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ARAR_BACSU
ID   ARAR_BACSU              Reviewed;         362 AA.
AC   P96711;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2002, sequence version 3.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Arabinose metabolism transcriptional repressor;
GN   Name=araR; Synonyms=araC, yvbS; OrderedLocusNames=BSU33970;
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=168;
RX   PubMed=9045819; DOI=10.1128/jb.179.5.1598-1608.1997;
RA   Sa-Nogueira I.M.G., Mota L.J.;
RT   "Negative regulation of L-arabinose metabolism in Bacillus subtilis:
RT   characterization of the araR (araC) gene.";
RL   J. Bacteriol. 179:1598-1608(1997).
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 1-10, AND CHARACTERIZATION.
RX   PubMed=10417639; DOI=10.1046/j.1365-2958.1999.01484.x;
RA   Mota L.J., Tavares P., Sa-Nogueira I.M.G.;
RT   "Mode of action of AraR, the key regulator of L-arabinose metabolism in
RT   Bacillus subtilis.";
RL   Mol. Microbiol. 33:476-489(1999).
RN   [4]
RP   CHARACTERIZATION.
RC   STRAIN=168;
RX   PubMed=11418559; DOI=10.1128/jb.183.14.4190-4201.2001;
RA   Mota L.J., Sarmento L.M., Sa-Nogueira I.M.G.;
RT   "Control of the arabinose regulon in Bacillus subtilis by AraR in vivo:
RT   crucial roles of operators, cooperativity, and DNA looping.";
RL   J. Bacteriol. 183:4190-4201(2001).
CC   -!- FUNCTION: Transcriptional repressor of the arabinose utilization genes.
CC       Also regulates its own expression. Binds to two sequences within the
CC       promoters of the araABDLMNPQ-abfA operon and the araE gene, and to one
CC       sequence in the araR promoter.
CC   -!- ACTIVITY REGULATION: Binding to DNA is inhibited by L-arabinose.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR   EMBL; X98354; CAA66999.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15402.2; -; Genomic_DNA.
DR   PIR; D69588; D69588.
DR   RefSeq; NP_391277.1; NC_000964.3.
DR   RefSeq; WP_003243070.1; NZ_JNCM01000033.1.
DR   PDB; 3TB6; X-ray; 2.21 A; A/B=71-362.
DR   PDB; 4EGY; X-ray; 2.30 A; A/B=1-68.
DR   PDB; 4EGZ; X-ray; 2.30 A; A/B=1-68.
DR   PDB; 4H0E; X-ray; 1.97 A; A/B=1-68.
DR   PDB; 5D4R; X-ray; 2.07 A; A/B=1-68.
DR   PDB; 5D4S; X-ray; 1.97 A; A/B=1-68.
DR   PDBsum; 3TB6; -.
DR   PDBsum; 4EGY; -.
DR   PDBsum; 4EGZ; -.
DR   PDBsum; 4H0E; -.
DR   PDBsum; 5D4R; -.
DR   PDBsum; 5D4S; -.
DR   AlphaFoldDB; P96711; -.
DR   SMR; P96711; -.
DR   STRING; 224308.BSU33970; -.
DR   PaxDb; P96711; -.
DR   PRIDE; P96711; -.
DR   EnsemblBacteria; CAB15402; CAB15402; BSU_33970.
DR   GeneID; 938635; -.
DR   KEGG; bsu:BSU33970; -.
DR   PATRIC; fig|224308.179.peg.3683; -.
DR   eggNOG; COG1609; Bacteria.
DR   InParanoid; P96711; -.
DR   OMA; DYIFPRI; -.
DR   BioCyc; BSUB:BSU33970-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   CDD; cd01541; PBP1_AraR; 1.
DR   CDD; cd07377; WHTH_GntR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR033532; AraR_ligand_bind_dom.
DR   InterPro; IPR046335; LacI/GalR-like_sensor.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00392; GntR; 1.
DR   Pfam; PF13377; Peripla_BP_3; 1.
DR   PRINTS; PR00035; HTHGNTR.
DR   SMART; SM00345; HTH_GNTR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
DR   PROSITE; PS50949; HTH_GNTR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..362
FT                   /note="Arabinose metabolism transcriptional repressor"
FT                   /id="PRO_0000050620"
FT   DOMAIN          1..70
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT   DNA_BIND        30..49
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT   HELIX           4..15
FT                   /evidence="ECO:0007829|PDB:5D4S"
FT   TURN            16..19
FT                   /evidence="ECO:0007829|PDB:5D4S"
FT   HELIX           30..37
FT                   /evidence="ECO:0007829|PDB:5D4S"
FT   HELIX           41..53
FT                   /evidence="ECO:0007829|PDB:5D4S"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:5D4S"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:5D4S"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:5D4S"
FT   STRAND          81..87
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   HELIX           94..107
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          111..116
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   HELIX           121..133
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          137..141
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   HELIX           153..161
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          166..171
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          180..183
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   HELIX           185..198
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          203..212
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   HELIX           213..228
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          238..241
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   HELIX           243..246
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   HELIX           249..260
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   TURN            261..263
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          267..270
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   HELIX           274..286
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   TURN            291..294
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   HELIX           305..308
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          309..311
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          314..317
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   HELIX           321..335
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          345..347
FT                   /evidence="ECO:0007829|PDB:3TB6"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:3TB6"
SQ   SEQUENCE   362 AA;  40488 MW;  679DC8FEE69FB421 CRC64;
     MLPKYAQVKE EISSWINQGK ILPDQKIPTE NELMQQFGVS RHTIRKAIGD LVSQGLLYSV
     QGGGTFVASR SAKSALHSNK TIGVLTTYIS DYIFPSIIRG IESYLSEQGY SMLLTSTNNN
     PDNERRGLEN LLSQHIDGLI VEPTKSALQT PNIGYYLNLE KNGIPFAMIN ASYAELAAPS
     FTLDDVKGGM MAAEHLLSLG HTHMMGIFKA DDTQGVKRMN GFIQAHRERE LFPSPDMIVT
     FTTEEKESKL LEKVKATLEK NSKHMPTAIL CYNDEIALKV IDMLREMDLK VPEDMSIVGY
     DDSHFAQISE VKLTSVKHPK SVLGKAAAKY VIDCLEHKKP KQEDVIFEPE LIIRQSARKL
     NE
 
 
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