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Database: UniProt
Entry: A0A1R1IEB2_9RHOO
LinkDB: A0A1R1IEB2_9RHOO
Original site: A0A1R1IEB2_9RHOO 
ID   A0A1R1IEB2_9RHOO        Unreviewed;       465 AA.
AC   A0A1R1IEB2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BJN45_01820 {ECO:0000313|EMBL:OMG56899.1};
OS   Azonexus hydrophilus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Azonexus.
OX   NCBI_TaxID=418702 {ECO:0000313|EMBL:OMG56899.1, ECO:0000313|Proteomes:UP000187526};
RN   [1] {ECO:0000313|EMBL:OMG56899.1, ECO:0000313|Proteomes:UP000187526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS02 {ECO:0000313|EMBL:OMG56899.1,
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:OMG56899.1}.
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DR   EMBL; MTHD01000001; OMG56899.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1IEB2; -.
DR   STRING; 418702.BJN45_01820; -.
DR   Proteomes; UP000187526; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187526}.
FT   DOMAIN          23..95
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          114..166
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          225..461
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          179..216
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   465 AA;  52363 MW;  3E347158341D0D30 CRC64;
     MKESNRKLLE SEHKRASDSR RNLQLFLSQI IDGDPVPTLV IDASHRITHW NKACAAISGL
     PAEQMVGTWD QWKAFYPESR PIMADLIVDG SLEERFDNYY HNLFRRSKTI ADAFEAESFF
     PHLGSSGRWL FFTTAPIRDS DGKIIGAIET LQDVTERRLA EEQLLQYQGQ LEAQVESRTQ
     ALARANQQLA KEHEELTNLL RKIEEAQQQL LQSEKMAAIG QLAAGVAHEI NNPIGFVNSN
     LGSLKTYTTN LLHLIDAYES GQAAAIAEAK RQADLEFLRE DLPSLLAESQ EGLDRVTRIV
     QDLKDFSRVD QAERQRADLN AALHSTLNVV RNELKYKADV IIELGEIPEI DCVPAQLNQV
     FMNLLVNAAQ AIPERGKIFV RSGLERDHVW FEIEDTGSGM SEETRHRIFE PFFTTKPVGK
     GTGLGLSISY DIIVKKHHGR VDVRSEPGKG TCFRIWLPID APAND
//
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