OPUAA_BACSU
ID OPUAA_BACSU Reviewed; 418 AA.
AC P46920;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Glycine betaine transport ATP-binding protein OpuAA;
DE EC=7.6.2.9;
DE AltName: Full=Quaternary-amine-transporting ATPase;
GN Name=opuAA; OrderedLocusNames=BSU02980;
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=7622480; DOI=10.1074/jbc.270.28.16701;
RA Kempf B., Bremer E.;
RT "OpuA, an osmotically regulated binding protein-dependent transport system
RT for the osmoprotectant glycine betaine in Bacillus subtilis.";
RL J. Biol. Chem. 270:16701-16713(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
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 SEQUENCE REVISION TO 35.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
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).
CC -!- FUNCTION: Involved in a multicomponent binding-protein-dependent
CC transport system for glycine betaine. Probably responsible for energy
CC coupling to the transport system. {ECO:0000269|PubMed:7622480,
CC ECO:0000269|PubMed:8752321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + quaternary ammonium(out) = ADP + H(+) + phosphate
CC + quaternary ammonium(in); Xref=Rhea:RHEA:11036, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:35267,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.6.2.9;
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (OpuAA),
CC two transmembrane proteins (OpuAB) and a solute-binding protein
CC (OpuAC). {ECO:0000269|PubMed:7622480}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U17292; AAC43455.1; -; Genomic_DNA.
DR EMBL; D50453; BAA08932.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12092.2; -; Genomic_DNA.
DR PIR; I40535; I40535.
DR RefSeq; NP_388180.2; NC_000964.3.
DR RefSeq; WP_003246301.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P46920; -.
DR SMR; P46920; -.
DR STRING; 224308.BSU02980; -.
DR TCDB; 3.A.1.12.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; P46920; -.
DR EnsemblBacteria; CAB12092; CAB12092; BSU_02980.
DR GeneID; 938362; -.
DR KEGG; bsu:BSU02980; -.
DR PATRIC; fig|224308.179.peg.310; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG4175; Bacteria.
DR InParanoid; P46920; -.
DR OMA; GQIFVVM; -.
DR PhylomeDB; P46920; -.
DR BioCyc; BSUB:BSU02980-MON; -.
DR BRENDA; 7.6.2.9; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0015418; F:ABC-type quaternary ammonium compound transporting activity; IEA:UniProtKB-EC.
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; 1.
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; Translocase; Transport.
FT CHAIN 1..418
FT /note="Glycine betaine transport ATP-binding protein OpuAA"
FT /id="PRO_0000092674"
FT DOMAIN 34..270
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 284..340
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 344..403
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 35
FT /note="T -> A (in Ref. 2; BAA08932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46468 MW; E7A32E331F3103E5 CRC64;
MSVDEKPIKI KVEKVSKIFG KQTKKAVQML ANGKTKKEIL KATGSTVGVN QADFEVYDGE
IFVIMGLSGS GKSTLVRMLN RLIEPTAGNI YIDGDMITNM SKDQLREVRR KKISMVFQKF
ALFPHRTILE NTEYGLELQG VDKQERQQKA LESLKLVGLE GFEHQYPDQL SGGMQQRVGL
ARALTNDPDI LLMDEAFSAL DPLIRKDMQD ELLDLHDNVG KTIIFITHDL DEALRIGDRI
VLMKDGNIVQ IGTPEEILMN PSNEYVEKFV EDVDLSKVLT AGHIMKRAET VRIDKGPRVA
LTLMKNLGIS SIYAVDKQKK LLGVIYASDA KKAAESDLSL QDILNTEFTT VPENTYLTEI
FDVVSDANIP IAVVDEKQRM KGIVVRGALI GALAGNNEYI NAEGTNEQTQ DPSAQEVK
