ID   NORR_PECAS              Reviewed;         512 AA.
AC   Q6D8R9;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=ECA0903;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(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. {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; BX950851; CAG73815.1; -; Genomic_DNA.
DR   RefSeq; WP_011092505.1; NC_004547.2.
DR   AlphaFoldDB; Q6D8R9; -.
DR   SMR; Q6D8R9; -.
DR   STRING; 218491.ECA0903; -.
DR   PRIDE; Q6D8R9; -.
DR   EnsemblBacteria; CAG73815; CAG73815; ECA0903.
DR   KEGG; eca:ECA0903; -.
DR   PATRIC; fig|218491.5.peg.907; -.
DR   eggNOG; COG3604; Bacteria.
DR   HOGENOM; CLU_000445_125_1_6; -.
DR   OMA; LRYEAHQ; -.
DR   OrthoDB; 123059at2; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000007966; 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   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..512
FT                   /note="Anaerobic nitric oxide reductase transcription
FT                   regulator NorR"
FT                   /id="PRO_0000305618"
FT   DOMAIN          187..416
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01314"
FT   DNA_BIND        488..507
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   512 AA;  56244 MW;  3C926505AB0E28C5 CRC64;
     MTLSINALAH IAIELQMGLS NQDRFQRLIN SLRQLLRCDA SALLRYENQL FRPLAIDGLA
     PDVLGRRFRL SDHPRLEAIA RAGDVVRFPA DSQLPDPYDG LIPSQEDLKV HACVGLPLFA
     NQNLIGALTV DGMDPCQFDH FSDEELRLVG AMAAAALSNA LLMERLERQL PAPVRAESPA
     AESVEEMVGL SEPMQRLKKE VDIVAGSDLN VLIMGETGVG KELVARAIHH GSSRANHPLV
     YLNCAALPES VAESELFGHV KGAFTGAIHH RTGKFEMADN GTLFLDEIGE LSLTLQAKLL
     RVLQYGDLQR VGDDSSLKVN VRVLAATNRD LRQAVLDGAF RADLFHRLSV FPLSVPPLRE
     RSQDVALLAG FFCERSRAQL GLARLALTAE AGALLEQYDW PGNVRELEHA IYRATVLARA
     GQESGEVLLG PEHFNLELPS QPIHATTGSP VAIDTVPTYF ISGGLREATD DYQRRIIQQT
     LVRHEGNWSS CARELEMDSG NLHRLAKRLG IK