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OPUCB_LISMN
ID   OPUCB_LISMN             Reviewed;         218 AA.
AC   Q9KHT8;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Carnitine transport permease protein OpuCB;
GN   Name=opuCB;
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; AAF91340.1; -; Genomic_DNA.
DR   PIR; AC1253; AC1253.
DR   RefSeq; WP_003721932.1; NZ_WUEB01000003.1.
DR   AlphaFoldDB; Q9KHT8; -.
DR   SMR; Q9KHT8; -.
DR   STRING; 1027396.LMOSA_23480; -.
DR   eggNOG; COG1174; Bacteria.
DR   OMA; MRYLFTH; -.
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..218
FT                   /note="Carnitine transport permease protein OpuCB"
FT                   /id="PRO_0000418134"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        79..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          19..198
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   218 AA;  23337 MW;  2BF907BD581C67B2 CRC64;
     MDAIVTFFQE NGHNLLVQTW QHLFISLSAV ILGIAVAVPT GILLTRSPKV ANFVIGVVSV
     LQTVPSLAIL AFIIPFLGVG TLPAIIALFI YALLPILRNT FIGVRGVDKN LIESGRGMGM
     TNWQLIVNVE IPNSISVIMA GIRLSAVYVI AWATLASYIG AGGLGDFIFN GLNLYRPDLI
     LGGAIPVTIL ALVVEFALGK LEYRLTPKAI REAREGGE
 
 
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