ID   NTRYL_RICPR             Reviewed;         599 AA.
AC   Q9ZCU7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Putative sensor histidine kinase NtrY-like;
DE            EC=2.7.13.3;
GN   OrderedLocusNames=RP614;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
CC   -!- FUNCTION: Member of the two-component regulatory system RP614/RP562.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA15057.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ235272; CAA15057.1; ALT_INIT; Genomic_DNA.
DR   PIR; G71666; G71666.
DR   RefSeq; NP_220981.1; NC_000963.1.
DR   RefSeq; WP_004599164.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCU7; -.
DR   SMR; Q9ZCU7; -.
DR   STRING; 272947.RP614; -.
DR   EnsemblBacteria; CAA15057; CAA15057; CAA15057.
DR   GeneID; 57569739; -.
DR   KEGG; rpr:RP614; -.
DR   PATRIC; fig|272947.5.peg.633; -.
DR   eggNOG; COG5000; Bacteria.
DR   HOGENOM; CLU_019564_1_0_5; -.
DR   Proteomes; UP000002480; 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; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..599
FT                   /note="Putative sensor histidine kinase NtrY-like"
FT                   /id="PRO_0000282375"
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;  67237 MW;  A228CB1E37B12D79 CRC64;
     MLSDLKQNLR SYFSSRILIL ALAIASIISV CTTFYVISLE AKNFSTIIGF LLIDLAIFLI
     LGILLTQKFF TKNNDNDSSK LQNRIVIAFS LVAAIPTIIV SVFSVYFFNL SVKAWFDKKI
     STVLDQSVIV AETYIAEHKV QLKETALAVA EDLSDMYYDL IHNPALFTKT LNTEADMRSL
     DEAIVLNKST NTIVANSYLS FSLSFATIPA HLIKKADLGE PVEVKSDPTT IRMLIKLKEY
     NDVYLLVGRL VDNKIIDHID ATNGAAAEYN SLKNEIDNIQ IKFSIMFIFI ALLLLFVAIN
     FGVLFTAKIV KPIKKLVTAT DKVKDGDLTV QVPENEVDKD EIGTLYAAFN RMIKQLSRQQ
     RDLVIAQRAM AWSDVAKKVA HEIKNPLTPI LLASERLLKK FSSEINEKSE FESYLKMIIR
     HTNDIKNIVS EFVLFARLPA PKFTKSELVY LVKHIIEARK LLNDNIVYTY DSNVDQFDFM
     CDATQINQVM INVLKNAEES IEGQEFGKID VILDAKDDFI SVIVMDNGKG FPPELIGKAT
     ESYVTTSSKG MGVGLAIVKR IVEEHCGVLD IANREDEGAI IDIKFDLKEL HLKVRRSGG