BETP_CORGL
ID BETP_CORGL Reviewed; 595 AA.
AC P54582;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glycine betaine transporter BetP {ECO:0000305};
DE AltName: Full=Glycine betaine permease {ECO:0000303|PubMed:8752342};
GN Name=betP {ECO:0000303|PubMed:8752342}; OrderedLocusNames=Cgl0892, cg1016;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=8752342; DOI=10.1128/jb.178.17.5229-5234.1996;
RA Peter H., Burkovski A., Kraemer R.;
RT "Isolation, characterization, and expression of the Corynebacterium
RT glutamicum betP gene, encoding the transport system for the compatible
RT solute glycine betaine.";
RL J. Bacteriol. 178:5229-5234(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=7642496; DOI=10.1128/jb.177.16.4690-4695.1995;
RA Farwick M., Siewe R.M., Kraemer R.;
RT "Glycine betaine uptake after hyperosmotic shift in Corynebacterium
RT glutamicum.";
RL J. Bacteriol. 177:4690-4695(1995).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, AND DOMAIN.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=9446558; DOI=10.1074/jbc.273.5.2567;
RA Peter H., Burkovski A., Kraemer R.;
RT "Osmo-sensing by N- and C-terminal extensions of the glycine betaine uptake
RT system BetP of Corynebacterium glutamicum.";
RL J. Biol. Chem. 273:2567-2574(1998).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10625602; DOI=10.1074/jbc.275.2.735;
RA Ruebenhagen R., Roensch H., Jung H., Kraemer R., Morbach S.;
RT "Osmosensor and osmoregulator properties of the betaine carrier BetP from
RT Corynebacterium glutamicum in proteoliposomes.";
RL J. Biol. Chem. 275:735-741(2000).
RN [7]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=11574473; DOI=10.1093/emboj/20.19.5412;
RA Ruebenhagen R., Morbach S., Kraemer R.;
RT "The osmoreactive betaine carrier BetP from Corynebacterium glutamicum is a
RT sensor for cytoplasmic K+.";
RL EMBO J. 20:5412-5420(2001).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND DOMAIN.
RX PubMed=15134432; DOI=10.1021/bi0359628;
RA Schiller D., Ruebenhagen R., Kraemer R., Morbach S.;
RT "The C-terminal domain of the betaine carrier BetP of Corynebacterium
RT glutamicum is directly involved in sensing K+ as an osmotic stimulus.";
RL Biochemistry 43:5583-5591(2004).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=15063732; DOI=10.1016/s0014-5793(04)00279-0;
RA Schiller D., Kraemer R., Morbach S.;
RT "Cation specificity of osmosensing by the betaine carrier BetP of
RT Corynebacterium glutamicum.";
RL FEBS Lett. 563:108-112(2004).
RN [10]
RP SUBUNIT.
RX PubMed=15046983; DOI=10.1016/j.jmb.2004.02.026;
RA Ziegler C., Morbach S., Schiller D., Kraemer R., Tziatzios C., Schubert D.,
RA Kuehlbrandt W.;
RT "Projection structure and oligomeric state of the osmoregulated
RT sodium/glycine betaine symporter BetP of Corynebacterium glutamicum.";
RL J. Mol. Biol. 337:1137-1147(2004).
RN [11]
RP ACTIVITY REGULATION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=15995189; DOI=10.1128/jb.187.14.4752-4759.2005;
RA Ozcan N., Kraemer R., Morbach S.;
RT "Chill activation of compatible solute transporters in Corynebacterium
RT glutamicum at the level of transport activity.";
RL J. Bacteriol. 187:4752-4759(2005).
RN [12]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=17390131; DOI=10.1007/s00253-007-0938-4;
RA Weinand M., Kraemer R., Morbach S.;
RT "Characterization of compatible solute transporter multiplicity in
RT Corynebacterium glutamicum.";
RL Appl. Microbiol. Biotechnol. 76:701-708(2007).
