ID   NORR_ECOLI              Reviewed;         504 AA.
AC   P37013; Q2MAC0; Q46875; Q46876;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 2.
DT   25-JAN-2012, entry version 102.
DE   RecName: Full=Anaerobic nitric oxide reductase transcription regulator norR;
GN   Name=norR; Synonyms=ygaA; OrderedLocusNames=b2709, JW5843;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   MEDLINE=95201288; PubMed=7894055;
RA   Ramseier T.M., Figge R.M., Saier M.H. Jr.;
RT   "DNA sequence of a gene in Escherichia coli encoding a putative
RT   tripartite transcription factor with receiver, ATPase and DNA binding
RT   domains.";
RL   DNA Seq. 5:17-24(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Yano K., Ikebukuro K., Takada Y., Tomiyama M., Karube I.;
RT   "Sequencing and characterization of the downstream region of hydA in
RT   Escherichia coli.";
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   ROLE IN NORV AND NORW EXPRESSION.
RC   STRAIN=K12 / AB1157;
RX   MEDLINE=21864186; PubMed=11751865; DOI=10.1074/jbc.M110471200;
RA   Gardner A.M., Helmick R.A., Gardner P.R.;
RT   "Flavorubredoxin, an inducible catalyst for nitric oxide reduction and
RT   detoxification in Escherichia coli.";
RL   J. Biol. Chem. 277:8172-8177(2002).
RN   [6]
RP   ROLE IN NORV AND NORW EXPRESSION.
RC   STRAIN=K12;
RX   MEDLINE=22474187; PubMed=12586421; DOI=10.1016/S0378-1097(02)01186-2;
RA   da Costa P.N., Teixeira M., Saraiva L.M.;
RT   "Regulation of the flavorubredoxin nitric oxide reductase gene in
RT   Escherichia coli: nitrate repression, nitrite induction, and possible
RT   post-transcription control.";
RL   FEMS Microbiol. Lett. 218:385-393(2003).
RN   [7]
RP   CHARACTERIZATION, AND REQUIREMENT OF SIGMA 54 FOR TRANSCRIPTIONAL
RP   ACTIVATION.
RC   STRAIN=K12 / AB1157;
RX   MEDLINE=22526737; PubMed=12529359; DOI=10.1074/jbc.M212462200;
RA   Gardner A.M., Gessner C.R., Gardner P.R.;
RT   "Regulation of the nitric oxide reduction operon (norRVW) in
RT   Escherichia coli: role of NorR and sigma 54 in the nitric oxide stress
RT   response.";
RL   J. Biol. Chem. 278:10081-10086(2003).
RN   [8]
RP   DNA-BINDING.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=15375149; DOI=10.1128/JB.186.19.6656-6660.2004;
RA   Tucker N.P., D'Autreaux B., Studholme D.J., Spiro S., Dixon R.;
RT   "DNA binding activity of the Escherichia coli nitric oxide sensor NorR
RT   suggests a conserved target sequence in diverse proteobacteria.";
RL   J. Bacteriol. 186:6656-6660(2004).
CC   -!- FUNCTION: Required for the expression of anaerobic nitric oxide
CC       (NO) reductase, acts as a transcriptional activator for at least
CC       the norVW operon. Activation also requires sigma-54. Not required
CC       for induction of the aerobic NO-detoxifying enzyme NO dioxygenase.
CC       Binds to the promoter region of norVW, to a consensus target
CC       sequence, GT-(N7)-AC, which is highly conserved among
CC       proteobacteria.
CC   -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC   -!- INDUCTION: By anaerobic conditions, however not induced by NO
CC       alone.
CC   -!- DOMAIN: Deletion of amino acids 30-164 allows induction of NO
CC       reductase activity even in the absence of NO, i.e., the need for
CC       an NO-induced signal has been bypassed.
