PaxDb; Q51389; -.
DR EnsemblBacteria; AAG06969; AAG06969; PA3581.
DR GeneID; 880152; -.
DR KEGG; pae:PA3581; -.
DR PATRIC; fig|208964.12.peg.3747; -.
DR PseudoCAP; PA3581; -.
DR HOGENOM; CLU_020019_9_3_6; -.
DR InParanoid; Q51389; -.
DR OMA; MTRTGMF; -.
DR PhylomeDB; Q51389; -.
DR BioCyc; PAER208964:G1FZ6-3650-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015254; F:glycerol channel activity; IBA:GO_Central.
DR GO; GO:0015793; P:glycerol transmembrane transport; IBA:GO_Central.
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..279
FT /note="Glycerol uptake facilitator protein"
FT /id="PRO_0000064084"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 9..37
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 38..42
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 43..63
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 64..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 67..70
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 71..81
FT /note="Helical; Name=M3"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 82..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 88..111
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 112..146
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 147..172
FT /note="Helical; Name=M5"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 173..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 181..197
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 198..201
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 202..205
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT INTRAMEM 206..219
FT /note="Helical; Name=M7"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 220..234
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TRANSMEM 235..257
FT /note="Helical; Name=M8"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT TOPO_DOM 258..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AER0"
FT MOTIF 71..73
FT /note="NPA 1"
FT /evidence="ECO:0000305"
FT MOTIF 206..208
FT /note="NPA 2"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="A -> S (in Ref. 1; AAB57803)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="T -> A (in Ref. 1; AAB57803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 28913 MW; 4596B21F1AB14949 CRC64;
MTTAAPTPSL FGQCLAEFLG TALLIFFGTG CVAALKVAGA SFGLWEISII WGVGVSMAIY
LSAGVSGAHL NPAVSIALWL FAGFEGRKLP FYITAQVAGA FCAAALVYTL YSSLFIEFEQ
AQNIVRGSQD SLALASVFST YPHPALSVGQ AFLVEVVITA ILMAVIMALT DDGNGLPRGP
LAPLLIGLLI AVIGSAMGPL TGFAMNPARD FGPKLMTYLA GWGPIAFTGG REIPYFLVPI
FAPILGACLG AGGYRVLIAR HLPSAAAPAE AEPEKVRAS
