OPUCB_BACSU
ID OPUCB_BACSU Reviewed; 217 AA.
AC O34878;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Glycine betaine/carnitine/choline transport system permease protein OpuCB;
GN Name=opuCB; Synonyms=yvbD; OrderedLocusNames=BSU33820;
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; AAB63769.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15387.1; -; Genomic_DNA.
DR PIR; D69670; D69670.
DR RefSeq; NP_391262.1; NC_000964.3.
DR RefSeq; WP_003228349.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O34878; -.
DR SMR; O34878; -.
DR STRING; 224308.BSU33820; -.
DR TCDB; 3.A.1.12.4; the atp-binding cassette (abc) superfamily.
DR PaxDb; O34878; -.
DR PRIDE; O34878; -.
DR EnsemblBacteria; CAB15387; CAB15387; BSU_33820.
DR GeneID; 937105; -.
DR KEGG; bsu:BSU33820; -.
DR PATRIC; fig|224308.179.peg.3667; -.
DR eggNOG; COG1174; Bacteria.
DR InParanoid; O34878; -.
DR OMA; MRYLFTH; -.
DR PhylomeDB; O34878; -.
DR BioCyc; BSUB:BSU33820-MON; -.
DR Proteomes; UP000001570; 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:0006865; P:amino acid transport; IEA:UniProtKB-KW.
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 Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..217
FT /note="Glycine betaine/carnitine/choline transport system
FT permease protein OpuCB"
FT /id="PRO_0000060156"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 84..101
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 180..200
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 217 AA; 23149 MW; 5A056B2167770E95 CRC64;
MNQMMTFLQT NGGELLYKTG EHLYISLIAV VLGIIVAVPL GVALTRMKKG AGAVIGFVNI
VQTLPSLAIL AFFIPLLGVG KVPAIVALFF YSVLPILRNT YTGIKGVNKN LLESGKGIGM
TGWEQIRLVE IPLAIPIIMA GIRTSTIYLI GWATLASFIG GGGLGDYIFI GLNLYQPEYI
IGGAVPVTIL AIIIDYVLAV TERKVTPKGL QGMKEVS
