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Glycine betaine transporter BetL (Glycine betaine-Na( ) symporter)

 BETL_LISMN              Reviewed;         507 AA.
Q9X4A5;
13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
18-JUL-2018, entry version 88.
RecName: Full=Glycine betaine transporter BetL;
AltName: Full=Glycine betaine-Na(+) symporter;
Name=betL;
Listeria monocytogenes.
Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
NCBI_TaxID=1639;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, AND DISRUPTION PHENOTYPE.
STRAIN=LO28 / Serovar 1/2c;
PubMed=10224004;
Sleator R.D., Gahan C.G., Abee T., Hill C.;
"Identification and disruption of BetL, a secondary glycine betaine
transport system linked to the salt tolerance of Listeria
monocytogenes LO28.";
Appl. Environ. Microbiol. 65:2078-2083(1999).
[2]
INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=LO28 / Serovar 1/2c;
PubMed=11016615; DOI=10.1016/S0168-1605(00)00316-0;
Sleator R.D., Gahan C.G.M., O'Driscoll B., Hill C.;
"Analysis of the role of betL in contributing to the growth and
survival of Listeria monocytogenes LO28.";
Int. J. Food Microbiol. 60:261-268(2000).
[3]
FUNCTION, ENZYME REGULATION, AND INDUCTION.
STRAIN=LO28 / Serovar 1/2c;
PubMed=14645273; DOI=10.1128/JB.185.24.7140-7144.2003;
Sleator R.D., Wood J.M., Hill C.;
"Transcriptional regulation and posttranslational activity of the
betaine transporter BetL in Listeria monocytogenes are controlled by
environmental salinity.";
J. Bacteriol. 185:7140-7144(2003).
[4]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=LO28 / Serovar 1/2c;
PubMed=15128551; DOI=10.1128/AEM.70.5.2912-2918.2004;
Wemekamp-Kamphuis H.H., Sleator R.D., Wouters J.A., Hill C., Abee T.;
"Molecular and physiological analysis of the role of osmolyte
transporters BetL, Gbu, and OpuC in growth of Listeria monocytogenes
at low temperatures.";
Appl. Environ. Microbiol. 70:2912-2918(2004).
-!- FUNCTION: High-affinity uptake of glycine betaine, driven by a
sodium-motive force. Involved, with GbuABC and OpuC, in
osmoprotection and cryoprotection of Listeria. Does not mediate
either carnitine or choline uptake. {ECO:0000269|PubMed:10224004,
ECO:0000269|PubMed:14645273, ECO:0000269|PubMed:15128551}.
-!- ENZYME REGULATION: Activated rapidly in response to an osmotic
upshift. {ECO:0000269|PubMed:14645273}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.9 uM for glycine betaine {ECO:0000269|PubMed:10224004};
Vmax=134 nmol/min/mg enzyme {ECO:0000269|PubMed:10224004};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- INDUCTION: Constitutively expressed. Up-regulated in response to
salt stress and cold shock. {ECO:0000269|PubMed:11016615,
ECO:0000269|PubMed:14645273, ECO:0000269|PubMed:15128551}.
-!- DISRUPTION PHENOTYPE: Mutants show a strong decrease in the rate
of glycine betaine uptake. Mutation does not significantly affect
cryoprotection or virulence of the organism, probably due to the
presence of other glycine betaine/carnitine transporters in the
cell. {ECO:0000269|PubMed:10224004, ECO:0000269|PubMed:11016615,
ECO:0000269|PubMed:15128551}.
-!- MISCELLANEOUS: Activation of preexisting BetL protein in response
to relatively low salt concentrations represents the most
immediate response of the cell to increased salinity. GbuABC
system is most important during prolonged exposure
(PubMed:14645273). {ECO:0000305|PubMed:14645273}.
-!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
{ECO:0000305}.
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EMBL; AF102174; AAD30266.1; -; Genomic_DNA.
PIR; AD1336; AD1336.
PIR; T48645; T48645.
RefSeq; WP_003731943.1; NZ_PXXI01000016.1.
ProteinModelPortal; Q9X4A5; -.
SMR; Q9X4A5; -.
TCDB; 2.A.15.1.11; the betaine/carnitine/choline transporter (bcct) family.
eggNOG; ENOG4105C94; Bacteria.
eggNOG; COG1292; LUCA.
HOGENOM; HOG000053240; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0015199; F:amino-acid betaine transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
GO; GO:0031460; P:glycine betaine transport; IMP:UniProtKB.
GO; GO:0009409; P:response to cold; IDA:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
InterPro; IPR018093; BCCT_CS.
InterPro; IPR000060; BCCT_transptr.
PANTHER; PTHR30047; PTHR30047; 1.
Pfam; PF02028; BCCT; 1.
TIGRFAMs; TIGR00842; bcct; 1.
PROSITE; PS01303; BCCT; 1.
1: Evidence at protein level;
Amino-acid transport; Cell membrane; Membrane; Stress response;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 507 Glycine betaine transporter BetL.
/FTId=PRO_0000417961.
TRANSMEM 7 27 Helical. {ECO:0000255}.
TRANSMEM 44 64 Helical. {ECO:0000255}.
TRANSMEM 85 105 Helical. {ECO:0000255}.
TRANSMEM 134 154 Helical. {ECO:0000255}.
TRANSMEM 184 204 Helical. {ECO:0000255}.
TRANSMEM 224 244 Helical. {ECO:0000255}.
TRANSMEM 256 276 Helical. {ECO:0000255}.
TRANSMEM 311 331 Helical. {ECO:0000255}.
TRANSMEM 342 362 Helical. {ECO:0000255}.
TRANSMEM 392 412 Helical. {ECO:0000255}.
TRANSMEM 440 460 Helical. {ECO:0000255}.
TRANSMEM 464 484 Helical. {ECO:0000255}.
SEQUENCE 507 AA; 55273 MW; 1470F1ED7AAB305B CRC64;
MKKLTNVFWG SGFLVLLAVL FGAFLPEQFE TFTNHIQKFL TSNFGWYYLI VVAIIIIFCL
FLVLSPIGSI RLGKPGEEPG YSNKSWFAML FSAGMGIGLV FWGAAEPLSH YAVQAPGGEV
GTQAAMKDAL RYSFFHWGIS AWSIYAIVAL ALAYFKFRKN APGLISATLY PILGKHAKGP
IGQLIDIIAV FATVIGVATT LGLGAQQING GLTYLFGVPN NFTVQFTIIV IVTILFMLSA
MSGLDKGIQL LSNVNIYVAG VLLVLTLILG PTLFIMNNFT NSFGDYLQNI IQMSFQTAPD
APDARKWIDS WTIFYWAWWL SWSPFVGIFI ARISRGRTIR QFLLGVIVLP ALVSVFWFAV
FGGSAIFVEQ HGNSGLSSLA TEQVLFGVFN EFPGGMMLSI VAMILIAVFF ITSADSATFV
LGMQTTGGSL NPPNSVKVTW GLLQAGIASV LLYAGGLTAL QNASIIAAFP FSIVIILMIV
SLFVSLTREQ EKLGLYVRPK KSQRSQL


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