ID   NORR_ECODH              Reviewed;         504 AA.
AC   B1XCN6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Anaerobic nitric oxide reductase transcription regulator NorR;
GN   Name=norR; OrderedLocusNames=ECDH10B_2877;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
RN   [2]
RP   ROLE IN NORV TRANSCRIPTION.
RX   PubMed=12142437; DOI=10.1128/jb.184.16.4640-4643.2002;
RA   Hutchings M.I., Mandhana N., Spiro S.;
RT   "The NorR protein of Escherichia coli activates expression of the
RT   flavorubredoxin gene norV in response to reactive nitrogen species.";
RL   J. Bacteriol. 184:4640-4643(2002).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC   -!- INDUCTION: By anaerobic conditions, however not induced by NO alone.
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DR   EMBL; CP000948; ACB03827.1; -; Genomic_DNA.
DR   RefSeq; WP_000010749.1; NC_010473.1.
DR   AlphaFoldDB; B1XCN6; -.
DR   SMR; B1XCN6; -.
DR   KEGG; ecd:ECDH10B_2877; -.
DR   HOGENOM; CLU_000445_125_0_6; -.
DR   OMA; LRYEAHQ; -.
DR   BioCyc; ECOL316385:ECDH10B_RS14610-MON; -.
DR   UniPathway; UPA00638; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01314; NorR; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR009057; Homeobox-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   Pfam; PF01590; GAF; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52540; SSF52540; 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   2: Evidence at transcript level;
KW   ATP-binding; DNA-binding; Nucleotide-binding; Phosphoprotein;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..504
FT                   /note="Anaerobic nitric oxide reductase transcription
FT                   regulator NorR"
FT                   /id="PRO_0000341319"
FT   DOMAIN          187..416
FT                   /note="Sigma-54 factor interaction"
FT   DNA_BIND        479..498
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
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