ID   GLPF_STRCO              Reviewed;         264 AA.
AC   P19255; Q9ADA8;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Probable glycerol uptake facilitator protein {ECO:0000250|UniProtKB:P0AER0};
GN   Name=glpF; Synonyms=gylA; OrderedLocusNames=SCO1659; ORFNames=SCI52.01;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RC   STRAIN=A3(2) / J802;
RX   PubMed=3225846; DOI=10.1016/0022-2836(88)90356-7;
RA   Smith C.P., Chater K.F.;
RT   "Structure and regulation of controlling sequences for the Streptomyces
RT   coelicolor glycerol operon.";
RL   J. Mol. Biol. 204:569-580(1988).
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   -!- INDUCTION: By glycerol.
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/Val (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; AL939109; CAC36362.1; -; Genomic_DNA.
DR   EMBL; X14188; CAA32391.1; -; Genomic_DNA.
DR   PIR; S02067; S02067.
DR   RefSeq; NP_625934.1; NC_003888.3.
DR   RefSeq; WP_003977166.1; NZ_VNID01000018.1.
DR   AlphaFoldDB; P19255; -.
DR   SMR; P19255; -.
DR   STRING; 100226.SCO1659; -.
DR   PRIDE; P19255; -.
DR   GeneID; 1097090; -.
DR   KEGG; sco:SCO1659; -.
DR   PATRIC; fig|100226.15.peg.1676; -.
DR   eggNOG; COG0580; Bacteria.
DR   HOGENOM; CLU_020019_9_2_11; -.
DR   InParanoid; P19255; -.
DR   OMA; MTRTGMF; -.
DR   PhylomeDB; P19255; -.
DR   Proteomes; UP000001973; 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   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..264
FT                   /note="Probable glycerol uptake facilitator protein"
FT                   /id="PRO_0000064089"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           67..69
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           214..216
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   264 AA;  26852 MW;  3D761BAA5C658693 CRC64;
     MSSSDIFIGE TIGTALLILL GGGVCAAVTL KASKARNAGW LAIAFGWGFA VMTAAYISGP
     LSGAHLNPAV TVGIAIKDGD WSNTPTYFAG QLLGAMIGAV LVWVAYYGQF QAHLTDREIV
     GGPGAQDTTA KSVEAQEKGA GPVLGVFSTG PEIRHTVQNL ATEIIGTFVL LLAILTQGLN
     DEGNGLGILG ALITGFVVVS IGLSLGGPTG YAINPVRDLG PRIVHALLPL PNKGGSDWSY
     AWIPVVGPLI GGAIAGGVYN VAFA