ID   OPUCA_LISM4             Reviewed;         397 AA.
AC   G2JZ44;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Carnitine transport ATP-binding protein OpuCA;
DE            EC=7.6.2.9;
GN   Name=opuCA; OrderedLocusNames=LMRG_00880;
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 energy coupling to the
CC       transport system. Involved, with BetL and GbuABC, in osmoprotection and
CC       cryoprotection of Listeria. Can also mediate weak glycine betaine
CC       transport. {ECO:0000269|PubMed:12039715, ECO:0000269|PubMed:12406761,
CC       ECO:0000269|PubMed:12571024}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + quaternary ammonium(out) = ADP + H(+) + phosphate
CC         + quaternary ammonium(in); Xref=Rhea:RHEA:11036, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:35267,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.6.2.9;
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   -!- 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 ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; CP002002; AEO06413.1; -; Genomic_DNA.
DR   RefSeq; WP_003721933.1; NC_017544.1.
DR   AlphaFoldDB; G2JZ44; -.
DR   SMR; G2JZ44; -.
DR   EnsemblBacteria; AEO06413; AEO06413; LMRG_00880.
DR   KEGG; lmt:LMRG_00880; -.
DR   HOGENOM; CLU_000604_2_2_9; -.
DR   OMA; MYEFNRA; -.
DR   Proteomes; UP000001288; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0015418; F:ABC-type quaternary ammonium compound transporting activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031460; P:glycine betaine transport; IEA:InterPro.
DR   Gene3D; 3.10.580.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005892; Gly-betaine_transp_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF00571; CBS; 2.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   TIGRFAMs; TIGR01186; proV; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; CBS domain; Nucleotide-binding; Repeat; Stress response;
KW   Translocase; Transport.
FT   CHAIN           1..397
FT                   /note="Carnitine transport ATP-binding protein OpuCA"
FT                   /id="PRO_0000418133"
FT   DOMAIN          2..236
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          255..311
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          315..373
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          377..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   397 AA;  45209 MW;  134CF427650AC83B CRC64;
     MLKFEHVTKT YKGGKKAVND LTLNIDKGEF VCFIGPSGCG KTTTMKMINR LIEPTEGKIF
     INDKDIMAED PVKLRRSIGY VIQQIGLMPH MTIRENIVLV PKLLKWSEEK KQERAKELIK
     LVDLPEEFLD RYPYELSGGQ QQRIGVLRAL AAEQNLILMD EPFGALDPIT RDSLQEEFKN
     LQKELGKTII FVTHDMDEAI KLADRIVIMK DGEIVQFDTP DEILRNPANS FVEDFIGKDR
     LIEAKPDVTQ VAQIMNTNPV SITADKSLQA AITVMKEKRV DTLLVVDEGN VLKGFIDVEQ
     IDLNRRTATS VMDIIEKNVF YVYEDTLLRD TVQRILKRGY KYIPVVDKDK RLVGIVTRAS
     LVDIVYDSIW GTLEDATENQ EEQADSKTTE PEMKQEG