NORR_SHIFL
ID NORR_SHIFL Reviewed; 504 AA.
AC P59402;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
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};
GN OrderedLocusNames=SF2732, S2923;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN44223.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP18049.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN44223.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP18049.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_708516.3; NC_004337.2.
DR RefSeq; WP_000010783.1; NZ_WPGW01000014.1.
DR AlphaFoldDB; P59402; -.
DR SMR; P59402; -.
DR STRING; 198214.SF2732; -.
DR EnsemblBacteria; AAN44223; AAN44223; SF2732.
DR EnsemblBacteria; AAP18049; AAP18049; S2923.
DR GeneID; 1027449; -.
DR KEGG; sfl:SF2732; -.
DR KEGG; sfx:S2923; -.
DR PATRIC; fig|198214.7.peg.3253; -.
DR HOGENOM; CLU_000445_125_0_6; -.
DR OMA; LRYEAHQ; -.
DR OrthoDB; 123059at2; -.
DR UniPathway; UPA00638; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..504
FT /note="Anaerobic nitric oxide reductase transcription
FT regulator NorR"
FT /id="PRO_0000081158"
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; 55243 MW; C5ADED3C602654D4 CRC64;
MSFSVDVLAN IAIELQRGIG HQDRFQRLIT TLRQVLECDA SALLRYDSRQ FIPLAIDGLA
KDVLGRRFAL EGHPRLEAIA RAGDVVRFPA DSELPDPYDG LIPGQESLKV HACVGLPLFV
GQNLIGALTL DGMQPDQFDV FSDEELRLIA ALAAGALSNA LLIEQLESQN MLPGDATPFE
AVKQTQMIGL SPGMTQLKKE IEIVAASDLN VLISGETGTG KELVAKAIHE ASPRAVNPLV
YLNCAALPES VAESELFGHV KGAFTGAISN RSGKFEMADN GTLFLDEIGE LSLALQAKLL
RVLQYGDIQR VGDDRSLRVD VRVLAATNRD LREEVLAGRF RADLFHRLSV FPLSVPPLRE
RGDDVILLAG YFCEQCRLRQ GLSRVVLSAG ARNLLQHYSF PGNVRELEHA IHRAVVLARA
TRNGDEVILE AQHFAFPEVT LPPPEAAAVP VVKQNLREAT EAFQRETIRQ ALAQNHHNWA
ACARMLETDV ANLHRLAKRL GLKD
