(data stored in SCRATCH zone)

SWISSPROT: OPUAC_BACSU

ID   OPUAC_BACSU             Reviewed;         293 AA.
AC   P46922;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 117.
DE   RecName: Full=Glycine betaine-binding protein OpuAC;
DE   Flags: Precursor;
GN   Name=opuAC; OrderedLocusNames=BSU03000;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 274-293.
RC   STRAIN=168 / JH642;
RA   Kempf B., Bremer E.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000269|PubMed:7622480,
CC       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 {ECO:0000255|PROSITE-
CC       ProRule:PRU00303, ECO:0000269|PubMed:7622480}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:7622480}.
DR   EMBL; U17292; AAC43457.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA08934.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12094.1; -; Genomic_DNA.
DR   EMBL; U47860; AAC44169.1; -; Genomic_DNA.
DR   PIR; I40537; I40537.
DR   RefSeq; NP_388182.1; NC_000964.3.
DR   RefSeq; WP_003246462.1; NZ_JNCM01000030.1.
DR   PDB; 2B4L; X-ray; 2.00 A; A=26-293.
DR   PDB; 2B4M; X-ray; 2.80 A; A/B=26-293.
DR   PDB; 3CHG; X-ray; 2.80 A; A/B/C/D=26-293.
DR   PDB; 5NXX; X-ray; 2.20 A; C/D=26-293.
DR   PDBsum; 2B4L; -.
DR   PDBsum; 2B4M; -.
DR   PDBsum; 3CHG; -.
DR   PDBsum; 5NXX; -.
DR   SMR; P46922; -.
DR   STRING; 224308.BSU03000; -.
DR   TCDB; 3.A.1.12.2; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P46922; -.
DR   PRIDE; P46922; -.
DR   EnsemblBacteria; CAB12094; CAB12094; BSU03000.
DR   GeneID; 938354; -.
DR   KEGG; bsu:BSU03000; -.
DR   PATRIC; fig|224308.179.peg.312; -.
DR   eggNOG; COG2113; LUCA.
DR   HOGENOM; HOG000279301; -.
DR   InParanoid; P46922; -.
DR   KO; K02002; -.
DR   OMA; AGPMWTA; -.
DR   PhylomeDB; P46922; -.
DR   BioCyc; BSUB:BSU03000-MONOMER; -.
DR   BRENDA; 3.6.3.32; 658.
DR   EvolutionaryTrace; P46922; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
DR   Pfam; PF04069; OpuAC; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P46922.
DR   SWISS-2DPAGE; P46922.
KW   3D-structure; Amino-acid transport; Cell membrane; Lipoprotein; Membrane;
KW   Palmitate; Reference proteome; Signal; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000305"
FT   CHAIN           21..293
FT                   /note="Glycine betaine-binding protein OpuAC"
FT                   /id="PRO_0000031844"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
FT   HELIX           31..34
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   TURN            35..37
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   STRAND          38..40
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           47..58
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   STRAND          65..67
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           71..83
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   STRAND          90..95
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           98..101
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   STRAND          104..106
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   STRAND          116..125
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           128..131
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           133..140
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           146..157
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           162..172
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           174..180
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   TURN            181..183
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   STRAND          191..196
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           200..216
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   STRAND          219..224
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           229..235
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   STRAND          238..247
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   TURN            248..251
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           252..257
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   TURN            258..260
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   STRAND          261..279
FT                   /evidence="ECO:0000244|PDB:2B4L"
FT   HELIX           288..291
FT                   /evidence="ECO:0000244|PDB:2B4L"
SQ   SEQUENCE   293 AA;  32215 MW;  B2BE74985069C4C7 CRC64;
     MLKKIIGIGV SAMLALSLAA CGSENDENAS AAEQVNKTII GIDPGSGIMS LTDKAMKDYD
     LNDWTLISAS SAAMTATLKK SYDRKKPIII TGWTPHWMFS RYKLKYLDDP KQSYGSAEEI
     HTITRKGFSK EQPNAAKLLS QFKWTQDEMG EIMIKVEEGE KPAKVAAEYV NKHKDQIAEW
     TKGVQKVKGD KINLAYVAWD SEIASTNVIG KVLEDLGYEV TLTQVEAGPM WTAIATGSAD
     ASLSAWLPNT HKAYAAKYKG KYDDIGTSMT GVKMGLVVPQ YMKNVNSIED LKK
//

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