RN [13]
RP ACTIVITY REGULATION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=17693504; DOI=10.1128/jb.00986-07;
RA Ozcan N., Ejsing C.S., Shevchenko A., Lipski A., Morbach S., Kraemer R.;
RT "Osmolality, temperature, and membrane lipid composition modulate the
RT activity of betaine transporter BetP in Corynebacterium glutamicum.";
RL J. Bacteriol. 189:7485-7496(2007).
RN [14]
RP SUBUNIT, AND MUTAGENESIS OF TRP-101 AND THR-351.
RX PubMed=21681199; DOI=10.1038/embor.2011.102;
RA Perez C., Khafizov K., Forrest L.R., Kraemer R., Ziegler C.;
RT "The role of trimerization in the osmoregulated betaine transporter BetP.";
RL EMBO Rep. 12:804-810(2011).
RN [15] {ECO:0007744|PDB:2WIT}
RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 30-595 IN COMPLEX WITH GLYCINE
RP BETAINE, FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND MUTAGENESIS OF GLU-135; TRP-189; TRP-194; TYR-197; ARG-210;
RP GLY-301; TRP-362; TRP-366; TRP-371; TRP-374; TRP-377; ARG-387 AND ARG-392.
RX PubMed=19262666; DOI=10.1038/nature07819;
RA Ressl S., Terwisscha van Scheltinga A.C., Vonrhein C., Ott V., Ziegler C.;
RT "Molecular basis of transport and regulation in the Na(+)/betaine symporter
RT BetP.";
RL Nature 458:47-52(2009).
RN [16] {ECO:0007744|PDB:3P03}
RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 30-595 OF MUTANT ASP-153 IN
RP COMPLEX WITH CHOLINE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBUNIT, TOPOLOGY, AND MUTAGENESIS OF GLY-149; GLY-151 AND
RP GLY-153.
RX PubMed=21364531; DOI=10.1038/emboj.2011.46;
RA Perez C., Koshy C., Ressl S., Nicklisch S., Kramer R., Ziegler C.;
RT "Substrate specificity and ion coupling in the Na+/betaine symporter
RT BetP.";
RL EMBO J. 30:1221-1229(2011).
RN [17] {ECO:0007744|PDB:4AIN, ECO:0007744|PDB:4DOJ}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 41-579 IN COMPLEXES WITH GLYCINE
RP BETAINE AND CHOLINE, FUNCTION, SUBUNIT, TOPOLOGY, AND MUTAGENESIS OF
RP PHE-156; PHE-369; TRP-373; TRP-374; TRP-377; PHE-380 AND PHE-384.
RX PubMed=22940865; DOI=10.1038/nature11403;
RA Perez C., Koshy C., Yildiz O., Ziegler C.;
RT "Alternating-access mechanism in conformationally asymmetric trimers of the
RT betaine transporter BetP.";
RL Nature 490:126-130(2012).
RN [18] {ECO:0007744|PDB:4C7R}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 30-595, FUNCTION, ACTIVITY
RP REGULATION, SUBUNIT, TOPOLOGY, AND MUTAGENESIS OF GLY-149; MET-150; ILE-152
RP AND GLY-153.
RX PubMed=24141878; DOI=10.1038/emboj.2013.226;
RA Koshy C., Schweikhard E.S., Gartner R.M., Perez C., Yildiz O., Ziegler C.;
RT "Structural evidence for functional lipid interactions in the betaine
RT transporter BetP.";
RL EMBO J. 32:3096-3105(2013).
RN [19] {ECO:0007744|PDB:4LLH}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 30-595, SUBUNIT, TOPOLOGY, AND
RP MUTAGENESIS OF GLY-153 AND ASN-309.
RX PubMed=25023443; DOI=10.1038/ncomms5231;
RA Perez C., Faust B., Mehdipour A.R., Francesconi K.A., Forrest L.R.,
RA Ziegler C.;
RT "Substrate-bound outward-open state of the betaine transporter BetP
RT provides insights into Na+ coupling.";
RL Nat. Commun. 5:4231-4231(2014).
