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DEOR_BACSU
ID   DEOR_BACSU              Reviewed;         313 AA.
AC   P39140;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Deoxyribonucleoside regulator {ECO:0000305};
GN   Name=deoR {ECO:0000303|PubMed:8550462}; Synonyms=yxxC;
GN   OrderedLocusNames=BSU39430;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=168;
RX   PubMed=8550462; DOI=10.1128/jb.178.2.424-434.1996;
RA   Saxild H.H., Andersen L.N., Hammer K.;
RT   "Dra-nupC-pdp operon of Bacillus subtilis: nucleotide sequence, induction
RT   by deoxyribonucleosides, and transcriptional regulation by the deoR-encoded
RT   DeoR repressor protein.";
RL   J. Bacteriol. 178:424-434(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / BGSC1A1;
RX   PubMed=8867804; DOI=10.1093/dnares/2.6.295;
RA   Yoshida K., Fujimyra M., Yanai N., Fujita Y.;
RT   "Cloning and sequencing of a 23-kb region of the Bacillus subtilis genome
RT   between the iol and hut operons.";
RL   DNA Res. 2:295-301(1995).
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, AND DNA-BINDING.
RC   STRAIN=168;
RX   PubMed=10074062; DOI=10.1128/jb.181.6.1719-1727.1999;
RA   Zeng X., Saxild H.H.;
RT   "Identification and characterization of a DeoR-specific operator sequence
RT   essential for induction of dra-nupC-pdp operon expression in Bacillus
RT   subtilis.";
RL   J. Bacteriol. 181:1719-1727(1999).
RN   [5]
RP   FUNCTION, DNA-BINDING, AND SUBUNIT.
RC   STRAIN=168;
RX   PubMed=10714997; DOI=10.1128/jb.182.7.1916-1922.2000;
RA   Zeng X., Saxild H.H., Switzer R.L.;
RT   "Purification and characterization of the DeoR repressor of Bacillus
RT   subtilis.";
RL   J. Bacteriol. 182:1916-1922(2000).
CC   -!- FUNCTION: Negative regulator of the dra-nupC-pdp operon. DeoR binds
CC       cooperatively to the operator DNA, which consists of a palindrome and a
CC       direct repeat sequence located 3' to the palindrome.
CC       {ECO:0000269|PubMed:10074062, ECO:0000269|PubMed:10714997,
CC       ECO:0000269|PubMed:8550462}.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:10714997}.
CC   -!- INTERACTION:
CC       P39140; P39140: deoR; NbExp=3; IntAct=EBI-9538573, EBI-9538573;
CC   -!- MISCELLANEOUS: Deoxyribose-5-phosphate is most likely the effector that
CC       modulates binding of DeoR to DNA. {ECO:0000269|PubMed:10074062,
CC       ECO:0000269|PubMed:10714997}.
CC   -!- SIMILARITY: Belongs to the SorC transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; X82174; CAA57661.1; -; Genomic_DNA.
DR   EMBL; D45912; BAA08336.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15979.1; -; Genomic_DNA.
DR   PIR; S78768; S49454.
DR   RefSeq; NP_391822.1; NC_000964.3.
DR   RefSeq; WP_003227124.1; NZ_JNCM01000034.1.
DR   PDB; 4OQP; X-ray; 1.60 A; A=56-313.
DR   PDB; 4OQQ; X-ray; 1.80 A; A/B=56-313.
DR   PDB; 7BHY; X-ray; 2.30 A; A/B/C=4-55.
DR   PDBsum; 4OQP; -.
DR   PDBsum; 4OQQ; -.
DR   PDBsum; 7BHY; -.
DR   AlphaFoldDB; P39140; -.
DR   SMR; P39140; -.
DR   MINT; P39140; -.
DR   STRING; 224308.BSU39430; -.
DR   PaxDb; P39140; -.
DR   PRIDE; P39140; -.
DR   EnsemblBacteria; CAB15979; CAB15979; BSU_39430.
DR   GeneID; 937543; -.
DR   KEGG; bsu:BSU39430; -.
DR   PATRIC; fig|224308.179.peg.4268; -.
DR   eggNOG; COG2390; Bacteria.
DR   InParanoid; P39140; -.
DR   OMA; WINGLVT; -.
DR   PhylomeDB; P39140; -.
DR   BioCyc; BSUB:BSU39430-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR   InterPro; IPR007324; Sugar-bd_dom_put.
DR   Pfam; PF04198; Sugar-bind; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   SUPFAM; SSF88659; SSF88659; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..313
FT                   /note="Deoxyribonucleoside regulator"
FT                   /id="PRO_0000062788"
FT   DNA_BIND        23..42
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:7BHY"
FT   HELIX           23..30
FT                   /evidence="ECO:0007829|PDB:7BHY"
FT   HELIX           34..46
FT                   /evidence="ECO:0007829|PDB:7BHY"
FT   STRAND          49..54
FT                   /evidence="ECO:0007829|PDB:7BHY"
FT   HELIX           61..72
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   STRAND          75..80
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   HELIX           87..105
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   HELIX           118..126
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   STRAND          136..141
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   STRAND          146..148
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   HELIX           153..163
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:4OQQ"
FT   HELIX           180..187
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   HELIX           190..201
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   STRAND          203..207
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   HELIX           217..219
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   HELIX           226..235
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   STRAND          238..240
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   STRAND          243..245
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   HELIX           254..257
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   HELIX           265..268
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   STRAND          271..277
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   HELIX           281..283
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   HELIX           284..292
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   STRAND          297..302
FT                   /evidence="ECO:0007829|PDB:4OQP"
FT   HELIX           303..310
FT                   /evidence="ECO:0007829|PDB:4OQP"
SQ   SEQUENCE   313 AA;  35253 MW;  DBBAE7EFFB71471B CRC64;
     MDREKQQLSI EAARLYYQSD YSQQQIAEQL NISRPTVSRL LQYAKEKGYV QIRVMDPFED
     LDALGSILEE KYGLLEAHVV FSPTPDYAGI THDLSRYGAE YMHETVKDGD IVGVSWGTTM
     YQIAQNMQPK QVKGVEVVQL KGGISHSRVN TYSAETIQLF AEAFQTMPRY LPLPVVFDNA
     DVKRMVEKDR HIERIIEMGK QANIALFTVG TVRDEALLFR LGYFNEEEKA LLKKQAVGDI
     CSRFFDAKGN ICSSAINDRT IGVELQDLRL KERSILVAGG SRKVSSIHGA LTGKYANVLI
     IDQHTARALV NDL
 
 
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