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OPUCD_LISM4
ID   OPUCD_LISM4             Reviewed;         223 AA.
AC   G2JZ41;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Carnitine transport permease protein OpuCD;
GN   Name=opuCD; OrderedLocusNames=LMRG_00877;
OS   Listeria monocytogenes serotype 1/2a (strain 10403S).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=393133;
RN   [1]
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   [2]
RP   FUNCTION, INDUCTION, AND SUBUNIT.
RC   STRAIN=10403S;
RX   PubMed=12039715; DOI=10.1128/aem.68.6.2644-2650.2002;
RA   Angelidis A.S., Smith L.T., Hoffman L.M., Smith G.M.;
RT   "Identification of opuC as a chill-activated and osmotically activated
RT   carnitine transporter in Listeria monocytogenes.";
RL   Appl. Environ. Microbiol. 68:2644-2650(2002).
RN   [3]
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   [4]
RP   FUNCTION IN CARNITINE AND GLYCINE BETAINE UPTAKE, AND INDUCTION.
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).
RN   [5]
RP   INDUCTION.
RC   STRAIN=10403S;
RX   PubMed=12676677; DOI=10.1128/aem.69.4.2015-2022.2003;
RA   Fraser K.R., Sue D., Wiedmann M., Boor K., O'Byrne C.P.;
RT   "Role of sigmaB in regulating the compatible solute uptake systems of
RT   Listeria monocytogenes: osmotic induction of opuC is sigmaB dependent.";
RL   Appl. Environ. Microbiol. 69:2015-2022(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex OpuCABCD involved in
CC       carnitine uptake. Probably responsible for the translocation of the
CC       substrate across the membrane. Involved, with BetL and GbuABC, in
CC       osmoprotection and cryoprotection of Listeria. Can also mediate weak
CC       glycine betaine transport. {ECO:0000269|PubMed:12039715,
CC       ECO:0000269|PubMed:12406761, ECO:0000269|PubMed:12571024}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (OpuCA),
CC       two transmembrane proteins (OpuCB and OpuCD) and a solute-binding
CC       protein (OpuCC). {ECO:0000305|PubMed:12039715}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- INDUCTION: The complex is induced by either hyperosmotic stress or by
CC       low temperature. Osmotic induction is sigma B-dependent.
CC       {ECO:0000269|PubMed:12039715, ECO:0000269|PubMed:12571024,
CC       ECO:0000269|PubMed:12676677}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; CP002002; AEO06410.1; -; Genomic_DNA.
DR   RefSeq; WP_003721930.1; NC_017544.1.
DR   AlphaFoldDB; G2JZ41; -.
DR   SMR; G2JZ41; -.
DR   EnsemblBacteria; AEO06410; AEO06410; LMRG_00877.
DR   KEGG; lmt:LMRG_00877; -.
DR   HOGENOM; CLU_046113_7_2_9; -.
DR   OMA; TAYVLQG; -.
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:0055085; P:transmembrane transport; IEA:InterPro.
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   Cell membrane; Membrane; Stress response; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..223
FT                   /note="Carnitine transport permease protein OpuCD"
FT                   /id="PRO_0000418137"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          22..202
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   223 AA;  23983 MW;  708253B3F2276923 CRC64;
     MDTLKQLIDY YQTNGSYVME EFWRHFLMSA YGVIFAAIIA IPLGVYIARK KRLAGWVIQI
     ANIIQTIPAL AMLAVLMLIM GLGTNTVVLS LFLYSLLPIL KNTYTGIRNV DGALLESGKA
     MGMTKWQVLR LIEMPLALSV IMAGIRNALV IAIGVAAIGT FVGAGGLGDI IVRGTNATNG
     TAIILAGAIP TAVMAILADV LLGWVERTLN PVKNKRKPLT EAL
 
 
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