ID   NTRYL_RICCN             Reviewed;         599 AA.
AC   Q92H24;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Putative sensor histidine kinase NtrY-like;
DE            EC=2.7.13.3;
GN   OrderedLocusNames=RC0948;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- FUNCTION: Member of the two-component regulatory system RC0948/RC0849.
CC       {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 membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AE006914; AAL03486.1; -; Genomic_DNA.
DR   PIR; D97818; D97818.
DR   RefSeq; WP_010977545.1; NC_003103.1.
DR   AlphaFoldDB; Q92H24; -.
DR   SMR; Q92H24; -.
DR   EnsemblBacteria; AAL03486; AAL03486; RC0948.
DR   KEGG; rco:RC0948; -.
DR   HOGENOM; CLU_019564_1_0_5; -.
DR   OMA; SKFARMP; -.
DR   Proteomes; UP000000816; 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   CDD; cd00082; HisKA; 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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR045671; NtrY-like_N.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF19312; NtrY_N; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 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 membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..599
FT                   /note="Putative sensor histidine kinase NtrY-like"
FT                   /id="PRO_0000282373"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          307..361
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          378..589
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         381
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   599 AA;  67493 MW;  0BD9838E96917AA2 CRC64;
     MLSYLKQNLH SYFSSRVLIF TLATAAIIFA CATFYVISLE SKNFSTIIGF LLVDLAIFLI
     LGVVLTQKFF TKNNNNDSSK LQNRIVIAFS LVAAIPTIIV SVFSVYFFNL SVQAWFDKKI
     STVLDQSVIV AESYIAEHKL QLKETALAVA EDLSDMYYDL IHNPALFTKT LNTEAEMRSL
     DEAIVLNKST NTIVANSYLS FSLSFATIPA HLIKKADLGE LVEVKSDPTK IRMLIKLKEY
     NDVYLLVGRL VDNKIIDHVD ATNGAAAEYN SLKNEIDNIQ IKFSIMFIFI ALLLLFVAIS
     FGVIFTAKIV KPIKKLVTAT DNVKDGDLTV QVPENEVDKD EIGTLYVAFN RMIKQLSRQQ
     RDLVIAQRAM AWSDVAKKVA HEIKNPLTPI LLASERLLKK FSPEIKERVE FENYLKMIIR
     HTNDIKNIVS EFVLFARLPA PKFTKSELVY LVKHIVEARK LLNDHILYKF ESNVEQFDFM
     CDATQINQVM INLLKNAEES IEGRESGKIE VTIDVKDDFI SVIVTDNGKG FPPELIGKAT
     ESYVTTSSKG MGVGLAIVKR IVEEHCGILD IANREAEGAI IDIKFDLKEL DLKAKRLEM