CC   -!- SIMILARITY: Contains 1 sigma-54 factor interaction domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69218.1; Type=Frameshift; Positions=324;
CC       Sequence=AAA69219.1; Type=Frameshift; Positions=324;
CC       Sequence=AAA92665.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; U03846; AAA92665.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U03846; AAA92666.1; -; Genomic_DNA.
DR   EMBL; D28595; BAA05931.1; -; Genomic_DNA.
DR   EMBL; U29579; AAA69219.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U29579; AAA69218.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00096; AAC75751.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76786.1; -; Genomic_DNA.
DR   PIR; A65051; A65051.
DR   RefSeq; NP_417189.2; NC_000913.2.
DR   ProteinModelPortal; P37013; -.
DR   SMR; P37013; 183-499.
DR   DIP; DIP-12092N; -.
DR   EnsemblBacteria; EBESCT00000004661; EBESCP00000004661; EBESCG00000003803.
DR   EnsemblBacteria; EBESCT00000017631; EBESCP00000016922; EBESCG00000016687.
DR   GeneID; 947186; -.
DR   GenomeReviews; AP009048_GR; JW5843.
DR   GenomeReviews; U00096_GR; b2709.
DR   KEGG; ecj:JW5843; -.
DR   KEGG; eco:b2709; -.
DR   PATRIC; 32120816; VBIEscCol129921_2800.
DR   EchoBASE; EB2032; -.
DR   EcoGene; EG12108; norR.
DR   eggNOG; COG3604; -.
DR   GeneTree; EBGT00050000008657; -.
DR   HOGENOM; HBG740884; -.
DR   OMA; RATRNGD; -.
DR   PhylomeDB; P37013; -.
DR   ProtClustDB; PRK05022; -.
DR   BioCyc; EcoCyc:EG12108-MONOMER; -.
DR   Genevestigator; P37013; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008134; F:transcription factor binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   HAMAP; MF_01314; NorR; 1; -.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR023944; NorR.
DR   InterPro; IPR002078; RNA_pol_sigma_54_int.
DR   KO; K12266; -.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; DNA-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    504       Anaerobic nitric oxide reductase
FT                                transcription regulator norR.
FT                                /FTId=PRO_0000081153.
FT   DOMAIN      187    416       Sigma-54 factor interaction.
FT   NP_BIND     215    222       ATP (Potential).
FT   NP_BIND     278    287       ATP (Potential).
FT   DNA_BIND    479    498       H-T-H motif (By similarity).
FT   REGION        1    186       NO sensor or transducer (Probable).
FT   MOD_RES      57     57       4-aspartylphosphate (By similarity).
SQ   SEQUENCE   504 AA;  55236 MW;  B868CF41494DFCC3 CRC64;
     MSFSVDVLAN IAIELQRGIG HQDRFQRLIT TLRQVLECDA SALLRYDSRQ FIPLAIDGLA
     KDVLGRRFAL EGHPRLEAIA RAGDVVRFPA DSELPDPYDG LIPGQESLKV HACVGLPLFA
     GQNLIGALTL DGMQPDQFDV FSDEELRLIA ALAAGALSNA LLIEQLESQN MLPGDATPFE
     AVKQTQMIGL SPGMTQLKKE IEIVAASDLN VLISGETGTG KELVAKAIHE ASPRAVNPLV
     YLNCAALPES VAESELFGHV KGAFTGAISN RSGKFEMADN GTLFLDEIGE LSLALQAKLL
     RVLQYGDIQR VGDDRCLRVD VRVLAATNRD LREEVLAGRF RADLFHRLSV FPLSVPPLRE
     RGDDVILLAG YFCEQCRLRQ GLSRVVLSAG ARNLLQHYSF PGNVRELEHA IHRAVVLARA
     TRSGDEVILE AQHFAFPEVT LPTPEVAAVP VVKQNLREAT EAFQRETIRQ ALAQNHHNWA
     ACARMLETDV ANLHRLAKRL GLKD
//