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Database: UniProt
Entry: NORR_SALA4
LinkDB: NORR_SALA4
Original site: NORR_SALA4 
ID   NORR_SALA4              Reviewed;         506 AA.
AC   B5F363;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=SeAg_B2959;
OS   Salmonella agona (strain SL483).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001138; ACH48780.1; -; Genomic_DNA.
DR   RefSeq; WP_000010808.1; NC_011149.1.
DR   AlphaFoldDB; B5F363; -.
DR   SMR; B5F363; -.
DR   KEGG; sea:SeAg_B2959; -.
DR   HOGENOM; CLU_000445_125_2_6; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000008819; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR32071:SF35; ANAEROBIC NITRIC OXIDE REDUCTASE TRANSCRIPTION REGULATOR NORR; 1.
DR   PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..506
FT                   /note="Anaerobic nitric oxide reductase transcription
FT                   regulator NorR"
FT                   /id="PRO_1000141196"
FT   DOMAIN          187..416
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01314"
FT   DNA_BIND        481..500
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   506 AA;  55433 MW;  80F696A6A395B0B6 CRC64;
     MSFSVEVLAG IAIELQRGIG HQDRFQRLIT TLRQVLACDA SALLRYESRQ FIPLAIDGLA
     QDVLGRRFTL EGHPRLEAIA RAGDVVRFPA DSDLPDPYDG LIPGQESLKV HACVGLPLFA
     GQNLIGALTL DAMTPEQFEV FSDEELRLVA ALAAGALSNA LLIEQLESQN MLPGSSGVFE
     PIKETHMIGL SPAMTQLKKE IEIVAGSDLN VLIGGETGTG KELVAKAIHQ GSPRAVNPLV
     YLNCAALPES VAESELFGHV KGAFTGAISN RSGKFEMADN GTLFLDEIGE LSLALQAKLL
     RVLQYGDIQR VGDDRSLRVD VRVLAATNRD LREEVLAGRF RADLFHRLSV FPLFVPPLRE
     RGDDVVLLAG YFCEQCRLRL GLSRVVLSPD ARRHLLNYGW PGNVRELEHA IHRAVVLARA
     TRAGDEVILE AQHFALSEDV LPAPPAESFL ALPTCRNLRE STENFQREMI RQALAQNNHN
     WAASARALET DVANLHRLAK RLGLKD
//
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