ID   GBUB_LISM4              Reviewed;         282 AA.
AC   Q9RR45; G2K537;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Glycine betaine/carnitine transport permease protein GbuB;
GN   Name=gbuB; OrderedLocusNames=LMRG_02115;
OS   Listeria monocytogenes serotype 1/2a (strain 10403S).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=393133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC   STRAIN=10403S;
RX   PubMed=10473414; DOI=10.1128/aem.65.9.4040-4048.1999;
RA   Ko R., Smith L.T.;
RT   "Identification of an ATP-driven, osmoregulated glycine betaine transport
RT   system in Listeria monocytogenes.";
RL   Appl. Environ. Microbiol. 65:4040-4048(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10403S;
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Borowsky M., Borodovsky M., Young S.K., Zeng Q., Koehrsen M.,
RA   Fitzgerald M., Wiedmann M., Swaminathan B., Lauer P., Portnoy D.,
RA   Cossart P., Buchrieser C., Higgins D., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Borenstein D., Brown A., Chapman S.B., Chen Z.,
RA   Dunbar C.D., Engels R., Freedman E., Gearin G., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Jen D., Larson L.,
RA   Lui A., MacDonald J., Mehta T., Montmayeur A., Neiman D., Park D.,
RA   Pearson M., Priest M., Richards J., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Listeria monocytogenes strain 10403S.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10762257; DOI=10.1128/jb.182.9.2544-2550.2000;
RA   Gerhardt P.N., Tombras Smith L., Smith G.M.;
RT   "Osmotic and chill activation of glycine betaine porter II in Listeria
RT   monocytogenes membrane vesicles.";
RL   J. Bacteriol. 182:2544-2550(2000).
RN   [4]
RP   FUNCTION IN CARNITINE UPTAKE.
RC   STRAIN=10403S;
RX   PubMed=12406761; DOI=10.1128/aem.68.11.5647-5655.2002;
RA   Mendum M.L., Smith L.T.;
RT   "Gbu glycine betaine porter and carnitine uptake in osmotically stressed
RT   Listeria monocytogenes cells.";
RL   Appl. Environ. Microbiol. 68:5647-5655(2002).
RN   [5]
RP   FUNCTION IN GLYCINE BETAINE AND CARNITINE UPTAKE.
RC   STRAIN=10403S;
RX   PubMed=12571024; DOI=10.1128/aem.69.2.1013-1022.2003;
RA   Angelidis A.S., Smith G.M.;
RT   "Three transporters mediate uptake of glycine betaine and carnitine by
RT   Listeria monocytogenes in response to hyperosmotic stress.";
RL   Appl. Environ. Microbiol. 69:1013-1022(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex GbuABC involved in
CC       glycine betaine uptake. Responsible for the translocation of the
CC       substrate across the membrane. Involved, with BetL and OpuC, in
CC       osmoprotection and cryoprotection of Listeria. Can also uptake
CC       carnitine when carnitine is abundant in the growth medium.
CC       {ECO:0000269|PubMed:10473414, ECO:0000269|PubMed:10762257,
CC       ECO:0000269|PubMed:12406761, ECO:0000269|PubMed:12571024}.
CC   -!- ACTIVITY REGULATION: The complex is activated by an osmotic gradient or
CC       by low temperature. {ECO:0000269|PubMed:10762257}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.9 uM for glycine betaine (in the presence of sucrose)
CC         {ECO:0000269|PubMed:10762257};
CC         KM=1.2 uM for glycine betaine (in the presence of KCl)
CC         {ECO:0000269|PubMed:10762257};
CC         Vmax=3730 pmol/min/mg enzyme (in the presence of sucrose)
CC         {ECO:0000269|PubMed:10762257};
CC         Vmax=2200 pmol/min/mg enzyme (in the presence of KCl)
CC         {ECO:0000269|PubMed:10762257};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GbuA),
CC       two transmembrane proteins (GbuB) and a solute-binding protein (GbuC).
CC       {ECO:0000305|PubMed:10473414}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; AF039835; AAD29105.1; -; Genomic_DNA.
DR   EMBL; CP002002; AEO06015.1; -; Genomic_DNA.
DR   PIR; AG1201; AG1201.
DR   RefSeq; WP_003722879.1; NC_017544.1.
DR   AlphaFoldDB; Q9RR45; -.
DR   SMR; Q9RR45; -.
DR   EnsemblBacteria; AEO06015; AEO06015; LMRG_02115.
DR   KEGG; lmt:LMRG_02115; -.
DR   HOGENOM; CLU_028473_1_0_9; -.
DR   OMA; HFNIMDP; -.
DR   SABIO-RK; Q9RR45; -.
DR   Proteomes; UP000001288; 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:0015199; F:amino-acid betaine transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015226; F:carnitine transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   GO; GO:0015879; P:carnitine transport; IDA:UniProtKB.
DR   GO; GO:0031460; P:glycine betaine transport; IDA:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IDA:UniProtKB.
DR   GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Membrane; Stress response;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..282
FT                   /note="Glycine betaine/carnitine transport permease protein
FT                   GbuB"
FT                   /id="PRO_0000417959"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          93..272
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   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