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   04-NOV-2026, entry version 187.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=7894055; DOI=10.3109/10425179409039700;
RA   Ramseier T.M., Figge R.M., Saier M.H. Jr.;
RT   "DNA sequence of a gene in Escherichia coli encoding a putative tripartite
RT   transcription factor with receiver, ATPase and DNA binding 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   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., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(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 MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   ROLE IN NORV AND NORW EXPRESSION.
RC   STRAIN=K12 / AB1157;
RX   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   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 post-
RT   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   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 Escherichia
RT   coli: role of NorR and sigma 54 in the nitric oxide stress 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 (NO)
CC       reductase, acts as a transcriptional activator for at least the norVW
CC       operon. Activation also requires sigma-54. Not required for induction
CC       of the aerobic NO-detoxifying enzyme NO dioxygenase. Binds to the
CC       promoter region of norVW, to a consensus target sequence, GT-(N7)-AC,
CC       which is highly conserved among proteobacteria.
CC       {ECO:0000269|PubMed:11751865, ECO:0000269|PubMed:12586421}.
CC   -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC   -!- INDUCTION: By anaerobic conditions, however not induced by NO alone.
CC   -!- DOMAIN: Deletion of amino acids 30-164 allows induction of NO reductase
CC       activity even in the absence of NO, i.e. the need for an NO-induced
CC       signal has been bypassed.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69218.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA69219.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA92665.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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_000913.3.
DR   RefSeq; WP_000010749.1; NZ_CP009789.1.
DR   AlphaFoldDB; P37013; -.
DR   SMR; P37013; -.
DR   BioGRID; 4262260; 109.
DR   DIP; DIP-12092N; -.
DR   FunCoup; P37013; 23.
DR   STRING; 511145.b2709; -.
DR   PaxDb; 511145-b2709; -.
DR   EnsemblBacteria; AAC75751; AAC75751; b2709.
DR   GeneID; 947186; -.
DR   KEGG; ecj:JW5843; -.
DR   KEGG; eco:b2709; -.
DR   KEGG; ecoc:C3026_14910; -.
DR   PATRIC; fig|1411691.4.peg.4033; -.
DR   EchoBASE; EB2032; -.
DR   eggNOG; COG3604; Bacteria.
DR   HOGENOM; CLU_000445_125_0_6; -.
DR   InParanoid; P37013; -.
DR   OMA; ADHPRME; -.
DR   OrthoDB; 9804019at2; -.
DR   PhylomeDB; P37013; -.
DR   BioCyc; EcoCyc:EG12108-MONOMER; -.
DR   UniPathway; UPA00638; -.
DR   PRO; PR:P37013; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P37013; -.
DR   GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR   GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR   GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0070026; F:nitric oxide binding; IDA:EcoCyc.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:2000144; P:positive regulation of DNA-templated transcription initiation; IDA:EcoCyc.
DR   CDD; cd00009; AAA; 1.
DR   FunFam; 1.10.10.60:FF:000188; Anaerobic nitric oxide reductase transcription regulator NorR; 1.
DR   FunFam; 1.10.8.60:FF:000045; Anaerobic nitric oxide reductase transcription regulator NorR; 1.
DR   FunFam; 3.30.450.40:FF:000021; Anaerobic nitric oxide reductase transcription regulator NorR; 1.
DR   FunFam; 3.40.50.300:FF:000006; DNA-binding transcriptional regulator NtrC; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01314; NorR; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR058031; AAA_lid_NorR.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR009057; Homeodomain-like_sf.
DR   InterPro; IPR023944; NorR.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   NCBIfam; NF003451; norR; 1.
DR   PANTHER; PTHR32071:SF35; ANAEROBIC NITRIC OXIDE REDUCTASE TRANSCRIPTION REGULATOR NORR; 1.
DR   PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF25601; AAA_lid_14; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50813; GAF; 1.
DR   PROSITE; PS52089; HTH_NTRC; 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; DNA-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..504
FT                   /note="Anaerobic nitric oxide reductase transcription
FT                   regulator NorR"
FT                   /id="PRO_0000081153"
FT   DOMAIN          4..162
FT                   /note="GAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01434"
FT   DOMAIN          187..416
FT                   /note="Sigma-54 factor interaction"
FT   DOMAIN          454..503
FT                   /note="HTH NtrC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01435"
FT   DNA_BIND        479..502
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01435"
FT   REGION          1..186
FT                   /note="NO sensor or transducer"
FT                   /evidence="ECO:0000305"
FT   BINDING         215..222
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         278..287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         57
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000250"
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
//