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GLTR_BACSU
ID   GLTR_BACSU              Reviewed;         296 AA.
AC   P94501; O07083;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=HTH-type transcriptional regulator GltR;
GN   Name=gltR; Synonyms=yrdL; OrderedLocusNames=BSU26670;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, REGULATION, MUTAGENESIS OF
RP   LEU-219, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / SMY;
RX   PubMed=9023181; DOI=10.1128/jb.179.4.1035-1043.1997;
RA   Belitsky B.R., Sonenshein A.L.;
RT   "Altered transcription activation specificity of a mutant form of Bacillus
RT   subtilis GltR, a LysR family member.";
RL   J. Bacteriol. 179:1035-1043(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9308178; DOI=10.1099/00221287-143-9-2939;
RA   Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J.,
RA   Duesterhoeft A., Ehrlich S.D.;
RT   "Sequence of the Bacillus subtilis genome region in the vicinity of the lev
RT   operon reveals two new extracytoplasmic function RNA polymerase sigma
RT   factors SigV and SigZ.";
RL   Microbiology 143:2939-2943(1997).
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   SEQUENCE REVISION TO 187.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: Positive regulator of glutamate biosynthesis (gltAB genes).
CC       Negatively regulates its own expression. {ECO:0000269|PubMed:9023181}.
CC   -!- DISRUPTION PHENOTYPE: No effect observed. {ECO:0000269|PubMed:9023181}.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; U79494; AAB47963.1; -; Genomic_DNA.
DR   EMBL; U93876; AAB80905.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14608.2; -; Genomic_DNA.
DR   PIR; C69635; C69635.
DR   RefSeq; NP_390544.2; NC_000964.3.
DR   RefSeq; WP_003246132.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P94501; -.
DR   SMR; P94501; -.
DR   STRING; 224308.BSU26670; -.
DR   PaxDb; P94501; -.
DR   PRIDE; P94501; -.
DR   DNASU; 938189; -.
DR   EnsemblBacteria; CAB14608; CAB14608; BSU_26670.
DR   GeneID; 938189; -.
DR   KEGG; bsu:BSU26670; -.
DR   PATRIC; fig|224308.179.peg.2898; -.
DR   eggNOG; COG0583; Bacteria.
DR   InParanoid; P94501; -.
DR   OMA; VELHIRP; -.
DR   PhylomeDB; P94501; -.
DR   BioCyc; BSUB:BSU26670-MON; -.
DR   PRO; PR:P94501; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   1: Evidence at protein level;
KW   Activator; Amino-acid biosynthesis; DNA-binding; Glutamate biosynthesis;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..296
FT                   /note="HTH-type transcriptional regulator GltR"
FT                   /id="PRO_0000105630"
FT   DOMAIN          1..58
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        18..37
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   MUTAGEN         219
FT                   /note="L->P: Gain-of-function mutation."
FT                   /evidence="ECO:0000269|PubMed:9023181"
FT   CONFLICT        187
FT                   /note="L -> V (in Ref. 2; AAB80905)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   296 AA;  32956 MW;  D92417A604E5B48C CRC64;
     MNIQLLQVFL TTAREGSISK AALTLNYAQS NVTNKIQQLE NDLQTKLFYR HSRGITLTPP
     GQILVSYSEK ILHTIEEARA AMGESSAPSG PLRIGSMETT AAVWLPQLLA HYNNLYPNVD
     LNLVTGPTEQ QIQAVLHYEL NGAFISGPIE HPDLVQEKVL DEEMVLVTSA SHPVISSIQD
     VQTQTMLVFR KGCSYRAKLN HILQEEGLLP IKLMEFGILE AIIGCVSAGL GISLLPRSII
     ASHEKEGRIR SHTISDKYSF VSTMFIRRKD TLITPALSAF LTHMRDHFQI KRPDQS
 
 
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