BETL_LISMN
ID BETL_LISMN Reviewed; 507 AA.
AC Q9X4A5;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Glycine betaine transporter BetL;
DE AltName: Full=Glycine betaine-Na(+) symporter;
GN Name=betL;
OS Listeria monocytogenes.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1639;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=10224004; DOI=10.1128/aem.65.5.2078-2083.1999;
RA Sleator R.D., Gahan C.G., Abee T., Hill C.;
RT "Identification and disruption of BetL, a secondary glycine betaine
RT transport system linked to the salt tolerance of Listeria monocytogenes
RT LO28.";
RL Appl. Environ. Microbiol. 65:2078-2083(1999).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=11016615; DOI=10.1016/s0168-1605(00)00316-0;
RA Sleator R.D., Gahan C.G.M., O'Driscoll B., Hill C.;
RT "Analysis of the role of betL in contributing to the growth and survival of
RT Listeria monocytogenes LO28.";
RL Int. J. Food Microbiol. 60:261-268(2000).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND INDUCTION.
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=14645273; DOI=10.1128/jb.185.24.7140-7144.2003;
RA Sleator R.D., Wood J.M., Hill C.;
RT "Transcriptional regulation and posttranslational activity of the betaine
RT transporter BetL in Listeria monocytogenes are controlled by environmental
RT salinity.";
RL J. Bacteriol. 185:7140-7144(2003).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=15128551; DOI=10.1128/aem.70.5.2912-2918.2004;
RA Wemekamp-Kamphuis H.H., Sleator R.D., Wouters J.A., Hill C., Abee T.;
RT "Molecular and physiological analysis of the role of osmolyte transporters
RT BetL, Gbu, and OpuC in growth of Listeria monocytogenes at low
RT temperatures.";
RL Appl. Environ. Microbiol. 70:2912-2918(2004).
CC -!- FUNCTION: High-affinity uptake of glycine betaine, driven by a sodium-
CC motive force. Involved, with GbuABC and OpuC, in osmoprotection and
CC cryoprotection of Listeria. Does not mediate either carnitine or
CC choline uptake. {ECO:0000269|PubMed:10224004,
CC ECO:0000269|PubMed:14645273, ECO:0000269|PubMed:15128551}.
CC -!- ACTIVITY REGULATION: Activated rapidly in response to an osmotic
CC upshift. {ECO:0000269|PubMed:14645273}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.9 uM for glycine betaine {ECO:0000269|PubMed:10224004};
CC Vmax=134 nmol/min/mg enzyme {ECO:0000269|PubMed:10224004};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed. Up-regulated in response to salt
CC stress and cold shock. {ECO:0000269|PubMed:11016615,
CC ECO:0000269|PubMed:14645273, ECO:0000269|PubMed:15128551}.
CC -!- DISRUPTION PHENOTYPE: Mutants show a strong decrease in the rate of
CC glycine betaine uptake. Mutation does not significantly affect
CC cryoprotection or virulence of the organism, probably due to the
CC presence of other glycine betaine/carnitine transporters in the cell.
CC {ECO:0000269|PubMed:10224004, ECO:0000269|PubMed:11016615,
CC ECO:0000269|PubMed:15128551}.
CC -!- MISCELLANEOUS: Activation of preexisting BetL protein in response to
CC relatively low salt concentrations represents the most immediate
CC response of the cell to increased salinity. GbuABC system is most
CC important during prolonged exposure (PubMed:14645273).
CC {ECO:0000305|PubMed:14645273}.
CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF102174; AAD30266.1; -; Genomic_DNA.
DR PIR; AD1336; AD1336.
DR PIR; T48645; T48645.
DR RefSeq; WP_003731943.1; NZ_WUEC01000003.1.
DR AlphaFoldDB; Q9X4A5; -.
DR SMR; Q9X4A5; -.
DR STRING; 1027396.LMOSA_790; -.
DR TCDB; 2.A.15.1.11; the betaine/carnitine/choline transporter (bcct) family.
DR eggNOG; COG1292; Bacteria.
DR OMA; VHAWAIY; -.
DR SABIO-RK; Q9X4A5; -.
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:0015199; F:amino-acid betaine transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0031460; P:glycine betaine transport; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IDA:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
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 membrane; Membrane; Stress response;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..507
FT /note="Glycine betaine transporter BetL"
FT /id="PRO_0000417961"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ 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
