NORR1_CUPNH
ID NORR1_CUPNH Reviewed; 514 AA.
AC Q9K4V0; Q7WX95;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Nitric oxide reductase transcription regulator NorR1;
GN Name=norR1; OrderedLocusNames=PHG246;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11069685; DOI=10.1046/j.1365-2958.2000.02157.x;
RA Pohlmann A., Cramm R., Schmelz K., Friedrich B.;
RT "A novel NO-responding regulator controls the reduction of nitric oxide in
RT Ralstonia eutropha.";
RL Mol. Microbiol. 38:626-638(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
CC -!- FUNCTION: Required for the nitric oxide (NO) induced expression of NO
CC reductase. Not required for expression of 2 other pathway members,
CC nitrate reductase (nirS) and nitrous oxide reductase (nosZ).
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification)
CC [regulation].
CC -!- INDUCTION: Negatively autoregulated; induced by anaerobic growth in the
CC presence of NO.
CC -!- DOMAIN: Deletion of amino acids 23-168 led to effector-independent
CC expression of NorB1, a downstream gene, i.e. the need for an NO-induced
CC signal has been bypassed.
CC -!- MISCELLANEOUS: There are two very similar, functionally redundant
CC regulators in this bacterium, NorR1 and NorR2.
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DR EMBL; AJ278371; CAC00710.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP85995.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9K4V0; -.
DR SMR; Q9K4V0; -.
DR STRING; 381666.PHG246; -.
DR EnsemblBacteria; AAP85995; AAP85995; PHG246.
DR KEGG; reh:PHG246; -.
DR eggNOG; COG3604; Bacteria.
DR HOGENOM; CLU_000445_125_1_4; -.
DR OMA; TWFEPDS; -.
DR UniPathway; UPA00652; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR002197; HTH_Fis.
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; PF02954; HTH_8; 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; Plasmid;
KW Reference proteome; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..514
FT /note="Nitric oxide reductase transcription regulator
FT NorR1"
FT /id="PRO_0000081161"
FT DOMAIN 187..416
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 490..509
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 215..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 287..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000250"
FT CONFLICT 72..75
FT /note="RLAA -> LACR (in Ref. 1; CAC00710)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="A -> R (in Ref. 1; CAC00710)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="L -> V (in Ref. 1; CAC00710)"
FT /evidence="ECO:0000305"
FT CONFLICT 386..396
FT /note="RLSAAAQDALR -> PVGRRAGRGV (in Ref. 1; CAC00710)"
FT /evidence="ECO:0000305"
FT CONFLICT 410..412
FT /note="VIS -> GDQPR (in Ref. 1; CAC00710)"
FT /evidence="ECO:0000305"
FT CONFLICT 418..420
FT /note="CVS -> E (in Ref. 1; CAC00710)"
FT /evidence="ECO:0000305"
FT CONFLICT 482..483
FT /note="AL -> GV (in Ref. 1; CAC00710)"
FT /evidence="ECO:0000305"
FT CONFLICT 509..510
FT /note="KR -> NG (in Ref. 1; CAC00710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 56302 MW; E15AB2B3C980211E CRC64;
MTPMYPELLT DLVTDLPHAV RLQRLVSGLR THFRCGAVAL LRLEEEHLRP VAVDGLVRDT
LGRRFAVSLH PRLAAILARR DVTCFHHDSM LPDPYDGLID EHVGEPLPVH DCMGTSLHLD
GRPWGVLTLD ALTVGTFDAA AQAELQRLTV IVEAAIRTTR LEAEIRALQL ARGKQPDGEG
PADDGEIIGQ SQAIAGLLHE LEVVADTDLP VLLLGETGVG KELFAHRLHR HSRRRGHPLV
HVNCAALPES LAESELFGHA RGAFSGATGE RPGRFEAAAG GTLFLDEVGE LPLSIQAKLL
RTLQNGEIQR LGSDRPRRVN VRVIAATNRN LREHVRDGSF RADLFHRLSV YPIPIPPLRE
RGNDVLLLAG RFLELNRARL GMRSLRLSAA AQDALRRYRW PGNVRELEHV ISRAALRCVS
RGADRNDIVT LEAELLDLDG LELPAGSAHH AAEAAIAHPA LPTGATLREA VEQTQRACIE
QALRAHDGSW AKAARQLGMD ASNLHKLAKR LGSK
