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OPUBC_BACSU
ID   OPUBC_BACSU             Reviewed;         306 AA.
AC   Q45462; O34432;
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-binding protein;
DE   Flags: Precursor;
GN   Name=opuBC; Synonyms=proX; OrderedLocusNames=BSU33710;
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: Member of a high affinity multicomponent binding-protein-
CC       dependent transport system for choline. {ECO:0000269|PubMed:10216873}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- INDUCTION: Repressed by GbsR. {ECO:0000269|PubMed:22408163}.
CC   -!- SIMILARITY: Belongs to the OsmX family. {ECO:0000305}.
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DR   EMBL; U38418; AAB01534.1; -; Genomic_DNA.
DR   EMBL; AF008930; AAC14358.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15376.1; -; Genomic_DNA.
DR   PIR; A69670; A69670.
DR   RefSeq; NP_391251.1; NC_000964.3.
DR   RefSeq; WP_003228372.1; NZ_JNCM01000033.1.
DR   PDB; 3R6U; X-ray; 1.61 A; A=23-306.
DR   PDB; 5NXY; X-ray; 1.90 A; A/C=23-306.
DR   PDB; 6EYG; X-ray; 1.42 A; A=1-306.
DR   PDB; 6EYH; X-ray; 1.60 A; A=1-306.
DR   PDB; 6EYL; X-ray; 1.50 A; A/B=1-306.
DR   PDB; 6EYQ; X-ray; 1.50 A; A/B=1-306.
DR   PDBsum; 3R6U; -.
DR   PDBsum; 5NXY; -.
DR   PDBsum; 6EYG; -.
DR   PDBsum; 6EYH; -.
DR   PDBsum; 6EYL; -.
DR   PDBsum; 6EYQ; -.
DR   AlphaFoldDB; Q45462; -.
DR   SMR; Q45462; -.
DR   STRING; 224308.BSU33710; -.
DR   TCDB; 3.A.1.12.3; the atp-binding cassette (abc) superfamily.
DR   PaxDb; Q45462; -.
DR   PRIDE; Q45462; -.
DR   EnsemblBacteria; CAB15376; CAB15376; BSU_33710.
DR   GeneID; 938475; -.
DR   KEGG; bsu:BSU33710; -.
DR   PATRIC; fig|224308.179.peg.3656; -.
DR   eggNOG; COG1732; Bacteria.
DR   InParanoid; Q45462; -.
DR   OMA; APMNNTY; -.
DR   PhylomeDB; Q45462; -.
DR   BioCyc; BSUB:BSU33710-MON; -.
DR   BRENDA; 7.6.2.9; 658.
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   GO; GO:0031460; P:glycine betaine transport; IBA:GO_Central.
DR   InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
DR   Pfam; PF04069; OpuAC; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid transport; Cell membrane; Lipoprotein; Membrane;
KW   Palmitate; Reference proteome; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..306
FT                   /note="Choline-binding protein"
FT                   /id="PRO_0000031845"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
FT   VARIANT         8
FT                   /note="L -> W (in strain: ATCC 6633)"
FT   VARIANT         13
FT                   /note="A -> T (in strain: ATCC 6633)"
FT   VARIANT         32
FT                   /note="A -> S (in strain: ATCC 6633)"
FT   VARIANT         84
FT                   /note="G -> R (in strain: ATCC 6633)"
FT   VARIANT         111
FT                   /note="D -> E (in strain: ATCC 6633)"
FT   VARIANT         146
FT                   /note="E -> K (in strain: ATCC 6633)"
FT   VARIANT         155
FT                   /note="T -> N (in strain: ATCC 6633)"
FT   VARIANT         194
FT                   /note="G -> S (in strain: ATCC 6633)"
FT   VARIANT         252
FT                   /note="K -> Q (in strain: ATCC 6633)"
FT   CONFLICT        17..19
FT                   /note="TLT -> MLP (in Ref. 1; AAB01534)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172..188
FT                   /note="NYWMKLKGNGYQDFTKT -> KVLDEAQGERLSRFYEN (in Ref. 1;
FT                   AAB01534)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        263..268
FT                   /note="IIKKML -> TIQKMI (in Ref. 1; AAB01534)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296..306
FT                   /note="EYLEKHRYFES -> AIFRKAPLLRIVKGGRSQ (in Ref. 1;
FT                   AAB01534)"
FT                   /evidence="ECO:0000305"
FT   HELIX           28..33
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   STRAND          36..43
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           44..60
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   STRAND          65..71
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           74..82
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           94..100
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           110..125
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   STRAND          139..143
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           145..151
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:5NXY"
FT   HELIX           157..165
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   STRAND          167..170
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           174..176
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   STRAND          178..181
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           182..189
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   STRAND          194..198
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           204..209
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   STRAND          212..219
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           224..227
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   STRAND          230..232
FT                   /evidence="ECO:0007829|PDB:6EYL"
FT   STRAND          244..250
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           251..256
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           260..264
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           265..267
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           273..284
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           290..300
FT                   /evidence="ECO:0007829|PDB:6EYG"
FT   HELIX           302..304
FT                   /evidence="ECO:0007829|PDB:6EYG"
SQ   SEQUENCE   306 AA;  34401 MW;  9D8B32E1F5E7AD0F CRC64;
     MKRKYLKLMI GLALAATLTL SGCSLPGLSA AADQTIKIGA QSMSESEIIA SMLGQLIEHH
     TDLKTTTIKN LGSNAVQQQA LMNGEIDIAA TRYTGDALTG TLRMEPEKDP DKALALTQRE
     FKKRYDLKWY DSYGFDNTYA FTVSKELADQ YHLETVSDVK KWAPQLKLGV DNYWMKLKGN
     GYQDFTKTYG MTFGGTYPMQ IGLVYDAVKS GKMDIVLAYS TDGRIKSYGL KMLKDDKQFF
     PPYDCSPVVP EKVLKEHPEL EGIIKKMLGK IDTATMQELN YEVDGNLKEP SVVAKEYLEK
     HRYFES
 
 
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