GLPF_THEMA
ID GLPF_THEMA Reviewed; 234 AA.
AC Q9X1E3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable glycerol uptake facilitator protein {ECO:0000250|UniProtKB:P0AER0};
GN Name=glpF; OrderedLocusNames=TM_1429;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
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; AE000512; AAD36499.1; -; Genomic_DNA.
DR PIR; B72254; B72254.
DR RefSeq; NP_229229.1; NC_000853.1.
DR RefSeq; WP_004081684.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X1E3; -.
DR SMR; Q9X1E3; -.
DR STRING; 243274.THEMA_07170; -.
DR PRIDE; Q9X1E3; -.
DR EnsemblBacteria; AAD36499; AAD36499; TM_1429.
DR KEGG; tma:TM1429; -.
DR eggNOG; COG0580; Bacteria.
DR InParanoid; Q9X1E3; -.
DR OMA; MTRTGMF; -.
DR OrthoDB; 1744995at2; -.
DR Proteomes; UP000008183; 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 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 membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..234
FT /note="Probable glycerol uptake facilitator protein"
FT /id="PRO_0000064092"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 64..66
FT /note="NPA 1"
FT /evidence="ECO:0000305"
FT MOTIF 185..187
FT /note="NPA 2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 24863 MW; 3A42AE91066D1C8E CRC64;
MSVYLAEFLG TMLLIILGDG VVANVVLKKS KGHNSGWIVI TTGWGLAVAM SVYLVGRISG
AHINPAVTIG LAFIGQFPWS KVPGYIFSQI LGAFVGAILV YLTYLPHWKE TDDPDAKLAV
FCTGPAVRKY GANLLTEIIG TMVLLMGVLG IGANKLADGL NPLLVGFLVW SIGLSLGGPT
GYAINPARDF GPRLAHAILP IPGKRDSDWS YSWVPIIGPI IGGILGASLY NWLF