ID   OPUCA_BACSU             Reviewed;         380 AA.
AC   O34992;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Glycine betaine/carnitine/choline transport ATP-binding protein OpuCA;
GN   Name=opuCA; Synonyms=yvbE; OrderedLocusNames=BSU33830;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC   STRAIN=168 / JH642;
RX   PubMed=10216873; DOI=10.1046/j.1365-2958.1999.01354.x;
RA   Kappes R.M., Kempf B., Kneip S., Boch J., Gade J., Meier-Wagner J.,
RA   Bremer E.;
RT   "Two evolutionarily closely related ABC transporters mediate the uptake of
RT   choline for synthesis of the osmoprotectant glycine betaine in Bacillus
RT   subtilis.";
RL   Mol. Microbiol. 32:203-216(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION IN GLYCINE BETAINE TRANSPORT.
RC   STRAIN=168 / JH642;
RX   PubMed=8752321; DOI=10.1128/jb.178.17.5071-5079.1996;
RA   Kappes R., Kempf B., Bremer E.;
RT   "Three transport systems for the osmoprotectant glycine betaine operate in
RT   Bacillus subtilis: characterization of OpuD.";
RL   J. Bacteriol. 178:5071-5079(1996).
RN   [4]
RP   INDUCTION.
RC   STRAIN=168;
RX   PubMed=23960087; DOI=10.1099/mic.0.067074-0;
RA   Lee C.H., Wu T.Y., Shaw G.C.;
RT   "Involvement of OpcR, a GbsR-type transcriptional regulator, in negative
RT   regulation of two evolutionarily closely related choline uptake genes in
RT   Bacillus subtilis.";
RL   Microbiology 159:2087-2096(2013).
CC   -!- FUNCTION: Involved in a high affinity multicomponent binding-protein-
CC       dependent transport system for glycine betaine, carnitine and choline;
CC       probably responsible for energy coupling to the transport system.
CC       {ECO:0000269|PubMed:10216873, ECO:0000269|PubMed:8752321}.
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:0000269|PubMed:10216873}.
CC   -!- INDUCTION: Repressed by OpcR. {ECO:0000269|PubMed:23960087}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF009352; AAB63768.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15388.1; -; Genomic_DNA.
DR   PIR; C69670; C69670.
DR   RefSeq; NP_391263.1; NC_000964.3.
DR   RefSeq; WP_003243370.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O34992; -.
DR   SMR; O34992; -.
DR   STRING; 224308.BSU33830; -.
DR   TCDB; 3.A.1.12.4; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O34992; -.
DR   PRIDE; O34992; -.
DR   EnsemblBacteria; CAB15388; CAB15388; BSU_33830.
DR   GeneID; 937136; -.
DR   KEGG; bsu:BSU33830; -.
DR   PATRIC; fig|224308.179.peg.3668; -.
DR   eggNOG; COG0517; Bacteria.
DR   eggNOG; COG1125; Bacteria.
DR   InParanoid; O34992; -.
DR   OMA; MYEFNRA; -.
DR   PhylomeDB; O34992; -.
DR   BioCyc; BSUB:BSU33830-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; 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   Amino-acid transport; ATP-binding; CBS domain; Nucleotide-binding;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN           1..380
FT                   /note="Glycine betaine/carnitine/choline transport ATP-
FT                   binding protein OpuCA"
FT                   /id="PRO_0000092677"
FT   DOMAIN          2..236
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          255..314
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   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   380 AA;  43247 MW;  A10E14DCBF1866A4 CRC64;
     MLKLEQVSKV YKGGKKAVNS IDLDIAKGEF ICFIGPSGCG KTTTMKMINR LIEPSSGRIF
     IDGENIMEQD PVELRRKIGY VIQQIGLFPH MTIQQNISLV PKLLKWPEEK RKERARELLK
     LVDMGPEYLD RYPHELSGGQ QQRIGVLRAL AAEPPLILMD EPFGALDPIT RDSLQEEFKK
     LQRTLNKTIV FVTHDMDEAI KLADRIVILK AGEIVQVGTP DEILRNPANE FVEEFIGKER
     LIQSRPDIER VEQMMNRTPV TVSADKTLSQ AIQLMREKRV DSLLVVDRQN VLKGYVDVEM
     IDQNRKKASI VGDVYRSDIY TVQKGALLRD TVRKILKQGI KYVPVVDEQN HLAGIVTRAS
     LVDIVYDSIW GDEENQLMTI