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Glycine betaine/carnitine transport permease protein GbuB

 GBUB_LISM4              Reviewed;         282 AA.
Q9RR45; G2K537;
13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-SEP-2018, entry version 103.
RecName: Full=Glycine betaine/carnitine transport permease protein GbuB;
Name=gbuB; OrderedLocusNames=LMRG_02115;
Listeria monocytogenes serotype 1/2a (strain 10403S).
Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
NCBI_TaxID=393133;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
STRAIN=10403S;
PubMed=10473414;
Ko R., Smith L.T.;
"Identification of an ATP-driven, osmoregulated glycine betaine
transport system in Listeria monocytogenes.";
Appl. Environ. Microbiol. 65:4040-4048(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=10403S;
The Broad Institute Genome Sequencing Platform;
The Broad Institute Genome Sequencing Center for Infectious Disease;
Borowsky M., Borodovsky M., Young S.K., Zeng Q., Koehrsen M.,
Fitzgerald M., Wiedmann M., Swaminathan B., Lauer P., Portnoy D.,
Cossart P., Buchrieser C., Higgins D., Abouelleil A., Alvarado L.,
Arachchi H.M., Berlin A., Borenstein D., Brown A., Chapman S.B.,
Chen Z., Dunbar C.D., Engels R., Freedman E., Gearin G., Gellesch M.,
Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
Jen D., Larson L., Lui A., MacDonald J., Mehta T., Montmayeur A.,
Neiman D., Park D., Pearson M., Priest M., Richards J., Roberts A.,
Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
White J., Yandava C., Haas B., Nusbaum C., Birren B.;
"The genome sequence of Listeria monocytogenes strain 10403S.";
Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10762257; DOI=10.1128/JB.182.9.2544-2550.2000;
Gerhardt P.N., Tombras Smith L., Smith G.M.;
"Osmotic and chill activation of glycine betaine porter II in Listeria
monocytogenes membrane vesicles.";
J. Bacteriol. 182:2544-2550(2000).
[4]
FUNCTION IN CARNITINE UPTAKE.
STRAIN=10403S;
PubMed=12406761; DOI=10.1128/AEM.68.11.5647-5655.2002;
Mendum M.L., Smith L.T.;
"Gbu glycine betaine porter and carnitine uptake in osmotically
stressed Listeria monocytogenes cells.";
Appl. Environ. Microbiol. 68:5647-5655(2002).
[5]
FUNCTION IN GLYCINE BETAINE AND CARNITINE UPTAKE.
STRAIN=10403S;
PubMed=12571024; DOI=10.1128/AEM.69.2.1013-1022.2003;
Angelidis A.S., Smith G.M.;
"Three transporters mediate uptake of glycine betaine and carnitine by
Listeria monocytogenes in response to hyperosmotic stress.";
Appl. Environ. Microbiol. 69:1013-1022(2003).
-!- FUNCTION: Part of the ABC transporter complex GbuABC involved in
glycine betaine uptake. Responsible for the translocation of the
substrate across the membrane. Involved, with BetL and OpuC, in
osmoprotection and cryoprotection of Listeria. Can also uptake
carnitine when carnitine is abundant in the growth medium.
{ECO:0000269|PubMed:10473414, ECO:0000269|PubMed:10762257,
ECO:0000269|PubMed:12406761, ECO:0000269|PubMed:12571024}.
-!- ACTIVITY REGULATION: The complex is activated by an osmotic
gradient or by low temperature. {ECO:0000269|PubMed:10762257}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.9 uM for glycine betaine (in the presence of sucrose)
{ECO:0000269|PubMed:10762257};
KM=1.2 uM for glycine betaine (in the presence of KCl)
{ECO:0000269|PubMed:10762257};
Vmax=3730 pmol/min/mg enzyme (in the presence of sucrose)
{ECO:0000269|PubMed:10762257};
Vmax=2200 pmol/min/mg enzyme (in the presence of KCl)
{ECO:0000269|PubMed:10762257};
-!- SUBUNIT: The complex is composed of two ATP-binding proteins
(GbuA), two transmembrane proteins (GbuB) and a solute-binding
protein (GbuC). {ECO:0000305|PubMed:10473414}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
-!- SIMILARITY: Belongs to the binding-protein-dependent transport
system permease family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF039835; AAD29105.1; -; Genomic_DNA.
EMBL; CP002002; AEO06015.1; -; Genomic_DNA.
PIR; AG1201; AG1201.
RefSeq; WP_003722879.1; NC_017544.1.
ProteinModelPortal; Q9RR45; -.
EnsemblBacteria; AEO06015; AEO06015; LMRG_02115.
KEGG; lmt:LMRG_02115; -.
HOGENOM; HOG000279300; -.
KO; K02001; -.
OMA; LDMGLAS; -.
Proteomes; UP000001288; Chromosome.
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; IDA:UniProtKB.
GO; GO:0015226; F:carnitine transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
GO; GO:0015879; P:carnitine transport; IDA:UniProtKB.
GO; GO:0031460; P:glycine betaine transport; IDA:UniProtKB.
GO; GO:0009409; P:response to cold; IDA:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
CDD; cd06261; TM_PBP2; 1.
Gene3D; 1.10.3720.10; -; 1.
InterPro; IPR000515; MetI-like.
InterPro; IPR035906; MetI-like_sf.
Pfam; PF00528; BPD_transp_1; 1.
SUPFAM; SSF161098; SSF161098; 1.
PROSITE; PS50928; ABC_TM1; 1.
1: Evidence at protein level;
Amino-acid transport; Cell membrane; Complete proteome; Membrane;
Stress response; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 282 Glycine betaine/carnitine transport
permease protein GbuB.
/FTId=PRO_0000417959.
TRANSMEM 44 64 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 70 90 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 99 119 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 140 160 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 220 240 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 251 271 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
DOMAIN 93 272 ABC transmembrane type-1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
SEQUENCE 282 AA; 30919 MW; 80FFBE75AEE835C0 CRC64;
MPNIPTIPLA SWIDKLVDGL TQFEGFFNVI TNIIGGIVDA FQWVFDLVPP WLFIILLVFG
TFWVNRKGKK WGLIIFEVVG LLLIWNLDFW RDMTQTLTLV LTSSLIALVI GVPLGIWMAK
SNIVESIFKP VLDFMQTMPA FVYLIPAVAF FGIGMVPGVV ASVIFAMPPT VRMTNLGIRQ
VSTELVEAAD SFGSTPWQKL WKVQLPMAKS TMMAGINQSI MLALSMVVIA SMIGAMGLGT
RVYFAVGRND AGGGFVAGIA IVIVAIILDR LTQAFNKKAK SE


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