CC -!- FUNCTION: Involved in response to osmotic stress (PubMed:7642496,
CC PubMed:9446558, PubMed:10625602, PubMed:19262666, PubMed:21364531,
CC PubMed:24141878). High-affinity glycine betaine-specific uptake system,
CC which couples the uptake of glycine betaine to the symport of two Na(+)
CC ions (PubMed:7642496, PubMed:10625602, PubMed:15134432,
CC PubMed:19262666, PubMed:21364531, PubMed:22940865, PubMed:24141878).
CC Transport is driven both by the Na(+) gradient and by the electrical
CC potential (PubMed:7642496, PubMed:10625602). In addition, functions
CC both as an osmosensor and as an osmoregulator that transduces signal to
CC the catalytic part of the carrier protein, which adapts its activity to
CC the extent of osmotic stress (PubMed:9446558, PubMed:10625602,
CC PubMed:11574473). {ECO:0000269|PubMed:10625602,
CC ECO:0000269|PubMed:11574473, ECO:0000269|PubMed:15134432,
CC ECO:0000269|PubMed:19262666, ECO:0000269|PubMed:21364531,
CC ECO:0000269|PubMed:22940865, ECO:0000269|PubMed:24141878,
CC ECO:0000269|PubMed:7642496, ECO:0000269|PubMed:9446558}.
CC -!- ACTIVITY REGULATION: Uptake is activated by hyperosmotic stress
CC (PubMed:7642496, PubMed:9446558, PubMed:10625602, PubMed:15134432,
CC PubMed:19262666, PubMed:21364531, PubMed:24141878). Osmoresponsive
CC activation is triggered by a change in the internal K(+) concentration
CC (PubMed:11574473, PubMed:15063732). In addition, shows a pronounced
CC chill stimulation, at temperatures around 10 degrees Celsius
CC (PubMed:15995189, PubMed:17693504). Chill activation may be influenced
CC by the membrane lipid composition (PubMed:17693504). Uptake is
CC completely abolished by the uncoupler CCCP, and to a different extent
CC by the ionophores valinomycin and nigericin (PubMed:7642496).
CC {ECO:0000269|PubMed:10625602, ECO:0000269|PubMed:11574473,
CC ECO:0000269|PubMed:15063732, ECO:0000269|PubMed:15134432,
CC ECO:0000269|PubMed:15995189, ECO:0000269|PubMed:17693504,
CC ECO:0000269|PubMed:19262666, ECO:0000269|PubMed:21364531,
CC ECO:0000269|PubMed:24141878, ECO:0000269|PubMed:7642496,
CC ECO:0000269|PubMed:9446558}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.6 uM for glycine betaine {ECO:0000269|PubMed:7642496};
CC KM=3.6 uM for glycine betaine {ECO:0000269|PubMed:10625602};
CC KM=3.5 uM for glycine betaine {ECO:0000269|PubMed:21364531};
CC KM=3 uM for glycine betaine {ECO:0000269|PubMed:15134432};
CC KM=4.1 mM for Na(+) {ECO:0000269|PubMed:7642496};
CC KM=15 mM for Na(+) {ECO:0000269|PubMed:10625602};
CC KM=38.1 mM for Na(+) {ECO:0000269|PubMed:15134432};
CC Vmax=110 nmol/min/mg enzyme {ECO:0000269|PubMed:7642496};
CC Vmax=2.3 mmol/min/mg enzyme {ECO:0000269|PubMed:10625602};
CC Vmax=2264 nmol/min/mg enzyme {ECO:0000269|PubMed:21364531};
CC Vmax=1693 nmol/min/mg enzyme {ECO:0000269|PubMed:15134432};
CC pH dependence:
CC Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:7642496};
CC -!- SUBUNIT: Homotrimer (PubMed:15046983, PubMed:21681199, PubMed:19262666,
CC PubMed:21364531, PubMed:22940865, PubMed:24141878, PubMed:25023443).
CC The monomer can accumulate glycine betaine, but trimerization is
CC required to properly respond to osmotic stress (PubMed:21681199).
