OUSA_DICD3
ID OUSA_DICD3 Reviewed; 501 AA.
AC Q47421; E0SGQ5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glycine betaine/proline/ectoine/pipecolic acid transporter OusA {ECO:0000305};
DE AltName: Full=Osmoprotectant uptake system A {ECO:0000303|PubMed:8550465};
GN Name=ousA {ECO:0000303|PubMed:8550465}; OrderedLocusNames=Dda3937_00791;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RC STRAIN=3937;
RX PubMed=8550465; DOI=10.1128/jb.178.2.447-455.1996;
RA Gouesbet G., Trautwetter A., Bonnassie S., Wu L.F., Blanco C.;
RT "Characterization of the Erwinia chrysanthemi osmoprotectant transporter
RT gene ousA.";
RL J. Bacteriol. 178:447-455(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=3937;
RX PubMed=16000740; DOI=10.1128/aem.71.7.3389-3398.2005;
RA Choquet G., Jehan N., Pissavin C., Blanco C., Jebbar M.;
RT "OusB, a broad-specificity ABC-type transporter from Erwinia chrysanthemi,
RT mediates uptake of glycine betaine and choline with a high affinity.";
RL Appl. Environ. Microbiol. 71:3389-3398(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=3937;
RX PubMed=15720084; DOI=10.1094/mpmi-18-0150;
RA Gloux K., Touze T., Pagot Y., Jouan B., Blanco C.;
RT "Mutations of ousA alter the virulence of Erwinia chrysanthemi.";
RL Mol. Plant Microbe Interact. 18:150-157(2005).
CC -!- FUNCTION: Involved in uptake and accumulation of various
CC osmoprotectants. Allows the uptake of glycine betaine, proline,
CC ectoine, and pipecolic acid (PubMed:8550465, PubMed:16000740). May be a
CC contributory factor in the infection progression within the host
CC (PubMed:15720084). {ECO:0000269|PubMed:15720084,
CC ECO:0000269|PubMed:16000740, ECO:0000269|PubMed:8550465}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for glycine betaine {ECO:0000269|PubMed:16000740};
CC Vmax=270 nmol/min/mg enzyme {ECO:0000269|PubMed:16000740};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8550465};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Induced by osmotic strength and repressed by
CC osmoprotectants. Expression is not affected by the growth phase.
CC {ECO:0000269|PubMed:8550465}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene enhances aggressiveness of
CC the bacterium. Under anaerobic conditions, disruption increases pectate
CC lyase (Pel) production and increases the maceration efficiency on
CC potato tubers (PubMed:15720084). Uptake of glycine betaine and choline
CC is completely abolished in the ousA-ousB double mutant
CC (PubMed:16000740). {ECO:0000269|PubMed:15720084,
CC ECO:0000269|PubMed:16000740}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; X82267; CAA57718.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM97704.1; -; Genomic_DNA.
DR RefSeq; WP_013317165.1; NC_014500.1.
DR AlphaFoldDB; Q47421; -.
DR SMR; Q47421; -.
DR STRING; 198628.Dda3937_00791; -.
DR EnsemblBacteria; ADM97704; ADM97704; Dda3937_00791.
DR GeneID; 9732923; -.
DR KEGG; ddd:Dda3937_00791; -.
DR PATRIC; fig|198628.6.peg.1498; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_001265_39_0_6; -.
DR OMA; FLVEMFP; -.
DR OrthoDB; 961781at2; -.
DR BioCyc; DDAD198628:DDA3937_RS07140-MON; -.
DR Proteomes; UP000006859; 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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004736; MHS_symport.
DR InterPro; IPR015041; Osmo_CC.
DR InterPro; IPR036292; ProP_C.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF08946; Osmo_CC; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR SUPFAM; SSF103661; SSF103661; 1.
DR TIGRFAMs; TIGR00883; 2A0106; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Coiled coil;
KW Membrane; Reference proteome; Stress response; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..501
FT /note="Glycine betaine/proline/ectoine/pipecolic acid
FT transporter OusA"
FT /id="PRO_0000050323"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8550465"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..66
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..122
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..195
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..298
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..350
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..417
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT COILED 461..495
FT /evidence="ECO:0000255"
FT CONFLICT 60
FT /note="Missing (in Ref. 1; CAA57718)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="M -> S (in Ref. 1; CAA57718)"
FT /evidence="ECO:0000305"
FT CONFLICT 79..80
FT /note="IR -> M (in Ref. 1; CAA57718)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..221
FT /note="RHA -> AT (in Ref. 1; CAA57718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 54858 MW; 7493159C53291F66 CRC64;
MKLKRKRVKP IALDDVTIID DGRLRKAITA AALGNAMEWF DFGVYGFVAY ALGQVFFPGA
DPGVQMIAAL ATFSVPFLIR PLGGVFFGAL GDKYGRQKIL AITIIIMSIS TFCIGLIPSY
ERIGIWAPIL LLLAKMAQGF SVGGEYTGAS IFVAEYSPDR KRGFMGSWLD FGSIAGFVLG
AGVVVLISTL IGEQAFLAWG WRLPFFLALP LGLIGLYLRH ALEETPAFRQ HVEKLEQNDR
DGLKAGPGVS FREIATHHWK SLLVCIGLVI ATNVTYYMLL TYMPSYLSHS LHYSENHGVL
IIIAIMIGML FVQPVMGLLS DRFGRKPFVV IGSVAMFFLA VPSFMLINSD IIGLIFLGLL
MLAVILNAFT GVMASTLPAL FPTHIRYSAL ASAFNISVLI AGLTPTVAAW LVESSQNLYM
PAYYLMVIAV IGLLTGLFMK ETANKPLKGA TPAASDLSEA KEILQEHHDN IEHKIEDITQ
QIAELEAKRQ LLVAQHPRIN D
