PDUF_CITFR
ID PDUF_CITFR Reviewed; 269 AA.
AC B1VB61;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Propanediol uptake facilitator PduF {ECO:0000303|PubMed:18332146};
GN Name=pduF {ECO:0000303|PubMed:18332146};
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POSSIBLE FUNCTION, MOTIF, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18332146; DOI=10.1074/jbc.m709214200;
RA Parsons J.B., Dinesh S.D., Deery E., Leech H.K., Brindley A.A., Heldt D.,
RA Frank S., Smales C.M., Lunsdorf H., Rambach A., Gass M.H., Bleloch A.,
RA McClean K.J., Munro A.W., Rigby S.E.J., Warren M.J., Prentice M.B.;
RT "Biochemical and Structural Insights into Bacterial Organelle Form and
RT Biogenesis.";
RL J. Biol. Chem. 283:14366-14375(2008).
CC -!- FUNCTION: Probably facilitates diffusion of 1,2-propanediol (1,2-PD)
CC into the cell. {ECO:0000305|PubMed:18332146}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane 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 -!- DISRUPTION PHENOTYPE: Not required for bacterial microcompartment (BMC)
CC formation upon expression of the 21-gene pdu operon in E.coli (this
CC gene is upstream and on the other strand from the pdu operon).
CC {ECO:0000269|PubMed:18332146}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AM498294; CAM57282.1; -; Genomic_DNA.
DR RefSeq; WP_016153527.1; NZ_LIDR01000043.1.
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; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..269
FT /note="Propanediol uptake facilitator PduF"
FT /id="PRO_0000454257"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 66..68
FT /note="NPA 1"
FT /evidence="ECO:0000269|PubMed:18332146"
FT MOTIF 201..203
FT /note="NPA 2"
FT /evidence="ECO:0000269|PubMed:18332146"
SQ SEQUENCE 269 AA; 28125 MW; 08CC16C67B3C2C58 CRC64;
MNDSLKAQCI AEFLGTGLFL FFGIGCLSAL KVAGASLGLW EICIIWGLGI SLAVYLTAGI
SGAHLNPAIT IALWLFACFP GRKVLPYTVA QVAGAFGGAL LAYLLYGSLF TEYESAHQMV
RGSLESLHLA SIFSTYPAAA LSVWQAALVE VVITSILMGM IMALTDDGNG VPKGPLAPLL
IGILVAVIGA STGPLTGFAM NPARDFGPKL FAWMAGWGDV AMTGGRDIPY FIVPIVAPII
GACAGAAIYR YLIGKNLPCN TCKLDENES
