OPUBB_BACSU
ID OPUBB_BACSU Reviewed; 217 AA.
AC Q45461; O34670;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Choline transport system permease protein OpuBB;
GN Name=opuBB; Synonyms=proW; OrderedLocusNames=BSU33720;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX PubMed=7592481; DOI=10.1128/jb.177.23.6874-6880.1995;
RA Lin Y., Hansen J.N.;
RT "Characterization of a chimeric proU operon in a subtilin-producing mutant
RT of Bacillus subtilis 168.";
RL J. Bacteriol. 177:6874-6880(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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 [3]
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 [4]
RP INDUCTION.
RC STRAIN=168 / JH642;
RX PubMed=22408163; DOI=10.1128/jb.06642-11;
RA Nau-Wagner G., Opper D., Rolbetzki A., Boch J., Kempf B., Hoffmann T.,
RA Bremer E.;
RT "Genetic control of osmoadaptive glycine betaine synthesis in Bacillus
RT subtilis through the choline-sensing and glycine betaine-responsive GbsR
RT repressor.";
RL J. Bacteriol. 194:2703-2714(2012).
CC -!- FUNCTION: Involved in a high affinity multicomponent binding-protein-
CC dependent transport system for choline; probably responsible for the
CC translocation of the substrate across the membrane.
CC {ECO:0000269|PubMed:10216873}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- INDUCTION: Repressed by GbsR. {ECO:0000269|PubMed:22408163}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {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; U38418; AAB01533.1; -; Genomic_DNA.
DR EMBL; AF008930; AAC14357.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15377.1; -; Genomic_DNA.
DR PIR; H69669; H69669.
DR RefSeq; NP_391252.1; NC_000964.3.
DR RefSeq; WP_003228370.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; Q45461; -.
DR SMR; Q45461; -.
DR STRING; 224308.BSU33720; -.
DR TCDB; 3.A.1.12.3; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q45461; -.
DR EnsemblBacteria; CAB15377; CAB15377; BSU_33720.
DR GeneID; 936225; -.
DR KEGG; bsu:BSU33720; -.
DR PATRIC; fig|224308.179.peg.3657; -.
DR eggNOG; COG1174; Bacteria.
DR InParanoid; Q45461; -.
DR OMA; NMGQATP; -.
DR PhylomeDB; Q45461; -.
DR BioCyc; BSUB:BSU33720-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 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..217
FT /note="Choline transport system permease protein OpuBB"
FT /id="PRO_0000060154"
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"
FT VARIANT 5
FT /note="V -> I (in strain: ATCC 6633 / PCI 219)"
FT VARIANT 130..131
FT /note="EL -> DV (in strain: ATCC 6633 / PCI 219)"
FT VARIANT 201
FT /note="A -> T (in strain: ATCC 6633 / PCI 219)"
FT VARIANT 216
FT /note="L -> V (in strain: ATCC 6633 / PCI 219)"
FT CONFLICT 67..72
FT /note="LAILAF -> PDSRHI (in Ref. 1; AAB01533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 23163 MW; A7915A2D22ABA58E CRC64;
MHHIVQFLQT NGGELLYKTY EHITISLIAV ILGVLVAVPL GVVLTRMKKG AGTIIGIVNI
IQTLPSLAIL AFFIPLLGVG KVPAIVALFF YSVLPILRNT YTGIRGVNKN LLESGKGIGM
TPAEQVRLVE LPLAAPVIMA GIRTSTIYLI GWATLASFIG GGGLGDYIFI GLNLYQPEYI
IGGAVPVTIL AIVIDYVLAV AERKLTPAGM QRLKELS
