GLPF_SHIFL
ID GLPF_SHIFL Reviewed; 281 AA.
AC P31140;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Glycerol uptake facilitator protein {ECO:0000250|UniProtKB:P0AER0};
DE AltName: Full=Aquaglyceroporin;
GN Name=glpF; OrderedLocusNames=SF4005, S3742;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M4243;
RX PubMed=1400248; DOI=10.1128/jb.174.21.6981-6991.1992;
RA Truniger V., Boos W., Sweet G.;
RT "Molecular analysis of the glpFKX regions of Escherichia coli and Shigella
RT flexneri.";
RL J. Bacteriol. 174:6981-6991(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
CC -!- CAUTION: All strains have an amber mutation in position 215.
CC {ECO:0000305}.
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DR EMBL; Z11768; CAA77815.2; -; Genomic_DNA.
DR EMBL; AE005674; AAN45438.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014073; AAP18762.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; WP_000084271.1; NZ_PUHI01000386.1.
DR AlphaFoldDB; P31140; -.
DR SMR; P31140; -.
DR STRING; 198214.SF4005; -.
DR EnsemblBacteria; AAN45438; AAN45438; SF4005.
DR EnsemblBacteria; AAP18762; AAP18762; S3742.
DR KEGG; sft:NCTC1_04335; -.
DR KEGG; sfx:S3742; -.
DR PATRIC; fig|623.158.peg.4367; -.
DR HOGENOM; CLU_020019_9_3_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000064085"
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; 29810 MW; 94E8C2E6DE6A6568 CRC64;
MSQTSTLKGQ CIAEFLGTGL LIFFGVGCVA ALKVAGASFG QWEISVIWGL GVAMAIYLTA
GVSGAHLNPA VTIALWLFAC FDKRKVIPFI VSQVAGAFCA AALVYGLYYN LFFDFEQTHH
IVRGSVESVD LAGTFSTYPN PHINFVQAFA VEMVITAILM GLILALTDDG NGVPRGPLAP
LLIGLLIAVI GASMGPLTGF AMNPARDFGP KVFAWLAGWG NVAFTGGRDI PYFLVPLFSP
IVGAIVGAFA YRKLIGRHLP CDICVVEEKE TTTPSEQKAS L
