OUSW_DICD3
ID OUSW_DICD3 Reviewed; 406 AA.
AC E0SCY2; Q71JC9;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Glycine betaine/choline transport system permease protein OusW {ECO:0000305};
GN Name=ousW {ECO:0000303|PubMed:16000740};
GN Synonyms=ousBW {ECO:0000312|EMBL:AAQ06631.1};
GN OrderedLocusNames=Dda3937_00900 {ECO:0000312|EMBL:ADM99773.1};
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, SUBUNIT, INDUCTION, AND
RP 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 [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).
CC -!- FUNCTION: Part of the OusB ABC transporter complex involved in glycine
CC betaine and choline uptake. May also transport several other
CC osmoprotectants such as ectoine, DMSA, DMSP, proline and carnitine.
CC Probably responsible for the translocation of the substrate across the
CC membrane. {ECO:0000269|PubMed:16000740}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (OusV),
CC two transmembrane proteins (OusW) and a solute-binding protein (OusX).
CC {ECO:0000305|PubMed:16000740}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P14176}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by increased medium osmolality. Repressed by glycine
CC betaine. {ECO:0000269|PubMed:16000740}.
CC -!- DISRUPTION PHENOTYPE: Uptake of glycine betaine and choline is
CC completely abolished in the ousA-ousB double mutant.
CC {ECO:0000269|PubMed:16000740}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; AF494101; AAQ06631.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM99773.1; -; Genomic_DNA.
DR RefSeq; WP_013319198.1; NC_014500.1.
DR AlphaFoldDB; E0SCY2; -.
DR SMR; E0SCY2; -.
DR STRING; 198628.Dda3937_00900; -.
DR EnsemblBacteria; ADM99773; ADM99773; Dda3937_00900.
DR GeneID; 9735044; -.
DR KEGG; ddd:Dda3937_00900; -.
DR PATRIC; fig|198628.6.peg.3520; -.
DR eggNOG; COG4176; Bacteria.
DR HOGENOM; CLU_028473_2_2_6; -.
DR OMA; HFNIMDP; -.
DR OrthoDB; 485527at2; -.
DR BioCyc; DDAD198628:DDA3937_RS16725-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:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..406
FT /note="Glycine betaine/choline transport system permease
FT protein OusW"
FT /id="PRO_0000441736"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 194..373
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 206
FT /note="F -> S (in Ref. 1; AAQ06631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 43060 MW; 9E4CA4BCEFE81D48 CRC64;
MTDTTQNPWE EDQAPDQAAA ANHSHAAATS GEHAAAAGSS GTPAQTDPWA ASSSAPAGNT
PAPDNAADAW SNAPPPAASD VHQSAADWLN STPTPTQEHF NLMDPFRHTL VPLDRWVTEG
IDWLVLHFRP LFQGIRVPVD MILTSFQQLL TGLPAPVAIL VFSLLAWQVS SFGMGVATLL
SLVAIGAIGA WSQAMVTLAL VLTALFFCVI IGLPLGIWLA HSDRAARIVR PLLDAMQTTP
AFVYLIPIVM LFGIGNVPGV VVTIIFALPP IIRLTILGIR QVPADLVEAA QSFGASPRQM
LFKVQLPLAM PTIMAGINQT LMLALSMVVI ASMIAVGGLG QMVLRGIGRL DMGLASIGGV
GIVILAIILD RLTQSLGRDA RSRGNRHWYH HGPLGLLARP FIKSRA
