ID   NARQ_HAEIN              Reviewed;         567 AA.
AC   P44604;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Sensor protein NarQ homolog;
DE            EC=2.7.13.3;
GN   Name=narQ; OrderedLocusNames=HI_0267;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Probable member of a two-component regulatory system. It is
CC       not known what protein it phosphorylates and in which regulatory
CC       pathway it acts, as the narL and other nar genes do not exist in
CC       H.influenzae.
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; L42023; AAC21933.1; -; Genomic_DNA.
DR   PIR; F64058; F64058.
DR   RefSeq; NP_438436.1; NC_000907.1.
DR   RefSeq; WP_005694037.1; NC_000907.1.
DR   AlphaFoldDB; P44604; -.
DR   SMR; P44604; -.
DR   STRING; 71421.HI_0267; -.
DR   EnsemblBacteria; AAC21933; AAC21933; HI_0267.
DR   KEGG; hin:HI_0267; -.
DR   PATRIC; fig|71421.8.peg.282; -.
DR   eggNOG; COG3850; Bacteria.
DR   HOGENOM; CLU_000445_20_10_6; -.
DR   OMA; IKHSQGT; -.
DR   PhylomeDB; P44604; -.
DR   BioCyc; HINF71421:G1GJ1-282-MON; -.
DR   BRENDA; 2.7.13.3; 2529.
DR   Proteomes; UP000000579; 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   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   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..567
FT                   /note="Sensor protein NarQ homolog"
FT                   /id="PRO_0000074811"
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..147
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..567
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          175..228
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          367..566
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         373
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   567 AA;  65238 MW;  A74F54998C6ECAB9 CRC64;
     MYTKGSVSTR IAKYLFIILI VAGVISSLSL AIMSSNKYDA EAINISGSLR MQSYRLLYEM
     QEQPESVETN LRRYHISLHS SALLEVQNQF FTPNVLKHSY QNILQRWTNM EKYARQQDVK
     NYSKQLTDYV ADVDYFVFEL QRFSEQKWIL GVSVLGFAML LILLMVSYVI WYTNREVVKP
     LHLMTKASMQ VQMRQFNHIP LDTRKQNELG TLARVFTQMS TELGQLYSRL EEAVNEKTQK
     LRQTNRTLST LYQSAQLLNT NTINDKILNQ VLNYIFISDH LNFVKVEVMG AEHWDITLGK
     QDANNELQIE TLSVDNEELG VLSWQAGLPC PDPRIMQNLA QMLARALYFH KNLRQKEQLL
     LMEERSIIAR ELHDSLAQVL SFLQIQLTLL KHNLKKEDEQ SKEKSLAIIA NFEQALSGGY
     AQLRELLATF RLTIQEANLQ LALKQVIDSL RSQTTMQMNV NCQLPSQSLN PQQLVHVLQI
     VREATTNAIK HSQGTVIEIS ARINAEGEYE ILVEDDGVGI PNLEEPEGHY GLNIMAERCR
     QLNAQLHIHR REQGGTQVKI TLPHTLY