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Database: UniProt
Entry: A0A3S2U1Z6_9BURK
LinkDB: A0A3S2U1Z6_9BURK
Original site: A0A3S2U1Z6_9BURK 
ID   A0A3S2U1Z6_9BURK        Unreviewed;       652 AA.
AC   A0A3S2U1Z6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ENE75_15985 {ECO:0000313|EMBL:RVT50501.1};
OS   Rubrivivax albus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Rubrivivax.
OX   NCBI_TaxID=2499835 {ECO:0000313|EMBL:RVT50501.1, ECO:0000313|Proteomes:UP000288178};
RN   [1] {ECO:0000313|EMBL:RVT50501.1, ECO:0000313|Proteomes:UP000288178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICH-3 {ECO:0000313|EMBL:RVT50501.1,
RC   ECO:0000313|Proteomes:UP000288178};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) 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:RVT50501.1}.
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DR   EMBL; SACT01000005; RVT50501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S2U1Z6; -.
DR   OrthoDB; 8929028at2; -.
DR   Proteomes; UP000288178; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 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; 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   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF12860; PAS_7; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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; 1.
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:UP000288178}.
FT   DOMAIN          231..283
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          296..516
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          538..650
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         588
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   652 AA;  71267 MW;  5BD25BFE67BD1D0B CRC64;
     MSTPSSPIED PLKRYRSLQA ALDLIDQGFT LIDNDLGLLA WNRSFLRLLD FPDTLAFPGA
     PFEGFIRYNA DRGEYGPGDA AAQVAERVEA ARRFESHEFE RVRPDGTVLK VRGVPVPGIG
     FITLYSDITA QKRAERQILE HAAELERRVA ERTSELRLSE AQMRLITDSI PALIAYFDHR
     KAYRYINRGY QDWFGLDPRR LDRVSAREFL GDTTYEAIRP NVTRAFAGEA VTYEYEARCV
     DGRVRTARTT LIPEKSADGA VVGCFELTFD VSELRRTQQQ LAQAEKMEAL GQLTGGIAHD
     FNNMLTVIIG NLGALRERMG DGEQAADFVD PTLAAARRGV DLIRALLGFA RRQPLNAGAA
     DIAPLAGTVV KLLRRSMPEG LKLEVDAGEK PLRAWVDASQ LQDALVNMIL NARDAKASRV
     TVRTAPAVLT PERAEELQAT PGPCVRIDVA DDGQGMDAAT RARVFEPFFT TKRHGAGTGL
     GMSMVYGFVR QSGGAIDIDS ALGRGTVVSL WLPVAAGAER ADIEVEAAGA ERVAGRSLAL
     LVEDDPDVRK VVRRSLIDLG FAVVEAENGT EAMTILDHTP QIDLLLSDVV MPGPVDGREV
     ARHALARRVP RVALMSGYAP GEIGNGPEGV PMLAKPFTQR QLADLVRHPA RD
//
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