ID   OPUCD_BACSU             Reviewed;         229 AA.
AC   O34742;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Glycine betaine/carnitine/choline transport system permease protein OpuCD;
GN   Name=opuCD; Synonyms=yvbB; OrderedLocusNames=BSU33800;
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 the translocation of the substrate across the
CC       membrane. {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   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- INDUCTION: Repressed by OpcR. {ECO:0000269|PubMed:23960087}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. CysTW subfamily. {ECO:0000305}.
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DR   EMBL; AF009352; AAB63771.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15385.1; -; Genomic_DNA.
DR   PIR; F69670; F69670.
DR   RefSeq; NP_391260.1; NC_000964.3.
DR   RefSeq; WP_003244403.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O34742; -.
DR   SMR; O34742; -.
DR   STRING; 224308.BSU33800; -.
DR   TCDB; 3.A.1.12.4; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O34742; -.
DR   EnsemblBacteria; CAB15385; CAB15385; BSU_33800.
DR   GeneID; 937199; -.
DR   KEGG; bsu:BSU33800; -.
DR   PATRIC; fig|224308.179.peg.3665; -.
DR   eggNOG; COG1174; Bacteria.
DR   InParanoid; O34742; -.
DR   OMA; TAYVLQG; -.
DR   PhylomeDB; O34742; -.
DR   BioCyc; BSUB:BSU33800-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   GO; GO:0031460; P:glycine betaine transport; IBA:GO_Central.
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   Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..229
FT                   /note="Glycine betaine/carnitine/choline transport system
FT                   permease protein OpuCD"
FT                   /id="PRO_0000060157"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        55..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        78..100
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   229 AA;  24551 MW;  FB00B4A1EF989054 CRC64;
     MEVLQQLGTY YSQNGGYVLQ EFYRHFLMSV YGVLFAAIVG IPLGILIARY RRLSGWVFAV
     TNVIQTIPAL AMLAVLMLVM GLGANTVILS LFLYSLLPII RNTYTGIISI EHAYLESGKA
     MGMTKFQVLR MVELPLALSV IMAGLRTALV IAIGITAIGT FVGAGGLGDI IVRGSNATNG
     TAIILAGAIP TALMAVIADL VMGWLERALS PIKKKKGNFI IADRKTTSI