CC {ECO:0000269|PubMed:15046983, ECO:0000269|PubMed:19262666,
CC ECO:0000269|PubMed:21364531, ECO:0000269|PubMed:21681199,
CC ECO:0000269|PubMed:22940865, ECO:0000269|PubMed:24141878,
CC ECO:0000269|PubMed:25023443}.
CC -!- INTERACTION:
CC P54582; P54582: betP; NbExp=14; IntAct=EBI-6985171, EBI-6985171;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:17390131,
CC ECO:0000269|PubMed:19262666}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19262666, ECO:0000269|PubMed:21364531,
CC ECO:0000269|PubMed:22940865, ECO:0000269|PubMed:24141878,
CC ECO:0000269|PubMed:25023443}.
CC -!- INDUCTION: Constitutively expressed at a basal level of activity
CC (PubMed:7642496). Induced upon hyperosmotic conditions, resulting in an
CC increase of its transport activity (PubMed:7642496, PubMed:17390131).
CC {ECO:0000269|PubMed:17390131, ECO:0000269|PubMed:7642496}.
CC -!- DOMAIN: Contains a negatively charged N-terminus and a positively
CC charged C-terminus, which are both involved in sensing and/or
CC transducing osmotic changes to the domain responsible for the
CC translocation of the substrate glycine betaine (PubMed:9446558). The C-
CC terminal domain is directly involved in K(+) sensing or K(+)-dependent
CC activation of BetP (PubMed:15134432). {ECO:0000269|PubMed:15134432,
CC ECO:0000269|PubMed:9446558}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows strongly decreased glycine betaine
CC uptake. {ECO:0000269|PubMed:8752342}.
CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
CC {ECO:0000305}.
CC -!- CAUTION: Binds 2 Na(+), but the precise binding sites are still
CC uncertain and may change during the transport cycle.
CC {ECO:0000305|PubMed:19262666, ECO:0000305|PubMed:22940865,
CC ECO:0000305|PubMed:25023443}.
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DR EMBL; X93514; CAA63771.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98285.1; -; Genomic_DNA.
DR EMBL; BX927150; CAF19598.1; -; Genomic_DNA.
DR RefSeq; NP_600119.1; NC_003450.3.
DR RefSeq; WP_011265645.1; NC_006958.1.
DR PDB; 2WIT; X-ray; 3.35 A; A/B/C=30-595.
DR PDB; 3P03; X-ray; 3.35 A; A/B/C=30-595.
DR PDB; 4AIN; X-ray; 3.10 A; A/B/C=41-579.
DR PDB; 4C7R; X-ray; 2.70 A; A/B/C=30-595.
DR PDB; 4DOJ; X-ray; 3.25 A; A/B/C=30-595.
DR PDB; 4LLH; X-ray; 2.80 A; A/B/C=30-595.
DR PDBsum; 2WIT; -.
DR PDBsum; 3P03; -.
DR PDBsum; 4AIN; -.
DR PDBsum; 4C7R; -.
DR PDBsum; 4DOJ; -.
DR PDBsum; 4LLH; -.
DR AlphaFoldDB; P54582; -.
DR SMR; P54582; -.
DR DIP; DIP-59738N; -.
DR MINT; P54582; -.
DR STRING; 196627.cg1016; -.
DR TCDB; 2.A.15.1.10; the betaine/carnitine/choline transporter (bcct) family.
DR KEGG; cgb:cg1016; -.
DR KEGG; cgl:Cgl0892; -.
DR PATRIC; fig|196627.13.peg.875; -.
DR eggNOG; COG1292; Bacteria.
DR HOGENOM; CLU_010118_4_0_11; -.
DR OMA; VHAWAIY; -.
DR EvolutionaryTrace; P54582; -.
DR Proteomes; UP000000582; 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0071705; P:nitrogen compound transport; IEA:InterPro.
DR InterPro; IPR018093; BCCT_CS.
DR InterPro; IPR000060; BCCT_transptr.
DR PANTHER; PTHR30047; PTHR30047; 1.
DR Pfam; PF02028; BCCT; 1.
DR TIGRFAMs; TIGR00842; bcct; 1.
