NARQ_ECOLI
ID NARQ_ECOLI Reviewed; 566 AA.
AC P27896;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Nitrate/nitrite sensor protein NarQ;
DE EC=2.7.13.3;
GN Name=narQ; OrderedLocusNames=b2469, JW2453;
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=1528845; DOI=10.1073/pnas.89.18.8419;
RA Rabin R.S., Stewart V.;
RT "Either of two functionally redundant sensor proteins, NarX and NarQ, is
RT sufficient for nitrate regulation in Escherichia coli K-12.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8419-8423(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=1508040; DOI=10.1111/j.1365-2958.1992.tb01364.x;
RA Chiang R.C., Cavicchioli R., Gunsalus R.P.;
RT "Identification and characterization of narQ, a second nitrate sensor for
RT nitrate-dependent gene regulation in Escherichia coli.";
RL Mol. Microbiol. 6:1913-1923(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 547-566.
RC STRAIN=K12;
RA Nilles M.L., Bertrand K.P.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Acts as a sensor for nitrate/nitrite and transduces signal of
CC nitrate/nitrite availability to the NarL/NarP proteins. NarQ probably
CC activates NarL and NarP by phosphorylation. NarQ probably negatively
CC regulates the NarL protein by dephosphorylation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
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DR EMBL; M94724; AAA24202.1; -; Genomic_DNA.
DR EMBL; X65714; CAA46630.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75522.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16343.1; -; Genomic_DNA.
DR EMBL; U12598; AAA20583.1; -; Genomic_DNA.
DR PIR; D65022; D65022.
DR RefSeq; NP_416964.1; NC_000913.3.
DR RefSeq; WP_001300881.1; NZ_CP014272.1.
DR PDB; 5IJI; X-ray; 1.94 A; A=1-230.
DR PDB; 5JEF; X-ray; 2.42 A; A/B=1-230.
DR PDB; 5JEQ; X-ray; 1.90 A; A=1-230.
DR PDB; 5JGP; X-ray; 2.70 A; A=1-230.
DR PDB; 6XYN; X-ray; 2.30 A; A=1-230.
DR PDB; 6YUE; X-ray; 2.40 A; A=1-230.
DR PDBsum; 5IJI; -.
DR PDBsum; 5JEF; -.
DR PDBsum; 5JEQ; -.
DR PDBsum; 5JGP; -.
DR PDBsum; 6XYN; -.
DR PDBsum; 6YUE; -.
DR AlphaFoldDB; P27896; -.
DR SMR; P27896; -.
DR BioGRID; 4260928; 11.
DR BioGRID; 851287; 2.
DR DIP; DIP-10318N; -.
DR IntAct; P27896; 12.
DR STRING; 511145.b2469; -.
DR PaxDb; P27896; -.
DR PRIDE; P27896; -.
DR EnsemblBacteria; AAC75522; AAC75522; b2469.
DR EnsemblBacteria; BAA16343; BAA16343; BAA16343.
DR GeneID; 946948; -.
DR KEGG; ecj:JW2453; -.
DR KEGG; eco:b2469; -.
DR PATRIC; fig|511145.12.peg.2563; -.
DR EchoBASE; EB1429; -.
DR eggNOG; COG3850; Bacteria.
DR HOGENOM; CLU_000445_20_10_6; -.
DR InParanoid; P27896; -.
DR OMA; IKHSQGT; -.
DR PhylomeDB; P27896; -.
DR BioCyc; EcoCyc:NARQ-MON; -.
DR BioCyc; MetaCyc:NARQ-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:P27896; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IMP:EcoCyc.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0071249; P:cellular response to nitrate; IMP:EcoCyc.
DR GO; GO:0071250; P:cellular response to nitrite; IMP:EcoCyc.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IMP:EcoCyc.
DR Gene3D; 1.20.120.960; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR029095; NarX-like_N.
DR InterPro; IPR042295; NarX-like_N_sf.
DR InterPro; IPR016380; Sig_transdc_His_kin_NarX/NarQ.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF13675; PilJ; 1.
DR PIRSF; PIRSF003167; STHK_NarX/NarQ; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Membrane; Nitrate assimilation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..566
FT /note="Nitrate/nitrite sensor protein NarQ"
FT /id="PRO_0000074810"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..146
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 174..227
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 364..559
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 370
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT HELIX 7..62
FT /evidence="ECO:0007829|PDB:5JEQ"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:5JEQ"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:5JEQ"
FT HELIX 93..114
FT /evidence="ECO:0007829|PDB:5JEQ"
FT HELIX 118..175
FT /evidence="ECO:0007829|PDB:5JEQ"
FT HELIX 177..191
FT /evidence="ECO:0007829|PDB:5JEQ"
FT HELIX 207..227
FT /evidence="ECO:0007829|PDB:5JEQ"
SQ SEQUENCE 566 AA; 63697 MW; 1D08EA5BD328ACE2 CRC64;
MIVKRPVSAS LARAFFYIVL LSILSTGIAL LTLASSLRDA EAINIAGSLR MQSYRLGYDL
QSGSPQLNAH RQLFQQALHS PVLTNLNVWY VPEAVKTRYA HLNANWLEMN NRLSKGDLPW
YQANINNYVN QIDLFVLALQ HYAERKMLLV VAISLAGGIG IFTLVFFTLR RIRHQVVAPL
NQLVTASQRI EHGQFDSPPL DTNLPNELGL LAKTFNQMSS ELHKLYRSLE ASVEEKTRDL
HEAKRRLEVL YQCSQALNTS QIDVHCFRHI LQIVRDNEAA EYLELNVGEN WRISEGQPNP
ELPMQILPVT MQETVYGELH WQNSHVSSSE PLLNSVSSML GRGLYFNQAQ KHFQQLLLME
ERATIARELH DSLAQVLSYL RIQLTLLKRS IPEDNATAQS IMADFSQALN DAYRQLRELL
TTFRLTLQQA DLPSALREML DTLQNQTSAK LTLDCRLPTL ALDAQMQVHL LQIIREAVLN
AMKHANASEI AVSCVTAPDG NHTVYIRDNG IGIGEPKEPE GHYGLNIMRE RAERLGGTLT
FSQPSGGGTL VSISFRSAEG EESQLM
