NARL_ECOLI
ID NARL_ECOLI Reviewed; 216 AA.
AC P0AF28; P10957;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nitrate/nitrite response regulator protein NarL;
GN Name=narL; Synonyms=frdR; OrderedLocusNames=b1221, JW1212;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2657652; DOI=10.1093/nar/17.8.2947;
RA Nohno T., Noji S., Taniguchi S., Saito T.;
RT "The narX and narL genes encoding the nitrate-sensing regulators of
RT Escherichia coli are homologous to a family of prokaryotic two-component
RT regulatory genes.";
RL Nucleic Acids Res. 17:2947-2957(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2649492; DOI=10.1128/jb.171.4.2229-2234.1989;
RA Stewart V., Parales J. Jr., Merkel S.M.;
RT "Structure of genes narL and narX of the nar (nitrate reductase) locus in
RT Escherichia coli K-12.";
RL J. Bacteriol. 171:2229-2234(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / JM103 / ATCC 39403 / DSM 2829 / KCTC 1112 / NCIMB 12044;
RX PubMed=2648330; DOI=10.1093/nar/17.5.1965;
RA Gunsalus R.P., Kalman L.V., Stewart R.S.;
RT "Nucleotide sequence of the narL gene that is involved in global regulation
RT of nitrate controlled respiratory genes of Escherichia coli.";
RL Nucleic Acids Res. 17:1965-1975(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP MUTAGENESIS.
RX PubMed=2066339; DOI=10.1128/jb.173.14.4424-4432.1991;
RA Egan S.M., Stewart V.;
RT "Mutational analysis of nitrate regulatory gene narL in Escherichia coli K-
RT 12.";
RL J. Bacteriol. 173:4424-4432(1991).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8780507; DOI=10.1021/bi960919o;
RA Baikalov I., Schroeder I., Kaczor-Grzeskowiak M., Grzeskowiak K.,
RA Gunsalus R.P., Dickerson R.E.;
RT "Structure of the Escherichia coli response regulator NarL.";
RL Biochemistry 35:11053-11061(1996).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=9521685; DOI=10.1021/bi972365a;
RA Baikalov I., Schroeder I., Kaczor-Grzeskowiak M., Cascio D., Gunsalus R.P.,
RA Dickerson R.E.;
RT "NarL dimerization? Suggestive evidence from a new crystal form.";
RL Biochemistry 37:3665-3676(1998).
CC -!- FUNCTION: This protein activates the expression of the nitrate
CC reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons and
CC represses the transcription of the fumarate reductase (frdABCD) operon
CC in response to a nitrate/nitrite induction signal transmitted by either
CC the NarX or NarQ proteins.
CC -!- INTERACTION:
CC P0AF28; P0AF28: narL; NbExp=2; IntAct=EBI-1122899, EBI-1122899;
CC P0AF28; P0AFA2: narX; NbExp=2; IntAct=EBI-1122899, EBI-1112775;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA33023.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X13360; CAA31742.1; -; Genomic_DNA.
DR EMBL; M24910; AAA24199.1; -; Genomic_DNA.
DR EMBL; X14884; CAA33023.1; ALT_INIT; Genomic_DNA.
DR EMBL; X69189; CAA48935.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74305.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36089.1; -; Genomic_DNA.
DR PIR; S09285; RGECNL.
DR RefSeq; NP_415739.1; NC_000913.3.
DR RefSeq; WP_000070491.1; NZ_STEB01000023.1.
DR PDB; 1A04; X-ray; 2.20 A; A/B=2-216.
DR PDB; 1JE8; X-ray; 2.12 A; A/B/E/F=147-216.
DR PDB; 1RNL; X-ray; 2.40 A; A=2-216.
DR PDB; 1ZG1; X-ray; 2.30 A; A/B/E/F=147-216.
DR PDB; 1ZG5; X-ray; 2.30 A; A/B/E/F=147-216.
DR PDBsum; 1A04; -.
DR PDBsum; 1JE8; -.
DR PDBsum; 1RNL; -.
DR PDBsum; 1ZG1; -.
DR PDBsum; 1ZG5; -.
DR AlphaFoldDB; P0AF28; -.
DR SMR; P0AF28; -.
DR BioGRID; 4261632; 23.
DR BioGRID; 850162; 1.
DR DIP; DIP-35941N; -.
DR IntAct; P0AF28; 5.
DR STRING; 511145.b1221; -.
DR jPOST; P0AF28; -.
DR PaxDb; P0AF28; -.
DR PRIDE; P0AF28; -.
DR EnsemblBacteria; AAC74305; AAC74305; b1221.
DR EnsemblBacteria; BAA36089; BAA36089; BAA36089.
DR GeneID; 60668739; -.
DR GeneID; 945795; -.
DR KEGG; ecj:JW1212; -.
DR KEGG; eco:b1221; -.
DR PATRIC; fig|1411691.4.peg.1061; -.
DR EchoBASE; EB0637; -.
DR eggNOG; COG2197; Bacteria.
DR HOGENOM; CLU_000445_90_8_6; -.
DR InParanoid; P0AF28; -.
DR OMA; LDKYATH; -.
DR PhylomeDB; P0AF28; -.
DR BioCyc; EcoCyc:NARL-MON; -.
DR BioCyc; MetaCyc:NARL-MON; -.
DR EvolutionaryTrace; P0AF28; -.
DR PRO; PR:P0AF28; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_00000880; -.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IMP:EcoCyc.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IMP:EcoCyc.
DR GO; GO:0090352; P:regulation of nitrate assimilation; IMP:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:EcoCyc.
DR CDD; cd06170; LuxR_C_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ATP-binding; DNA-binding; Nitrate assimilation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..216
FT /note="Nitrate/nitrite response regulator protein NarL"
FT /id="PRO_0000081145"
FT DOMAIN 8..124
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 149..214
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 173..192
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 115
FT /note="D -> H (in Ref. 2; AAA24199)"
FT /evidence="ECO:0000305"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:1A04"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1A04"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:1A04"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:1A04"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1A04"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1RNL"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:1A04"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1A04"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:1A04"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1A04"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:1A04"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1A04"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:1A04"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1JE8"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:1JE8"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1JE8"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:1JE8"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:1JE8"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:1JE8"
SQ SEQUENCE 216 AA; 23927 MW; 7DED78E4EF7EC57D CRC64;
MSNQEPATIL LIDDHPMLRT GVKQLISMAP DITVVGEASN GEQGIELAES LDPDLILLDL
NMPGMNGLET LDKLREKSLS GRIVVFSVSN HEEDVVTALK RGADGYLLKD MEPEDLLKAL
HQAAAGEMVL SEALTPVLAA SLRANRATTE RDVNQLTPRE RDILKLIAQG LPNKMIARRL
DITESTVKVH VKHMLKKMKL KSRVEAAVWV HQERIF
