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OPUCD_LISMN
ID   OPUCD_LISMN             Reviewed;         223 AA.
AC   Q9KHT6;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Carnitine transport permease protein OpuCD;
GN   Name=opuCD;
OS   Listeria monocytogenes.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1639;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC   STRAIN=EGD / Serotype 1/2a;
RX   PubMed=11055912; DOI=10.1128/aem.66.11.4696-4704.2000;
RA   Fraser K.R., Harvie D., Coote P.J., O'Byrne C.P.;
RT   "Identification and characterization of an ATP binding cassette L-carnitine
RT   transporter in Listeria monocytogenes.";
RL   Appl. Environ. Microbiol. 66:4696-4704(2000).
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.
CC       {ECO:0000269|PubMed:11055912}.
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:11055912}.
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; AF249729; AAF91342.1; -; Genomic_DNA.
DR   PIR; AI1252; AI1252.
DR   RefSeq; WP_003721930.1; NZ_WUEC01000001.1.
DR   AlphaFoldDB; Q9KHT6; -.
DR   SMR; Q9KHT6; -.
DR   STRING; 1027396.LMOSA_23460; -.
DR   eggNOG; COG1174; Bacteria.
DR   OMA; TAYVLQG; -.
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_0000418136"
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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