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CNRH_CUPMC
ID   CNRH_CUPMC              Reviewed;         191 AA.
AC   P37978; P37976; Q5NUX2; Q7B057;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=RNA polymerase sigma factor CnrH;
GN   Name=cnrH; OrderedLocusNames=Rmet_6207; ORFNames=RMe0086;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OG   Plasmid pMOL28.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8380802; DOI=10.1128/jb.175.3.767-778.1993;
RA   Liesegang H., Lemke K., Siddiqui R.A., Schlegel H.-G.;
RT   "Characterization of the inducible nickel and cobalt resistance determinant
RT   cnr from pMOL28 of Alcaligenes eutrophus CH34.";
RL   J. Bacteriol. 175:767-778(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   van der Lelie D., Monchy S., Taghavi S., McCorkle S., Dunn J.,
RA   Benotmane M., Vallaeys T., Lapidus A., Mergeay M.;
RT   "Sequence and features of the Ralstonia metallidurans CH34 heavy metal
RT   plasmids pMOL28 and pMOL30.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
RN   [4]
RP   IDENTIFICATION, AND SIMILARITY TO OTHER ECF SIGMA FACTORS.
RX   PubMed=8052622; DOI=10.1073/pnas.91.16.7573;
RA   Lonetto M.A., Brown K.L., Rudd K.E., Buttner M.J.;
RT   "Analysis of the Streptomyces coelicolor sigE gene reveals the existence of
RT   a subfamily of eubacterial RNA polymerase sigma factors involved in the
RT   regulation of extracytoplasmic functions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:7573-7577(1994).
RN   [5]
RP   CHARACTERIZATION, AND INDUCTION.
RX   PubMed=10671463; DOI=10.1128/jb.182.5.1390-1398.2000;
RA   Grass G., Grosse C., Nies D.H.;
RT   "Regulation of the cnr cobalt and nickel resistance determinant from
RT   Ralstonia sp. strain CH34.";
RL   J. Bacteriol. 182:1390-1398(2000).
RN   [6]
RP   DNA-BINDING, AND INDUCTION.
RX   PubMed=10671464; DOI=10.1128/jb.182.5.1399-1409.2000;
RA   Tibazarwa C., Wuertz S., Mergeay M., Wyns L., van der Lelie D.;
RT   "Regulation of the cnr cobalt and nickel resistance determinant of
RT   Ralstonia eutropha (Alcaligenes eutrophus) CH34.";
RL   J. Bacteriol. 182:1399-1409(2000).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released. This sigma factor regulates the genes for a membrane-located
CC       efflux system that confers resistance to nickel and cobalt.
CC   -!- FUNCTION: CnrH alone is able to activate CNR expression, while both
CC       CnrY and CrnX are needed for nickel induction of cnrH
CC       (PubMed:10671463). Binds DNA in an RNA polymerase-dependent fashion
CC       (PubMed:10671464). CnrH may be controlled by a CnrYX transmembrane
CC       anti-sigma factor complex which binds CnrH in the absence of Ni(2+). If
CC       Ni(2+) appears in the periplasm, it may be bound by CnrR (CnrX); the
CC       signal then would be transmitted by CnrY into the cytoplasm and CnrH
CC       would be released. {ECO:0000269|PubMed:10671463,
CC       ECO:0000269|PubMed:10671464}.
CC   -!- INDUCTION: By nickel and cobalt. {ECO:0000269|PubMed:10671463,
CC       ECO:0000269|PubMed:10671464}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M91650; AAA21967.1; -; Genomic_DNA.
DR   EMBL; AJ276513; CAB82450.1; -; Genomic_DNA.
DR   EMBL; X90708; CAI30230.1; -; Genomic_DNA.
DR   EMBL; CP000355; ABF13066.1; -; Genomic_DNA.
DR   RefSeq; WP_011239969.1; NC_007972.2.
DR   RefSeq; YP_161708.1; NC_006525.1.
DR   PDB; 4CXF; X-ray; 1.75 A; A=1-191.
DR   PDBsum; 4CXF; -.
DR   AlphaFoldDB; P37978; -.
DR   SMR; P37978; -.
DR   PRIDE; P37978; -.
DR   EnsemblBacteria; ABF13066; ABF13066; Rmet_6207.
DR   GeneID; 60825775; -.
DR   KEGG; rme:Rmet_6207; -.
DR   HOGENOM; CLU_047691_3_0_4; -.
DR   OMA; WHALDDF; -.
DR   OrthoDB; 1914729at2; -.
DR   Proteomes; UP000002429; Plasmid pMOL28.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR039425; RNA_pol_sigma-70-like.
DR   InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR   InterPro; IPR000838; RNA_pol_sigma70_ECF_CS.
DR   InterPro; IPR007627; RNA_pol_sigma70_r2.
DR   InterPro; IPR013249; RNA_pol_sigma70_r4_t2.
DR   InterPro; IPR013325; RNA_pol_sigma_r2.
DR   InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR43133; PTHR43133; 1.
DR   Pfam; PF04542; Sigma70_r2; 1.
DR   Pfam; PF08281; Sigma70_r4_2; 1.
DR   SUPFAM; SSF88659; SSF88659; 1.
DR   SUPFAM; SSF88946; SSF88946; 1.
DR   TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR   PROSITE; PS01063; SIGMA70_ECF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cobalt; DNA-binding; Nickel; Plasmid; Reference proteome;
KW   Sigma factor; Transcription; Transcription regulation.
FT   CHAIN           1..191
FT                   /note="RNA polymerase sigma factor CnrH"
FT                   /id="PRO_0000094009"
FT   DNA_BIND        156..175
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   MOTIF           49..62
FT                   /note="Polymerase core binding"
FT   HELIX           6..15
FT                   /evidence="ECO:0007829|PDB:4CXF"
FT   HELIX           19..39
FT                   /evidence="ECO:0007829|PDB:4CXF"
FT   HELIX           44..61
FT                   /evidence="ECO:0007829|PDB:4CXF"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:4CXF"
FT   HELIX           71..87
FT                   /evidence="ECO:0007829|PDB:4CXF"
FT   HELIX           126..135
FT                   /evidence="ECO:0007829|PDB:4CXF"
FT   HELIX           140..150
FT                   /evidence="ECO:0007829|PDB:4CXF"
FT   HELIX           156..163
FT                   /evidence="ECO:0007829|PDB:4CXF"
FT   HELIX           167..188
FT                   /evidence="ECO:0007829|PDB:4CXF"
SQ   SEQUENCE   191 AA;  20623 MW;  711DE56029AB4816 CRC64;
     MNPEDADRIL AAQAASGNQR AFGQLVARHG VALAQAARSF GIPETDVDDV VQDTFVAAWH
     ALDDFDPDRP FRAWLFRIGL NKMRDLYRFR RVRQFLFGAE NLGDLELAGG VANDEPGPEQ
     QVAARLELAR VASTLGKLDT GSREVIVLTA IVGMSQPEAA AVLGLSVKAV EGRIGRARAK
     LSALLDADSE K
 
 
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