ID   NORR_ECO81              Reviewed;         504 AA.
AC   B7MZ04;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Anaerobic nitric oxide reductase transcription regulator NorR {ECO:0000255|HAMAP-Rule:MF_01314};
GN   Name=norR {ECO:0000255|HAMAP-Rule:MF_01314}; OrderedLocusNames=ECED1_3158;
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01314}.
CC   -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC       {ECO:0000255|HAMAP-Rule:MF_01314}.
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DR   EMBL; CU928162; CAR09321.2; -; Genomic_DNA.
DR   RefSeq; WP_000010781.1; NC_011745.1.
DR   AlphaFoldDB; B7MZ04; -.
DR   SMR; B7MZ04; -.
DR   EnsemblBacteria; CAR09321; CAR09321; ECED1_3158.
DR   KEGG; ecq:ECED1_3158; -.
DR   HOGENOM; CLU_000445_125_0_6; -.
DR   OMA; LRYEAHQ; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000000748; Chromosome.
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   3: Inferred from homology;
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_1000165589"
FT   DOMAIN          187..416
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01314"
FT   DNA_BIND        479..498
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01314"
FT   BINDING         215..222
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01314"
FT   BINDING         278..287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01314"
FT   MOD_RES         57
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01314"
SQ   SEQUENCE   504 AA;  55187 MW;  461C4664282848BC CRC64;
     MSFSVDVLAN IAIELQRGIG HQDRFQRLIT TLRQVLECDA SALLRYDSRQ FIPLAIDGLA
     KDVLGRRFAL EGHPRLEAIA RAGDVVRFPA DSELPDPYDG LIPGQESLKV HACVGLPLFA
     GQNLIGALTL DGMQPDQFDV FSNEELRLIA ALAAGALSNA LLIEQLESQN MLPGDAASFE
     AVKQTQMIGL SPGMTQLKKE IEIVAASDLN VLISGETGTG KELVAKAIHE ASPRAVNPLV
     YLNCAALPES VAESELFGHV KGAFTGAISN RSGKFEMADN GTLFLDEIGE LSLALQAKLL
     RVLQYGDIQR VGDDRSLRVD VRVLAATNRD LREEVLAGRF RADLFHRLSV FPLSVPPLRE
     RGDDVILLAG YFCEQCRLRL GLSRVVLSAG ARNLLQHYNF PGNVRELEHA IHRAVVLARA
     TRSGDEVILE AQHFAFPEVT LPPPEVAAVP VVKQNLREAT EAFQRETIRQ ALAQNHHNWA
     ACARMLETDV ANLHRLAKRL GLKD