NARX_ECO57
ID NARX_ECO57 Reviewed; 598 AA.
AC P0AFA3; P10956;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Nitrate/nitrite sensor protein NarX;
DE EC=2.7.13.3;
GN Name=narX; OrderedLocusNames=Z1998, ECs1727;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 (By similarity). {ECO:0000250}.
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 {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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DR EMBL; AE005174; AAG56082.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35150.1; -; Genomic_DNA.
DR PIR; F85702; F85702.
DR PIR; G90844; G90844.
DR RefSeq; NP_309754.1; NC_002695.1.
DR RefSeq; WP_000918073.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AFA3; -.
DR SMR; P0AFA3; -.
DR STRING; 155864.EDL933_1928; -.
DR EnsemblBacteria; AAG56082; AAG56082; Z1998.
DR EnsemblBacteria; BAB35150; BAB35150; ECs_1727.
DR GeneID; 58390543; -.
DR GeneID; 913134; -.
DR KEGG; ece:Z1998; -.
DR KEGG; ecs:ECs_1727; -.
DR PATRIC; fig|386585.9.peg.1827; -.
DR eggNOG; COG3850; Bacteria.
DR HOGENOM; CLU_000445_20_10_6; -.
DR OMA; AHISGRN; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW 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_0000074813"
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"
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
