BETS_RHIML
ID BETS_RHIML Reviewed; 706 AA.
AC G3XCN6;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Glycine betaine/proline betaine transporter BetS {ECO:0000303|PubMed:11976294};
GN Name=betS {ECO:0000303|PubMed:11976294};
GN Synonyms=betP {ECO:0000312|EMBL:AAL37253.1};
OS Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OG Plasmid pSymB (megaplasmid 2) {ECO:0000312|EMBL:AAL37253.1}.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=382;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=102F34; PLASMID=pSymB (megaplasmid 2);
RX PubMed=11976294; DOI=10.1128/jb.184.10.2654-2663.2002;
RA Boscari A., Mandon K., Dupont L., Poggi M.C., Le Rudulier D.;
RT "BetS is a major glycine betaine/proline betaine transporter required for
RT early osmotic adjustment in Sinorhizobium meliloti.";
RL J. Bacteriol. 184:2654-2663(2002).
CC -!- FUNCTION: High-affinity Na(+)-coupled glycine betaine and proline
CC betaine transport. Required for a rapid adaptation to osmotic stress.
CC Does not transport other trimethylammonium or related molecules, such
CC as choline, carnitine and ectoine. {ECO:0000269|PubMed:11976294}.
CC -!- ACTIVITY REGULATION: Uptake is stimulated by high osmolarity.
CC Stimulation is probably due to conformational changes.
CC {ECO:0000269|PubMed:11976294}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for glycine betaine {ECO:0000269|PubMed:11976294};
CC KM=56 uM for proline betaine {ECO:0000269|PubMed:11976294};
CC Vmax=41 nmol/min/mg enzyme with glycine betaine as substrate
CC {ECO:0000269|PubMed:11976294};
CC Vmax=75 nmol/min/mg enzyme with proline betaine as substrate
CC {ECO:0000269|PubMed:11976294};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:11976294}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:11976294}.
CC -!- DISRUPTION PHENOTYPE: Inactivation results in loss of protection by
CC both glycine betaine and proline betaine after an osmotic upshock.
CC {ECO:0000269|PubMed:11976294}.
CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
CC {ECO:0000305}.
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DR EMBL; AF323271; AAL37253.1; -; Genomic_DNA.
DR RefSeq; WP_010975214.1; NZ_PVNM01000297.1.
DR AlphaFoldDB; G3XCN6; -.
DR SMR; G3XCN6; -.
DR SABIO-RK; G3XCN6; -.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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 Amino-acid transport; Cell inner membrane; Cell membrane; Ion transport;
KW Membrane; Plasmid; Sodium; Sodium transport; Stress response;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..706
FT /note="Glycine betaine/proline betaine transporter BetS"
FT /id="PRO_0000435136"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..93
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..180
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..270
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..357
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..441
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..515
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11976294"
SQ SEQUENCE 706 AA; 77603 MW; E1C23CC7DFE6FEDE CRC64;
MQNRVVSCRF TGSTARRATM PEGIRGRSHI LFLVPLSRAE SVGRLHQVQR FKVNLPVFVG
SVAVIALFVG IGVIAPKRAE SIFSGMQTAI LSGFGWLYLL SVAVFLFSML FLAFSRYGEL
KLGPDDSEPE FRYLSWIAML FAAGMGIGLM YFAVGEPMTH FASPPEAEPL TIAAQREAMS
VTFFHWGVHA WAIYSVVGLS LAYFGYRYNL PLTVRSGLYP LLKEGIHGPI GHVVDIFAIC
GTMFGLATSL GFGILQINSG LNYLLGIPQS IYVQLLLVTV VTAIATISVV TGVEKGVRIL
SETNLFLAVL LMLFVLVVGP TGTLMRDFVQ NIGLYLDSLV LRTFNIYAYE PRPWIDSWTL
FYWAWWISWS PFVGMFIARI SRGRTVREFV TAVLFVPAMF TFLWMTVFGN TAIYVDTTIA
NGELARDVKA DLSVALFQFF EYLPWPAVTS TLAVLLVSIF FVTSSDSGSL VIDTIASGGE
TATPALQRIF WCSLSGIVAA VLLSTGGLTA LQSATISTAL PFSLVMLILV WSLFVGMRAD
LARTQSPGSL GPRAYPASGV PWQRRLAMTL STPDRRAVEK FLQASVLPAL EAVARELTRR
SRPASVGRDA ETGALTLTVP AEGHRDFVYG VQMSEHKLPA FTAYDATVAD VRYEARTFFS
DGSRGYDIMG MADNQIINDV LFQFERYTGF VRSPESSLLA TSPEER
