GenomeNet

Database: UniProt
Entry: A0A1I2F1Q1_9BURK
LinkDB: A0A1I2F1Q1_9BURK
Original site: A0A1I2F1Q1_9BURK 
ID   A0A1I2F1Q1_9BURK        Unreviewed;       749 AA.
AC   A0A1I2F1Q1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-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=SAMN04489711_10945 {ECO:0000313|EMBL:SFE98949.1};
OS   Paracidovorax wautersii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=1177982 {ECO:0000313|EMBL:SFE98949.1, ECO:0000313|Proteomes:UP000199119};
RN   [1] {ECO:0000313|EMBL:SFE98949.1, ECO:0000313|Proteomes:UP000199119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27981 {ECO:0000313|EMBL:SFE98949.1,
RC   ECO:0000313|Proteomes:UP000199119};
RA   de Groot N.N.;
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FONX01000009; SFE98949.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2F1Q1; -.
DR   STRING; 1177982.SAMN04489711_10945; -.
DR   OrthoDB; 5389366at2; -.
DR   Proteomes; UP000199119; 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; 2.
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; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}.
FT   DOMAIN          216..287
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          354..577
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          629..745
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         680
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   749 AA;  80362 MW;  FE4DF17D55B48D0F CRC64;
     MTRPDLSSLF RHLQDSSSAD GGSSLPPGQP ERRRPGRATE EVGQLIAELR ASQAELEVQN
     RVLSFSQAAA ESASERFETL FASVPLALMV LDEHDMVVQA NSMAHRSFQP TEADRPLTSL
     MPFVSEADAP RVREAFDAAR SAGSAEVTEV VFHTGESARI NGDLHIARIE AKQDDDPTAL
     QFLCAVIDQG PLLAERRALQ DSAATLKERN AQILASERRL EAVINSALDA IICVDPQHRI
     TVFNPTASAL FVCAQEDALG SPLERFLPDA AQAMAMAQVT TQAVLGEVTA LTATGRELAV
     EVSLSFENQG DGTSATVFAR DLTGRKKAEA HRNELEAQLR ESHKMQAVGT MAGGIAHDFN
     NILSAILGNV ELAKADAGAD APMLESLLEI EKAGRRARDL VRQILTFSRN EPPKRTAVPV
     QETLNDTVRL LRVTVPPAVD LQVRIDPGVP PMLADPTQVE QALLNLCTNA IHALGDQRGT
     VLLQATYAQP DPRVCERLSL LPGDYVCLRV SDNGPGMDAA TQQRIFEPFF TTKPVGQGTG
     LGLAVVHGVM RTHGGAVDVY SLPGEGSSFT LYFPSAGPGT TDSLPQDAGA SVADTRAPAV
     PPPAAIAPAP PATEEAAATQ AEEEPRLRHV MYVDDDQALV FLVQRLLRRR GYRVSGFTDP
     HEATAALRAD PQAYDLVVTD YNMPGYCGVD LVREARRIRP GLPVALASGY ITTEIEQAAL
     AEGAQALIHK PNDVEELCAT VHRLVHGGE
//
DBGET integrated database retrieval system