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NSRR_STRCO
ID   NSRR_STRCO              Reviewed;         148 AA.
AC   Q9L132;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=HTH-type transcriptional repressor NsrR;
GN   Name=nsrR; OrderedLocusNames=SCO7427; ORFNames=SC6D11.23;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   DNA-BINDING, COFACTOR, AND SUBUNIT.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=18989365; DOI=10.1371/journal.pone.0003623;
RA   Tucker N.P., Hicks M.G., Clarke T.A., Crack J.C., Chandra G., Le Brun N.E.,
RA   Dixon R., Hutchings M.I.;
RT   "The transcriptional repressor protein NsrR senses nitric oxide directly
RT   via a [2Fe-2S] cluster.";
RL   PLoS ONE 3:E3623-E3623(2008).
CC   -!- FUNCTION: Binds DNA; this binding is disrupted by nitrosylation upon
CC       exposure to nitric oxide (NO) and also by EDTA and iron chelators. The
CC       2Fe-2S cluster is stable in the presence of O(2).
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000269|PubMed:18989365};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000269|PubMed:18989365};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18989365}.
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DR   EMBL; AL939131; CAB76346.1; -; Genomic_DNA.
DR   RefSeq; NP_631476.1; NC_003888.3.
DR   RefSeq; WP_011031657.1; NZ_VNID01000005.1.
DR   PDB; 5N07; X-ray; 1.95 A; A=1-148.
DR   PDB; 5N08; X-ray; 3.90 A; A/B/C/D/E=1-148.
DR   PDBsum; 5N07; -.
DR   PDBsum; 5N08; -.
DR   AlphaFoldDB; Q9L132; -.
DR   SMR; Q9L132; -.
DR   STRING; 100226.SCO7427; -.
DR   GeneID; 1102865; -.
DR   KEGG; sco:SCO7427; -.
DR   PATRIC; fig|100226.15.peg.7537; -.
DR   eggNOG; COG1959; Bacteria.
DR   HOGENOM; CLU_107144_2_0_11; -.
DR   InParanoid; Q9L132; -.
DR   OMA; AQEAFYA; -.
DR   PhylomeDB; Q9L132; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; 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; IPR000944; Tscrpt_reg_Rrf2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR33221; PTHR33221; 1.
DR   Pfam; PF02082; Rrf2; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   TIGRFAMs; TIGR00738; rrf2_super; 1.
DR   PROSITE; PS51197; HTH_RRF2_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; DNA-binding; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..148
FT                   /note="HTH-type transcriptional repressor NsrR"
FT                   /id="PRO_0000368278"
FT   DOMAIN          2..132
FT                   /note="HTH rrf2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00540"
FT   DNA_BIND        29..52
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00540"
FT   BINDING         93
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000305"
FT   BINDING         99
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000305"
FT   BINDING         105
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..18
FT                   /evidence="ECO:0007829|PDB:5N07"
FT   HELIX           29..35
FT                   /evidence="ECO:0007829|PDB:5N07"
FT   HELIX           40..52
FT                   /evidence="ECO:0007829|PDB:5N07"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:5N07"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:5N07"
FT   HELIX           70..74
FT                   /evidence="ECO:0007829|PDB:5N07"
FT   HELIX           77..85
FT                   /evidence="ECO:0007829|PDB:5N07"
FT   STRAND          93..97
FT                   /evidence="ECO:0007829|PDB:5N07"
FT   TURN            100..103
FT                   /evidence="ECO:0007829|PDB:5N07"
FT   HELIX           106..122
FT                   /evidence="ECO:0007829|PDB:5N07"
FT   HELIX           127..131
FT                   /evidence="ECO:0007829|PDB:5N07"
FT   HELIX           135..141
FT                   /evidence="ECO:0007829|PDB:5N07"
SQ   SEQUENCE   148 AA;  15954 MW;  75FD46017BF13729 CRC64;
     MRLTKFTDLA LRSLMRLAVV RDGDEPLATR EVAEVVGVPY THAAKAITRL QHLGVVEARR
     GRGGGLTLTD LGRRVSVGWL VRELEGEAEV VDCEGDNPCP LRGACRLRRA LRDAQEAFYA
     ALDPLTVTDL VAAPTGPVLL GLTDRPSG
 
 
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