PDUF_SALTY
ID PDUF_SALTY Reviewed; 264 AA.
AC P37451;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Propanediol uptake facilitator PduF {ECO:0000303|PubMed:8071226};
GN Name=pduF {ECO:0000303|PubMed:8071226}; OrderedLocusNames=STM2037;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POSSIBLE FUNCTION, MOTIF, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=8071226; DOI=10.1128/jb.176.17.5474-5482.1994;
RA Chen P., Anderson D.I., Roth J.R.;
RT "The control region of the pdu/cob regulon in Salmonella typhimurium.";
RL J. Bacteriol. 176:5474-5482(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=9352910; DOI=10.1128/jb.179.21.6633-6639.1997;
RA Bobik T.A., Xu Y., Jeter R.M., Otto K.E., Roth J.R.;
RT "Propanediol utilization genes (pdu) of Salmonella typhimurium: three genes
RT for the propanediol dehydratase.";
RL J. Bacteriol. 179:6633-6639(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=10498708; DOI=10.1128/jb.181.19.5967-5975.1999;
RA Bobik T.A., Havemann G.D., Busch R.J., Williams D.S., Aldrich H.C.;
RT "The propanediol utilization (pdu) operon of Salmonella enterica serovar
RT typhimurium LT2 includes genes necessary for formation of polyhedral
RT organelles involved in coenzyme B(12)-dependent 1, 2-propanediol
RT degradation.";
RL J. Bacteriol. 181:5967-5975(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [5]
RP PROBABLE FUNCTION, AND INDUCTION BY PROPANEDIOL.
RC STRAIN=LT2;
RX PubMed=7559322; DOI=10.1128/jb.177.19.5401-5410.1995;
RA Chen P., Ailion M., Bobik T., Stormo G., Roth J.;
RT "Five promoters integrate control of the cob/pdu regulon in Salmonella
RT typhimurium.";
RL J. Bacteriol. 177:5401-5410(1995).
RN [6]
RP SYSTEM-MODELING, AND POSSIBLE FUNCTION.
RC STRAIN=LT2;
RX PubMed=28475631; DOI=10.1371/journal.pcbi.1005525;
RA Jakobson C.M., Tullman-Ercek D., Slininger M.F., Mangan N.M.;
RT "A systems-level model reveals that 1,2-Propanediol utilization
RT microcompartments enhance pathway flux through intermediate
RT sequestration.";
RL PLoS Comput. Biol. 13:e1005525-e1005525(2017).
CC -!- FUNCTION: Probably facilitates diffusion of 1,2-propanediol (1,2-PD)
CC into the cell (Probable). Modeling suggests active transport of 1,2-PD
CC is required at low extracellular concentrations to allow maximal growth
CC and saturation of PduP/PduQ within the bacterial microcompartment
CC (BMC); this protein may be the cellular transporter (Probable).
CC {ECO:0000305|PubMed:11677609, ECO:0000305|PubMed:28475631,
CC ECO:0000305|PubMed:8071226}.
CC -!- FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC)
CC concentrates low levels of 1,2-PD catabolic enzymes, concentrates
CC volatile reaction intermediates thus enhancing pathway flux and keeps
CC the level of toxic, mutagenic propionaldehyde low.
CC {ECO:0000305|PubMed:28475631}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: By propanediol aerobically and anaerobically, under control
CC of PocR, Arc and Crp. Has 2 promoters. {ECO:0000269|PubMed:7559322}.
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|PubMed:8071226}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, not required for BMC
CC formation (PubMed:8071226, PubMed:9352910). Reduced levels of PocR
CC protein; pocR is transcribed in part from the pduF promoters
CC (PubMed:7559322). {ECO:0000269|PubMed:7559322,
CC ECO:0000269|PubMed:8071226, ECO:0000269|PubMed:9352910}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AF026270; AAB84108.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20941.1; -; Genomic_DNA.
DR RefSeq; NP_460982.1; NC_003197.2.
DR RefSeq; WP_001000023.1; NC_003197.2.
DR AlphaFoldDB; P37451; -.
DR SMR; P37451; -.
DR STRING; 99287.STM2037; -.
DR PaxDb; P37451; -.
DR EnsemblBacteria; AAL20941; AAL20941; STM2037.
DR GeneID; 1253558; -.
DR KEGG; stm:STM2037; -.
DR PATRIC; fig|99287.12.peg.2159; -.
DR HOGENOM; CLU_020019_9_3_6; -.
DR OMA; ACFPGRK; -.
DR PhylomeDB; P37451; -.
DR BioCyc; SENT99287:STM2037-MON; -.
DR Proteomes; UP000001014; 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 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..264
FT /note="Propanediol uptake facilitator PduF"
FT /id="PRO_0000064095"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
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:8071226"
FT MOTIF 201..203
FT /note="NPA 2"
FT /evidence="ECO:0000269|PubMed:8071226"
FT CONFLICT 121
FT /note="R -> A (in Ref. 1; AAB84108)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..181
FT /note="APLLI -> RLCLL (in Ref. 1; AAB84108)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 27744 MW; CBFB5E729061A26C CRC64;
MNDSLKAQCG AEFLGTGLFL FFGIGCLSAL KVAGASLGLW EICIIWGLGI SLAVYLTAGI
SGGHLNPAVT IALWLFACFP KQKVLPYIIA QFAGAFGGAL LAYVLYSSLF TEFETAHHMV
RGSVESLQLA SIFSTYPAAA LNVWQAALVE VVITSILMGM IMALTDDGNG IPKGPLAPLL
IGILVAVIGA STGPLTGFAM NPARDFGPKL FTWLAGWGNM AMSGGREIPY FIVPIVAPVI
GACAGAAIYR YFIGKNLPCN RCEL
