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UniProtKB/Swiss-Prot entry P37013


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NORR_ECOLI
Primary accession number P37013
Secondary accession numbers Q2MAC0 Q46875 Q46876
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on March 25, 2003 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 78)
Name and origin of the protein
Protein name Anaerobic nitric oxide reductase transcription regulator norR
Synonyms None
Gene name
Name: norR
Synonyms: ygaA
OrderedLocusNames: b2709, JW5843
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=7894055 [NCBI, ExPASy, EBI, Israel, Japan]
Ramseier T.M., Figge R.M., Saier M.H. Jr.;
"DNA sequence of a gene in Escherichia coli encoding a putative tripartite transcription factor with receiver, ATPase and DNA binding domains.";
DNA Seq. 5:17-24(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Yano K., Ikebukuro K., Takada Y., Tomiyama M., Karube I.;
"Sequencing and characterization of the downstream region of hydA in Escherichia coli.";
Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
ROLE IN NORV AND NORW EXPRESSION.
STRAIN=K12 / AB1157;
DOI=10.1074/jbc.M110471200; PubMed=11751865 [NCBI, ExPASy, EBI, Israel, Japan]
Gardner A.M., Helmick R.A., Gardner P.R.;
"Flavorubredoxin, an inducible catalyst for nitric oxide reduction and detoxification in Escherichia coli.";
J. Biol. Chem. 277:8172-8177(2002).
[6]
ROLE IN NORV AND NORW EXPRESSION.
STRAIN=K12;
DOI=10.1016/S0378-1097(02)01186-2; PubMed=12586421 [NCBI, ExPASy, EBI, Israel, Japan]
da Costa P.N., Teixeira M., Saraiva L.M.;
"Regulation of the flavorubredoxin nitric oxide reductase gene in Escherichia coli: nitrate repression, nitrite induction, and possible post-transcription control.";
FEMS Microbiol. Lett. 218:385-393(2003).
[7]
CHARACTERIZATION, AND REQUIREMENT OF SIGMA 54 FOR TRANSCRIPTIONAL ACTIVATION.
STRAIN=K12 / AB1157;
DOI=10.1074/jbc.M212462200; PubMed=12529359 [NCBI, ExPASy, EBI, Israel, Japan]
Gardner A.M., Gessner C.R., Gardner P.R.;
"Regulation of the nitric oxide reduction operon (norRVW) in Escherichia coli: role of NorR and sigma 54 in the nitric oxide stress response.";
J. Biol. Chem. 278:10081-10086(2003).
[8]
DNA-BINDING.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
DOI=10.1128/JB.186.19.6656-6660.2004; PubMed=15375149 [NCBI, ExPASy, EBI, Israel, Japan]
Tucker N.P., D'Autreaux B., Studholme D.J., Spiro S., Dixon R.;
"DNA binding activity of the Escherichia coli nitric oxide sensor NorR suggests a conserved target sequence in diverse proteobacteria.";
J. Bacteriol. 186:6656-6660(2004).
Comments
  • FUNCTION: Required for the expression of anaerobic nitric oxide (NO) reductase, acts as a transcriptional activator for at least the norVW operon. Activation also requires sigma-54. Not required for induction of the aerobic NO-detoxifying enzyme NO dioxygenase. Binds to the promoter region of norVW, to a consensus target sequence, GT-(N7)-AC, which is highly conserved among proteobacteria.
  • PATHWAY: Nitrogen metabolism; nitric oxide reduction.
  • INDUCTION: By anaerobic conditions, however not induced by NO alone.
  • DOMAIN: Deletion of amino acids 30-164 allows induction of NO reductase activity even in the absence of NO, i.e., the need for an NO-induced signal has been bypassed.
  • SIMILARITY: Contains 1 sigma-54 factor interaction domain.
  • SEQUENCE CAUTION:
    • Sequence=AAA69218.1; Type=Frameshift; Positions=324;
    • Sequence=AAA69219.1; Type=Frameshift; Positions=324;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U03846; AAA92665.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U03846; AAA92666.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D28595; BAA05931.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U29579; AAA69219.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U29579; AAA69218.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75751.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76786.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A65051; A65051.
RefSeq AP_003276.1; -.
NP_417189.2; -.
3D structure databases
ModBase P37013.
Protein-protein interaction databases
DIP DIP:12092N; -.
Enzyme and pathway databases
BioCyc EcoCyc:EG12108-MON; -.
Organism-specific databases
EchoBASE EB2032; -.
EcoGene EG12108; norR.
Ontologies
GO
GO:0005622; Cellular component: intracellular (inferred from electronic annotation from InterPro).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0017111; Molecular function: nucleoside-triphosphatase activity (inferred from electronic annotation from InterPro).
GO:0003700; Molecular function: transcription factor activity (inferred from electronic annotation from HAMAP).
GO:0008134; Molecular function: transcription factor binding (inferred from electronic annotation from InterPro).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from HAMAP).
GO:0007600; Biological process: sensory perception (inferred from electronic annotation from HAMAP).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
GO:0000160; Biological process: two-component signal transduction system (phosphorelay) (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01314; -; 1.
PBIL [Tree]
InterPro IPR003593; ATPase_AAA+_core.
IPR003018; GAF.
IPR002078; RNA_pol_sigma_54_int.
Graphical view of domain structure.
Pfam PF01590; GAF; 1.
PF00158; Sigma54_activat; 1.
Pfam graphical view of domain structure.
SMART SM00382; AAA; 1.
SM00065; GAF; 1.
SMART graphical view of domain structure.
PROSITE PS00675; SIGMA54_INTERACT_1; 1.
PS00676; SIGMA54_INTERACT_2; 1.
PS00688; SIGMA54_INTERACT_3; 1.
PS50045; SIGMA54_INTERACT_4; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 947186; -.
GenomeReviews AP009048_GR; JW5843.
U00096_GR; b2709.
KEGG ecj:JW5843; -.
eco:b2709; -.
Phylogenomic databases
HOGENOM P37013; -.
OMA P37013; RATRNGD.
Genome annotation databases
CMR P37013; b2709.
Other
ProtoNet P37013.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; DNA-binding; Nucleotide-binding; Phosphoprotein; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   504  504     Anaerobic nitric oxide reductase transcription regulator norR. PRO_0000081153
DOMAIN   187   416  230     Sigma-54 factor interaction. 
NP_BIND   215   222  8     ATP (Potential). 
NP_BIND   278   287  10     ATP (Potential). 
DNA_BIND   479   498  20     H-T-H motif (By similarity). 
REGION   1   186  186     NO sensor or transducer (Probable). 
MOD_RES   57    57        4-aspartylphosphate (By similarity). 
Sequence information
Length: 504 AA [This is the length of the unprocessed precursor] Molecular weight: 55236 Da [This is the MW of the unprocessed precursor] CRC64: B868CF41494DFCC3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSFSVDVLAN IAIELQRGIG HQDRFQRLIT TLRQVLECDA SALLRYDSRQ FIPLAIDGLA 

