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Database: UniProt
Entry: A0A1R1I1D2_9RHOO
LinkDB: A0A1R1I1D2_9RHOO
Original site: A0A1R1I1D2_9RHOO 
ID   A0A1R1I1D2_9RHOO        Unreviewed;       791 AA.
AC   A0A1R1I1D2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BJN45_14820 {ECO:0000313|EMBL:OMG52555.1};
OS   Azonexus hydrophilus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Azonexus.
OX   NCBI_TaxID=418702 {ECO:0000313|EMBL:OMG52555.1, ECO:0000313|Proteomes:UP000187526};
RN   [1] {ECO:0000313|EMBL:OMG52555.1, ECO:0000313|Proteomes:UP000187526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS02 {ECO:0000313|EMBL:OMG52555.1,
RC   ECO:0000313|Proteomes:UP000187526};
RA   Salah Z., Rout S.P., Humphreys P.N.;
RT   "Alkaliphiles isolated from bioreactors.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMG52555.1}.
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DR   EMBL; MTHD01000005; OMG52555.1; -; Genomic_DNA.
DR   RefSeq; WP_076096582.1; NZ_MTHD01000005.1.
DR   AlphaFoldDB; A0A1R1I1D2; -.
DR   STRING; 418702.BJN45_14820; -.
DR   OrthoDB; 8552871at2; -.
DR   Proteomes; UP000187526; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000187526}.
FT   DOMAIN          198..252
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          328..381
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          417..637
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          665..781
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         714
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   791 AA;  87496 MW;  F2AE802C96967954 CRC64;
     MPVVACSVVE ASFLVALAES VSVIAATGDV GTLLGYPAVA LVQGEVSLPE RIHGDDADIA
     EALFGPDIPR GEQVDNLRLR QASGRIRCVK AIYAKRQRDD GVVELTLRLQ DAKSLPRTMD
     DAANTANFRA MMENTNDFVY FKDRNHVFTG ASQTLVSLCH PAEQWTDLLG LTDYDVFPEP
     YADLYYRLEK QVFSGVAAAQ EIQEFLSKDG QLNGWVDNRK FPIHDEAGEI IGLFGVARDI
     TERIHAENRL KESEYFFRDS QRAANIGSYK FDICYDCWTS SEVMEQIFGI GPDYPRTLQG
     WLEAVHPDDR QMMQDYFTSN VLKNREPFNK EYRILRRSDG EMRWVLGLGQ LRFDDDGQPC
     WMLGTIQDIT ERKQLDAELA HYRHNLETLV EERTLELSKA KDAAEAASFS KSAFLANMSH
     EIRTPLNAIT GMAHLIRKGG LSPLQIDQLG KLESAGEHLL EIINAVLELS KIEAGKYLLE
     ETGVSVAGVV GGVVSIMQNR ADAKGLKLRT ELCQLPARLL GDPTRLQQTL LNYLSNAIKF
     TEHGEVVLQV EMLENGDDNV LLRFSVRDTG IGIAPEAVER LFTAFEQADN TTTRLYGGTG
     LGLAIARKLA CMMGGEAGVD STPGIGSTFW FSARLRRCVG DETEMPAATA DDAANAIKRK
     FCGARVLLAE DEPINCEITL LLLEDAGLLA DTAEDGMAAV EKAATNDYAL ILMDMQMPRM
     DGLEATRHIR RLDRQADTPI LAMTANAFAE DRVRCLEAGM VDFIAKPVKP EIFYSVLLKA
     LSAADSRASI L
//
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