NARX_ECOLI
ID NARX_ECOLI Reviewed; 598 AA.
AC P0AFA2; P10956;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Nitrate/nitrite sensor protein NarX;
DE EC=2.7.13.3;
GN Name=narX; Synonyms=narR; OrderedLocusNames=b1222, JW1213;
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 [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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
RC STRAIN=K12;
RX PubMed=2668029; DOI=10.1016/0014-5793(89)80906-8;
RA Noji S., Nohno T., Saito T., Taniguchi S.;
RT "The narK gene product participates in nitrate transport induced in
RT Escherichia coli nitrate-respiring cells.";
RL FEBS Lett. 252:139-143(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-598.
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RA Cavicchioli R., Gunsalus R.P., Chiang R.C.;
RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 availability to the NarL protein and of both nitrate/nitrite to
CC the NarP protein. NarX probably activates NarL and NarP by
CC phosphorylation in the presence of nitrate. NarX also plays a negative
CC role in controlling NarL activity, probably through dephosphorylation
CC in the absence of nitrate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- INTERACTION:
CC P0AFA2; P0AF28: narL; NbExp=2; IntAct=EBI-1112775, EBI-1122899;
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; X13360; CAA31741.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74306.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36090.1; -; Genomic_DNA.
DR EMBL; X15996; CAA34125.1; -; Genomic_DNA.
DR EMBL; M24910; AAA24198.1; -; Genomic_DNA.
DR EMBL; X65715; CAA46631.1; -; Genomic_DNA.
DR EMBL; X69189; CAA48934.1; -; Genomic_DNA.
DR PIR; S26137; RGECNX.
DR RefSeq; NP_415740.1; NC_000913.3.
DR RefSeq; WP_000918073.1; NZ_STEB01000023.1.
DR PDB; 3EZH; X-ray; 1.70 A; A/B=38-151.
DR PDB; 3EZI; X-ray; 1.70 A; A/B/C/D=42-148.
DR PDBsum; 3EZH; -.
DR PDBsum; 3EZI; -.
DR AlphaFoldDB; P0AFA2; -.
DR SMR; P0AFA2; -.
DR BioGRID; 4263270; 17.
DR DIP; DIP-35785N; -.
DR IntAct; P0AFA2; 5.
DR STRING; 511145.b1222; -.
DR jPOST; P0AFA2; -.
DR PaxDb; P0AFA2; -.
DR PRIDE; P0AFA2; -.
DR EnsemblBacteria; AAC74306; AAC74306; b1222.
DR EnsemblBacteria; BAA36090; BAA36090; BAA36090.
DR GeneID; 58390543; -.
DR GeneID; 945788; -.
DR KEGG; ecj:JW1213; -.
DR KEGG; eco:b1222; -.
DR PATRIC; fig|1411691.4.peg.1060; -.
DR EchoBASE; EB0640; -.
DR eggNOG; COG3850; Bacteria.
DR HOGENOM; CLU_000445_20_10_6; -.
DR InParanoid; P0AFA2; -.
DR OMA; AHISGRN; -.
DR PhylomeDB; P0AFA2; -.
DR BioCyc; EcoCyc:NARX-MON; -.
DR BioCyc; MetaCyc:NARX-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR EvolutionaryTrace; P0AFA2; -.
DR PRO; PR:P0AFA2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0071249; P:cellular response to nitrate; IEP: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:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IDA: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..598
FT /note="Nitrate/nitrite sensor protein NarX"
FT /id="PRO_0000074812"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..151
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 176..228
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 393..587
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 399
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 42..52
FT /note="GSAHAINKAGS -> AAPMRSTKRDA (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="A -> G (in Ref. 6; AAA24198)"
FT /evidence="ECO:0000305"
FT HELIX 43..62
FT /evidence="ECO:0007829|PDB:3EZH"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3EZH"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:3EZH"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:3EZH"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:3EZH"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:3EZH"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3EZH"
FT HELIX 124..150
FT /evidence="ECO:0007829|PDB:3EZH"
SQ SEQUENCE 598 AA; 67084 MW; 886BA0FC2C8F3C3E CRC64;
MLKRCLSPLT LVNQVALIVL LSTAIGLAGM AVSGWLVQGV QGSAHAINKA GSLRMQSYRL
LAAVPLSEKD KPLIKEMEQT AFSAELTRAA ERDGQLAQLQ GLQDYWRNEL IPALMRAQNR
ETVSADVSQF VAGLDQLVSG FDRTTEMRIE TVVLVHRVMA VFMALLLVFT IIWLRARLLQ
PWRQLLAMAS AVSHRDFTQR ANISGRNEMA MLGTALNNMS AELAESYAVL EQRVQEKTAG
LEHKNQILSF LWQANRRLHS RAPLCERLSP VLNGLQNLTL LRDIELRVYD TDDEENHQEF
TCQPDMTCDD KGCQLCPRGV LPVGDRGTTL KWRLADSHTQ YGILLATLPQ GRHLSHDQQQ
LVDTLVEQLT ATLALDRHQE RQQQLIVMEE RATIARELHD SIAQSLSCMK MQVSCLQMQG
DALPESSREL LSQIRNELNA SWAQLRELLT TFRLQLTEPG LRPALEASCE EYSAKFGFPV
KLDYQLPPRL VPSHQAIHLL QIAREALSNA LKHSQASEVV VTVAQNDNQV KLTVQDNGCG
VPENAIRSNH YGMIIMRDRA QSLRGDCRVR RRESGGTEVV VTFIPEKTFT DVQGDTHE