        70         80         90        100        110        120 
KDVLGRRFAL EGHPRLEAIA RAGDVVRFPA DSELPDPYDG LIPGQESLKV HACVGLPLFA 

       130        140        150        160        170        180 
GQNLIGALTL DGMQPDQFDV FSDEELRLIA ALAAGALSNA LLIEQLESQN MLPGDATPFE 

       190        200        210        220        230        240 
AVKQTQMIGL SPGMTQLKKE IEIVAASDLN VLISGETGTG KELVAKAIHE ASPRAVNPLV 

       250        260        270        280        290        300 
YLNCAALPES VAESELFGHV KGAFTGAISN RSGKFEMADN GTLFLDEIGE LSLALQAKLL 

       310        320        330        340        350        360 
RVLQYGDIQR VGDDRCLRVD VRVLAATNRD LREEVLAGRF RADLFHRLSV FPLSVPPLRE 

       370        380        390        400        410        420 
RGDDVILLAG YFCEQCRLRQ GLSRVVLSAG ARNLLQHYSF PGNVRELEHA IHRAVVLARA 

       430        440        450        460        470        480 
TRSGDEVILE AQHFAFPEVT LPTPEVAAVP VVKQNLREAT EAFQRETIRQ ALAQNHHNWA 

       490        500 
ACARMLETDV ANLHRLAKRL GLKD 

P37013 in FASTA format

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