OPUCB_LISM4
ID OPUCB_LISM4 Reviewed; 218 AA.
AC G2JZ43;
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 OpuCB;
GN Name=opuCB; OrderedLocusNames=LMRG_00879;
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, SUBUNIT, AND DISRUPTION PHENOTYPE.
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 -!- DISRUPTION PHENOTYPE: Mutants are impaired in both chill-activated and
CC osmotically activated carnitine transport.
CC {ECO:0000269|PubMed:12039715}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; CP002002; AEO06412.1; -; Genomic_DNA.
DR RefSeq; WP_003721932.1; NC_017544.1.
DR AlphaFoldDB; G2JZ43; -.
DR SMR; G2JZ43; -.
DR EnsemblBacteria; AEO06412; AEO06412; LMRG_00879.
DR KEGG; lmt:LMRG_00879; -.
DR HOGENOM; CLU_046113_7_2_9; -.
DR OMA; MRYLFTH; -.
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..218
FT /note="Carnitine transport permease protein OpuCB"
FT /id="PRO_0000418135"
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
