ID A0A1G9P702_9BURK Unreviewed; 744 AA.
AC A0A1G9P702;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05428957_101236 {ECO:0000313|EMBL:SDL94578.1};
OS Oryzisolibacter propanilivorax.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Oryzisolibacter.
OX NCBI_TaxID=1527607 {ECO:0000313|EMBL:SDL94578.1, ECO:0000313|Proteomes:UP000198552};
RN [1] {ECO:0000313|Proteomes:UP000198552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPL6 {ECO:0000313|Proteomes:UP000198552};
RA Varghese N., Submissions S.;
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};
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DR EMBL; FNHP01000001; SDL94578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9P702; -.
DR STRING; 1527607.SAMN05428957_101236; -.
DR OrthoDB; 5389366at2; -.
DR Proteomes; UP000198552; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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; PF00989; PAS; 1.
DR Pfam; PF13188; PAS_8; 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; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198552}.
FT DOMAIN 354..577
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 626..742
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 39..66
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 196..223
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 677
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 744 AA; 80212 MW; 08F19AD43773AAB9 CRC64;
MSRPDLSFLM HAAGGEEGSA APAQAPAPAD ERRGPARARG DVAALIEELR ASKAELEAQN
HMLRYSQAVA ESASERFEAL FSSVPLALMV LDEHDMVVQA NSMAQRSFQP AEHDRPLVSL
MPFVDPAHAA RVQAAFDAAR HQATAEATEV VFRLDAERAI TGDLHIARIE SRTEDEQPLT
QFLCAVIDQG PLLAERQALQ KSAAELRERN EQLHTSERRL EAVINSALDA IICVDQHQRI
TVFNPTAAML FQCPASDALG SAITRFIPNA EQLLAFAQLT TQAVLGEMTA LTASGRELAV
EIGVSFERHA GGETTTVFAR DLTARKRAEA RRAELEGQLR ESHKMQAVGT MAGGIAHDFN
NILHAILGNV ELARADCPPG SPVCDSLVEI DKAGRRARDL VRQILTFSRN EPPRRARVSL
TDVARDTQQL LRVTLPPQIE LTVHEADGVP PVLADATQVE QALLNLCTNA VHAIGAQRGR
VEVDIAVAQP AQRLRERLTL SGDRYVAVSV RDDGPGMDEA TLTRIFEPFF TTKPVGQGTG
LGLAVVHGVM RTHEGAVDVH SVPGEGSRFT LYFPALLKLR AADDGAPPAH GGAPGTATPA
TAPAPAALLV ATAPEPTPDA PGRQRHVMYV DDDEALVLLV QRLLRRRGYV VSGFTDPRQA
TQALQEAPER YDLLVTDYNM PGFSGLDLVR AAHAIRADLP IALASGYVTA DIEQQALAEG
ARALIHKPND VQELCATVDR LVHG
//