GBUC_LISM4
ID GBUC_LISM4 Reviewed; 300 AA.
AC Q9RR44; G2K538;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Glycine betaine/carnitine transport binding protein GbuC;
DE Flags: Precursor;
GN Name=gbuC; OrderedLocusNames=LMRG_02116;
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, 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. Involved, with BetL and OpuC, in osmoprotection
CC and cryoprotection of Listeria. Can also uptake carnitine when
CC 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 -!- 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:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR EMBL; AF039835; AAD29106.1; -; Genomic_DNA.
DR EMBL; CP002002; AEO06016.1; -; Genomic_DNA.
DR RefSeq; WP_003733788.1; NC_017544.1.
DR AlphaFoldDB; Q9RR44; -.
DR SMR; Q9RR44; -.
DR EnsemblBacteria; AEO06016; AEO06016; LMRG_02116.
DR KEGG; lmt:LMRG_02116; -.
DR HOGENOM; CLU_082654_0_0_9; -.
DR OMA; NTHKAYA; -.
DR Proteomes; UP000001288; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
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 InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
DR Pfam; PF04069; OpuAC; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Signal; Stress response; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..300
FT /note="Glycine betaine/carnitine transport binding protein
FT GbuC"
FT /id="PRO_0000417960"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CONFLICT 266
FT /note="K -> N (in Ref. 1; AAD29106)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 33276 MW; 0EEE78317C41301E CRC64;
MLKKLITTAV LAMLIFTLAA CGTTLAPYDA KKDLGEQINY TITGIDAGAG IMLATQNAIK
DYHLDDDNWQ LQTSSTAAMT STLQKAMKDK RPIVVTGWTP HWMFTKFDLK FLDDPKNVYG
NAENIHTIVR KGLKEDKPSA YQVLDNFFWT AEDMSEVMLE VNDGVDPEEA AKKWIKNNPD
KVAKWTDGVE KVDGDEIKLT YVAWDSEIAS TNVVAEALKQ VGYKPTIQAM EIQPMWASVA
TDAADGMVAA WLPNTSGIYY KDYKGKFEDL GPNLKGAKIG LAVPKYMTNI NSIEDLKTSK