DR PROSITE; PS01303; BCCT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; Metal-binding;
KW Reference proteome; Sodium; Stress response; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..595
FT /note="Glycine betaine transporter BetP"
FT /id="PRO_0000201483"
FT TOPO_DOM 1..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9446558"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 81..98
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 120..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 159..185
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 207..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 258..276
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 277..296
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 297..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 300..323
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 324..365
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 387..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 418..451
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 452..476
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 477..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 511..520
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24141878"
FT TOPO_DOM 542..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9446558"
FT REGION 570..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..595
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:19262666,
FT ECO:0000305|PubMed:22940865, ECO:0000305|PubMed:25023443"
FT BINDING 148
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:19262666"
FT BINDING 150
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:19262666,
FT ECO:0000305|PubMed:22940865, ECO:0000305|PubMed:25023443"
FT BINDING 152..153
FT /ligand="glycine betaine"
FT /ligand_id="ChEBI:CHEBI:17750"
FT /evidence="ECO:0000269|PubMed:22940865,
FT ECO:0007744|PDB:4AIN"
FT BINDING 253
FT /ligand="glycine betaine"
FT /ligand_id="ChEBI:CHEBI:17750"
FT /evidence="ECO:0000269|PubMed:22940865,
FT ECO:0007744|PDB:4AIN"
FT BINDING 306
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:19262666"
FT BINDING 310
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:19262666"
FT BINDING 373..377
FT /ligand="glycine betaine"
FT /ligand_id="ChEBI:CHEBI:17750"
FT /evidence="ECO:0000269|PubMed:19262666,
FT ECO:0000269|PubMed:22940865, ECO:0007744|PDB:4AIN"
FT MUTAGEN 101
FT /note="W->A: Mainly monomeric, shows a decrease in activity
FT and cannot be activated in response to increased
FT osmolality; when associated with A-351."
FT /evidence="ECO:0000269|PubMed:21681199"
FT MUTAGEN 135
FT /note="E->A: Strongly decreased betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 149
FT /note="G->A: Decreases betaine transport. No effect on
FT activation by increased osmolality."
FT /evidence="ECO:0000269|PubMed:21364531,
FT ECO:0000269|PubMed:24141878"
FT MUTAGEN 150
FT /note="M->F: No effect on activation by increased
FT osmolality; when associated with A-152."
FT /evidence="ECO:0000269|PubMed:24141878"
FT MUTAGEN 151
FT /note="G->A: Nearly abolishes betaine transport."
FT /evidence="ECO:0000269|PubMed:21364531"
FT MUTAGEN 152
FT /note="I->A: No effect on activation by increased
FT osmolality; when associated with F-150."
FT /evidence="ECO:0000269|PubMed:24141878"
FT MUTAGEN 153
FT /note="G->A: Decreases betaine transport and alters
FT activation at higher osmolality."
FT /evidence="ECO:0000269|PubMed:21364531,
FT ECO:0000269|PubMed:24141878"
FT MUTAGEN 153
FT /note="G->D: Changes substrate specificity, giving rise to
FT proton-coupled choline transport. Decreases sodium-
FT dependent betaine transport."
FT /evidence="ECO:0000269|PubMed:21364531,
FT ECO:0000269|PubMed:25023443"
FT MUTAGEN 156
FT /note="F->A: Decreases betaine transport, but has no major
FT effect on affinity for glycine betaine."
FT /evidence="ECO:0000269|PubMed:22940865"
FT MUTAGEN 189
FT /note="W->C: Mildly decreased betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 194
FT /note="W->L: Strongly decreased betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 197
FT /note="Y->L: Nearly abolishes betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 210
FT /note="R->A: Nearly abolishes betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 301
FT /note="G->L: Strongly decreased betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 309
FT /note="N->A: Decreases affinity for sodium ions."
FT /evidence="ECO:0000269|PubMed:25023443"
FT MUTAGEN 351
FT /note="T->A: Mainly trimeric, but shows reduced activity at
FT high osmolalities. Mainly monomeric, shows a decrease in
FT activity and cannot be activated in response to increased
FT osmolality; when associated with A-101."
