ID   Y367_LISIN              Reviewed;         113 AA.
AC   Q92EU1;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Putative glycerol transporter Lin0367 {ECO:0000305|PubMed:22773791};
GN   OrderedLocusNames=lin0367 {ECO:0000312|EMBL:CAC95600.1};
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=22773791; DOI=10.1128/jb.00801-12;
RA   Monniot C., Zebre A.C., Ake F.M., Deutscher J., Milohanic E.;
RT   "Novel listerial glycerol dehydrogenase- and phosphoenolpyruvate-dependent
RT   dihydroxyacetone kinase system connected to the pentose phosphate
RT   pathway.";
RL   J. Bacteriol. 194:4972-4982(2012).
CC   -!- FUNCTION: Could be involved in the glycerol uptake either via
CC       facilitated diffusion or active transport.
CC       {ECO:0000305|PubMed:22773791}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Repressed by GolR. {ECO:0000269|PubMed:22773791}.
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DR   EMBL; AL596164; CAC95600.1; -; Genomic_DNA.
DR   PIR; AH1478; AH1478.
DR   RefSeq; WP_003729093.1; NC_003212.1.
DR   AlphaFoldDB; Q92EU1; -.
DR   STRING; 272626.lin0367; -.
DR   EnsemblBacteria; CAC95600; CAC95600; CAC95600.
DR   GeneID; 61169374; -.
DR   KEGG; lin:lin0367; -.
DR   eggNOG; ENOG5032T9Q; Bacteria.
DR   HOGENOM; CLU_149873_0_0_9; -.
DR   OMA; IGMIINA; -.
DR   OrthoDB; 2068744at2; -.
DR   Proteomes; UP000002513; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Glycerol metabolism; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..113
FT                   /note="Putative glycerol transporter Lin0367"
FT                   /id="PRO_0000439495"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   113 AA;  11686 MW;  3FD41E161A36AF99 CRC64;
     MSIGIALATI AGGFLFPFAI RMMWGKMVDE WGAIGGWMAA AFIVGTVWTI NHGIPKSMIY
     QSGTVWVDMA VAAGIGVFTA SLLTGGKFSK SVVNLAAAVV GGVLGGFLLS LFL