ID   NTRYL_RICBR             Reviewed;         610 AA.
AC   Q1RJB3;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Putative sensor histidine kinase NtrY-like;
DE            EC=2.7.13.3;
GN   OrderedLocusNames=RBE_0470;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: Member of the two-component regulatory system
CC       RBE_0470/RBE_0312. {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; CP000087; ABE04551.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1RJB3; -.
DR   SMR; Q1RJB3; -.
DR   STRING; 336407.RBE_0470; -.
DR   PRIDE; Q1RJB3; -.
DR   EnsemblBacteria; ABE04551; ABE04551; RBE_0470.
DR   KEGG; rbe:RBE_0470; -.
DR   eggNOG; COG5000; Bacteria.
DR   HOGENOM; CLU_019564_1_0_5; -.
DR   OMA; SKFARMP; -.
DR   Proteomes; UP000001951; 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..610
FT                   /note="Putative sensor histidine kinase NtrY-like"
FT                   /id="PRO_0000282372"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          314..368
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          385..596
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         388
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   610 AA;  68791 MW;  63EA83B7D5F3A878 CRC64;
     MPKLKIFLFK YLYSKRFIGI LVAIAIIFSY FTYYTISIGT KNGAVNSSKV IWFLLIDLII
     FLVLGILLTR KFFQSFFFKN SDQNTSKLQN RIVVAFSLAA AIPTIIVSIS SAYFLNLSIQ
     AWFDRKISVV LDQSIMVADS YIAEHKVLLR ETALAVAEDL SDMYYDLIHN PALFTKTLNT
     EAEMRSLDEA IVLNKSTNTI IANSYLSFSL SFATIPAHLI KKADSCEPVE VKSDPTKIRM
     LIKLKEYNDV YLLVGRSIDN KIIDHIDATN GAAAEYHRLK NQIGNIQIKF SIIFIFIALL
     LLLIAISFGV IVTAKIVNPI KKLVIATDKV KSGDLTVQVP ENEVDKDEIG TLYAAFNRMI
     KQLSRQQRDL VIAQRALAWS DVAKKVAHEI KNPLTPILLA SERLLKKFSP EIKERAEFEN
     YLKMIIRHTN DIKNIVSEFV LFARLPAPKF TNCDLIYVIN NIVEARKLLN NNILYSFETN
     IDQFDFTCDT TQINQVMINL LKNAEESLEG SNQAAIKVNI NTSEQFINIT VLDNGRGFPP
     ELIGKATESY VTTRSKGMGV GLAIVKRIVE EHCGVLDIAN RETGGAVIDI RFNLEELKLK
     VKRHEIGVIS