ID   GBUA_LISM4              Reviewed;         397 AA.
AC   Q9RR46; G2K536;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Glycine betaine/carnitine transport ATP-binding protein GbuA;
DE            EC=7.6.2.9;
GN   Name=gbuA; OrderedLocusNames=LMRG_02114;
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, SUBUNIT, AND DISRUPTION
RP   PHENOTYPE.
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, AND ACTIVITY REGULATION.
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 energy coupling to the
CC       transport system. Involved, with BetL and OpuC, in osmoprotection and
CC       cryoprotection of Listeria. Can also uptake carnitine when carnitine is
CC       abundant in the growth medium. {ECO:0000269|PubMed:10473414,
CC       ECO:0000269|PubMed:10762257, ECO:0000269|PubMed:12406761,
CC       ECO:0000269|PubMed:12571024}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + quaternary ammonium(out) = ADP + H(+) + phosphate
CC         + quaternary ammonium(in); Xref=Rhea:RHEA:11036, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:35267,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.6.2.9;
CC   -!- ACTIVITY REGULATION: The complex is activated by an osmotic gradient or
CC       by low temperature. {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   -!- DISRUPTION PHENOTYPE: Mutants are impaired in the transport of glycine
CC       betaine at elevated osmolarity and at decreased temperature.
CC       {ECO:0000269|PubMed:10473414}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AF039835; AAD29104.1; -; Genomic_DNA.
DR   EMBL; CP002002; AEO06014.1; -; Genomic_DNA.
DR   PIR; AF1201; AF1201.
DR   RefSeq; WP_003722878.1; NC_017544.1.
DR   AlphaFoldDB; Q9RR46; -.
DR   SMR; Q9RR46; -.
DR   EnsemblBacteria; AEO06014; AEO06014; LMRG_02114.
DR   GeneID; 67409290; -.
DR   KEGG; lmt:LMRG_02114; -.
DR   HOGENOM; CLU_000604_2_0_9; -.
DR   OMA; GQIFVVM; -.
DR   Proteomes; UP000001288; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0031459; F:ABC-type glycine betaine transporter activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   Gene3D; 3.10.580.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005892; Gly-betaine_transp_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF00571; CBS; 2.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   TIGRFAMs; TIGR01186; proV; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   Amino-acid transport; ATP-binding; CBS domain; Nucleotide-binding; Repeat;
KW   Stress response; Translocase; Transport.
FT   CHAIN           1..397
FT                   /note="Glycine betaine/carnitine transport ATP-binding
FT                   protein GbuA"
FT                   /id="PRO_0000417958"
FT   DOMAIN          28..264
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          279..335
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          340..395
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   397 AA;  43626 MW;  50D99F8625625434 CRC64;
     MSKIKVEELT KIFGKKASKA SSLLSQGKSK TDILKETGAT IGVNKASFSV EEGEIFVIMG
     LSGSGKSTLV RLLNRLIEPT SGKIWLDGKE LSSLNKKELL EVRRKSMSMV FQNFGLFPNR
     TINRNVEYGL EIQGMDKEER EKNAAESLAL VGLAGYGDQY PSQLSGGMQQ RVGLARALAN
     NPDILLMDEA FSALDPLNRK DMQDQLLDLQ DKMKKTIIFI THDLDEALRI GDHIMIMRDG
     SVVQTGSPEE ILAHPANEYV EKFIEDVDRS KVYTASNVMI RPEIVNFEKD GPRVALKRMR
     EAGTSSVFVV KRNRELVGIV HAAEVSKLVK ENITSLETAL HRDVPTTGLD TPLAEIMDTI
     STTTIPIAVT EDGKLKGIII RGSVLAALSG NEVNVNA