FT /evidence="ECO:0000269|PubMed:21681199"
FT MUTAGEN 362
FT /note="W->C: Strongly decreased betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 366
FT /note="W->C: No effect on betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 369
FT /note="F->G: Decreases affinity for glycine betaine.
FT Decreases betaine transport."
FT /evidence="ECO:0000269|PubMed:22940865"
FT MUTAGEN 371
FT /note="W->L: No effect on betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 373
FT /note="W->A: Strongly decreases affinity for glycine
FT betaine and betaine transport."
FT /evidence="ECO:0000269|PubMed:22940865"
FT MUTAGEN 374
FT /note="W->A: Strongly decreases betaine transport, but has
FT no major effect on affinity for glycine betaine."
FT /evidence="ECO:0000269|PubMed:22940865"
FT MUTAGEN 374
FT /note="W->L: No effect on betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 377
FT /note="W->A: Abolishes betaine transport."
FT /evidence="ECO:0000269|PubMed:22940865"
FT MUTAGEN 377
FT /note="W->L: Nearly abolishes betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 380
FT /note="F->A: Decreases betaine transport, but has no effect
FT on affinity for glycine betaine."
FT /evidence="ECO:0000269|PubMed:22940865"
FT MUTAGEN 384
FT /note="F->A: Decreases betaine transport, but has no effect
FT on affinity for glycine betaine."
FT /evidence="ECO:0000269|PubMed:22940865"
FT MUTAGEN 387
FT /note="R->A: Mildly decreased betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT MUTAGEN 392
FT /note="R->K: Moderately decreased betaine transport."
FT /evidence="ECO:0000269|PubMed:19262666"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:4AIN"
FT HELIX 60..79
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 81..98
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 100..119
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:4C7R"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 191..209
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 233..265
FT /evidence="ECO:0007829|PDB:4C7R"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 276..291
FT /evidence="ECO:0007829|PDB:4C7R"
FT TURN 292..296
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 298..323
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 326..348
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:4C7R"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 367..376
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 394..425
FT /evidence="ECO:0007829|PDB:4C7R"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 436..445
FT /evidence="ECO:0007829|PDB:4C7R"
FT TURN 448..452
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 453..478
FT /evidence="ECO:0007829|PDB:4C7R"
FT TURN 479..483
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 489..510
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 514..524
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 527..545
FT /evidence="ECO:0007829|PDB:4C7R"
FT HELIX 548..582
FT /evidence="ECO:0007829|PDB:4C7R"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:4C7R"
SQ SEQUENCE 595 AA; 64209 MW; 8354B41C834CEFE2 CRC64;
MTTSDPNPKP IVEDAQPEQI TATEELAGLL ENPTNLEGKL ADAEEEIILE GEDTQASLNW
SVIVPALVIV LATVVWGIGF KDSFTNFASS ALSAVVDNLG WAFILFGTVF VFFIVVIAAS
KFGTIRLGRI DEAPEFRTVS WISMMFAAGM GIGLMFYGTT EPLTFYRNGV PGHDEHNVGV
AMSTTMFHWT LHPWAIYAIV GLAIAYSTFR VGRKQLLSSA FVPLIGEKGA EGWLGKLIDI
LAIIATVFGT ACSLGLGALQ IGAGLSAANI IEDPSDWTIV GIVSVLTLAF IFSAISGVGK
GIQYLSNANM VLAALLAIFV FVVGPTVSIL NLLPGSIGNY LSNFFQMAGR TAMSADGTAG
EWLGSWTIFY WAWWISWSPF VGMFLARISR GRSIREFILG VLLVPAGVST VWFSIFGGTA
IVFEQNGESI WGDGAAEEQL FGLLHALPGG QIMGIIAMIL LGTFFITSAD SASTVMGTMS
QHGQLEANKW VTAAWGVATA AIGLTLLLSG GDNALSNLQN VTIVAATPFL FVVIGLMFAL
VKDLSNDVIY LEYREQQRFN ARLARERRVH NEHRKRELAA KRRRERKASG AGKRR
