OPUBA_BACSU
ID OPUBA_BACSU Reviewed; 381 AA.
AC Q45460; O34332;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Choline transport ATP-binding protein OpuBA;
GN Name=opuBA; Synonyms=proV; OrderedLocusNames=BSU33730;
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=168 / LH45, and 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 energy
CC coupling to the transport system. {ECO:0000269|PubMed:10216873}.
CC -!- INDUCTION: Repressed by GbsR. {ECO:0000269|PubMed:22408163}.
CC -!- MISCELLANEOUS: LH45 is not a natural strain. It has been constructed by
CC transformation of strain 168 with linear DNA from B.subtilis ATCC 6633.
CC It is a subtilin-producing mutant of B.subtilis 168 (PubMed:7592481).
CC {ECO:0000305|PubMed:7592481}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U38418; AAB01532.1; -; Genomic_DNA.
DR EMBL; AF008930; AAC14356.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15378.1; -; Genomic_DNA.
DR PIR; G69669; G69669.
DR RefSeq; NP_391253.1; NC_000964.3.
DR RefSeq; WP_003242811.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; Q45460; -.
DR SMR; Q45460; -.
DR STRING; 224308.BSU33730; -.
DR TCDB; 3.A.1.12.3; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q45460; -.
DR PRIDE; Q45460; -.
DR EnsemblBacteria; CAB15378; CAB15378; BSU_33730.
DR GeneID; 936230; -.
DR KEGG; bsu:BSU33730; -.
DR PATRIC; fig|224308.179.peg.3658; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG1125; Bacteria.
DR InParanoid; Q45460; -.
DR OMA; QHDAGWV; -.
DR PhylomeDB; Q45460; -.
DR BioCyc; BSUB:BSU33730-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 2: Evidence at transcript level;
KW Amino-acid transport; ATP-binding; CBS domain; Nucleotide-binding;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..381
FT /note="Choline transport ATP-binding protein OpuBA"
FT /id="PRO_0000092676"
FT DOMAIN 2..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 256..314
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 316..374
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"
FT VARIANT 68
FT /note="D -> E (in strain: 168 / LH45)"
FT VARIANT 72
FT /note="V -> E (in strain: 168 / LH45)"
FT VARIANT 82
FT /note="I -> F (in strain: 168 / LH45)"
FT VARIANT 110
FT /note="Q -> H (in strain: 168 / LH45)"
FT VARIANT 129
FT /note="V -> L (in strain: 168 / LH45)"
FT VARIANT 259
FT /note="Q -> K (in strain: 168 / LH45)"
FT VARIANT 313
FT /note="S -> G (in strain: 168 / LH45)"
FT VARIANT 320
FT /note="I -> L (in strain: 168 / LH45)"
FT VARIANT 341
FT /note="V -> I (in strain: 168 / LH45)"
FT VARIANT 349..350
FT /note="ED -> GN (in strain: 168 / LH45)"
FT CONFLICT 1..11
FT /note="MLTLENVSKTY -> MFADIRKCLENI (in Ref. 1; AAB01532)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="A -> R (in Ref. 1; AAB01532)"
FT /evidence="ECO:0000305"
FT CONFLICT 288..291
FT /note="NDER -> DGEH (in Ref. 1; AAB01532)"
FT /evidence="ECO:0000305"
FT CONFLICT 370..381
FT /note="LWGEEKQLAALS -> SGGKKISSRYCHREVTSHASYYSIFTNQRGRTPV
FT (in Ref. 1; AAB01532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 43075 MW; C91A2DC57345967F CRC64;
MLTLENVSKT YKGGKKAVNN VNLKIAKGEF ICFIGPSGCG KTTTMKMINR LIEPSAGKIF
IDGENIMDQD PVELRRKIGY VIQQIGLFPH MTIQQNISLV PKLLKWPEQQ RKERARELLK
LVDMGPEYVD RYPHELSGGQ QQRIGVLRAL AAEPPLILMD EPFGALDPIT RDSLQEEFKK
LQKTLHKTIV FVTHDMDEAI KLADRIVILK AGEIVQVGTP DDILRNPADE FVEEFIGKER
LIQSSSPDVE RVDQIMNTQP VTITADKTLS EAIQLMRQER VDSLLVVNDE RVLQGYVDVE
IIDQCRKKAN LVSEVLHEDI YTVLGGTLLR DTVRKILKRG VKYVPVVDED RRLIGIVTRA
SLVDIVYDSL WGEEKQLAAL S
