(data stored in SCRATCH zone)

SWISSPROT: OPUAB_BACSU

ID   OPUAB_BACSU             Reviewed;         282 AA.
AC   P46921;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 120.
DE   RecName: Full=Glycine betaine transport system permease protein OpuAB;
GN   Name=opuAB; OrderedLocusNames=BSU02990;
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   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 the
CC       translocation of the substrate across the membrane.
CC       {ECO:0000269|PubMed:7622480, ECO:0000269|PubMed:8752321}.
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   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. CysTW subfamily. {ECO:0000305}.
DR   EMBL; U17292; AAC43456.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA08933.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12093.1; -; Genomic_DNA.
DR   PIR; I40536; I40536.
DR   RefSeq; NP_388181.1; NC_000964.3.
DR   RefSeq; WP_003234703.1; NZ_JNCM01000030.1.
DR   STRING; 224308.BSU02990; -.
DR   TCDB; 3.A.1.12.2; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P46921; -.
DR   PRIDE; P46921; -.
DR   EnsemblBacteria; CAB12093; CAB12093; BSU02990.
DR   GeneID; 938360; -.
DR   KEGG; bsu:BSU02990; -.
DR   PATRIC; fig|224308.179.peg.311; -.
DR   eggNOG; ENOG4107SQ8; Bacteria.
DR   eggNOG; COG4176; LUCA.
DR   HOGENOM; HOG000279300; -.
DR   InParanoid; P46921; -.
DR   KO; K02001; -.
DR   OMA; LDMGLAS; -.
DR   PhylomeDB; P46921; -.
DR   BioCyc; BSUB:BSU02990-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:1902495; C:transmembrane transporter complex; IBA:GO_Central.
DR   GO; GO:0005275; F:amine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015226; F:carnitine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   GO; GO:1902603; P:carnitine transmembrane transport; IBA:GO_Central.
DR   GO; GO:0015871; P:choline transport; IBA:GO_Central.
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;
DR   PRODOM; P46921.
DR   SWISS-2DPAGE; P46921.
KW   Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..282
FT                   /note="Glycine betaine transport system permease protein
FT                   OpuAB"
FT                   /id="PRO_0000060153"
FT   TOPO_DOM        1..18
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        40..44
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        66..69
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        91..93
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        115..137
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        159..215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        237..242
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        264..282
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          90..269
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   282 AA;  30247 MW;  B05FDABD403BDBC1 CRC64;
     MDRLPRIPLA DIIDRFVDWI TMTFGGFFDG IANGLAAFVN GIVTGLGFIP SILLTIIFAA
     LAWWISTRGI ALFTLIGFLL IDYLGYWDPM LQTLALVLTS VIISIVVGVP IGIWASQKET
     VRRIVTPILD LMQTMPAFVY LLPAIFFFNI GVVPGVVASV IFAMPPTIRM TVLGIKQVPA
     DLIEATEAFG STTAQRLFKV QLPLATKTIL AGINQSIMLA LSMVVIAAMV GAPGLGSEVY
     SAVTQLKTGV GVEAGIAIVI VAITLDRITQ NIKVKKKSRG NA
//

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