NORR2_CUPNH
ID NORR2_CUPNH Reviewed; 521 AA.
AC Q9K4U8; Q0JYR7;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Nitric oxide reductase transcription regulator NorR2;
GN Name=norR2; OrderedLocusNames=H16_B2325;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
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=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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: By anaerobic growth in the presence of NO.
CC -!- MISCELLANEOUS: There are two very similar, functionally redundant
CC regulators in this bacterium, NorR1 and NorR2.
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DR EMBL; AJ278372; CAC00712.1; -; Genomic_DNA.
DR EMBL; AM260480; CAJ97107.1; -; Genomic_DNA.
DR RefSeq; WP_011617790.1; NZ_CP039288.1.
DR AlphaFoldDB; Q9K4U8; -.
DR SMR; Q9K4U8; -.
DR STRING; 381666.H16_B2325; -.
DR EnsemblBacteria; CAJ97107; CAJ97107; H16_B2325.
DR GeneID; 57648221; -.
DR KEGG; reh:H16_B2325; -.
DR eggNOG; COG3604; Bacteria.
DR HOGENOM; CLU_000445_125_1_4; -.
DR OMA; LRYEAHQ; -.
DR OrthoDB; 123059at2; -.
DR UniPathway; UPA00652; -.
DR Proteomes; UP000008210; Chromosome 2.
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 PRINTS; PR01590; HTHFIS.
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 Reference proteome; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..521
FT /note="Nitric oxide reductase transcription regulator
FT NorR2"
FT /id="PRO_0000081162"
FT DOMAIN 193..422
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 497..516
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 293..302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000250"
FT CONFLICT 124
FT /note="Q -> T (in Ref. 1; CAC00712)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..288
FT /note="GT -> QP (in Ref. 1; CAC00712)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..325
FT /note="RV -> GS (in Ref. 1; CAC00712)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="S -> T (in Ref. 1; CAC00712)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..401
FT /note="SGGAQDAL -> FRRCAGCV (in Ref. 1; CAC00712)"
FT /evidence="ECO:0000305"
FT CONFLICT 418..424
FT /note="SRAALRA -> QPRGAAC (in Ref. 1; CAC00712)"
FT /evidence="ECO:0000305"
FT CONFLICT 460..464
FT /note="ASAFA -> PARSH (in Ref. 1; CAC00712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 56494 MW; B3E4D73A8B6087B0 CRC64;
MLPSAMYPEL LADLVTDLPH AVRLQRLVSM LRTHFRCGAV ALLRLEEDHL RPVAVDGLVR
DALGRRFAVG LHPRLAAILA RRGVTCFHHD SMLPDPYDGL IDEHVGEPLP VHDCMGTSLA
VDGQPWGALT LDALAIGTFD AAAQAELQRL TVIVEAAIRT TRLEGEIRAL QLARGTPEAD
EGTAQHGDIG GEIIGQSEAI ANLLHELEVV ADTDLPVLLL GETGVGKELF AHRLHRQSRR
RAQPLVHVNC AALPESLAES ELFGHARGAF SGATGERPGR FEAADGGTLF LDEVGELPLA
IQAKLLRTLQ NGEIQRLGSD RPRRVNVRVI AATNRNLREH VRDGSFRADL YHRLSVYPIP
IPPLRERGND VLLLAGRFLE LNRARLGLRS LRLSGGAQDA LRSYRWPGNV RELEHVISRA
ALRAVSRGAG RNDIVTLEPE LLDLDGLEVP AAHHAGAGMA SAFAAPALAA GITLRDAVEQ
TQRACIEQAL KDQGGNWAQA ARQLGIDASN LHKLARRLGC K
