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Database: UniProt
Entry: Q24RD1_DESHY
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Original site: Q24RD1_DESHY 
ID   Q24RD1_DESHY            Unreviewed;       592 AA.
AC   Q24RD1;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=DSY3622 {ECO:0000313|EMBL:BAE85411.1};
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE85411.1, ECO:0000313|Proteomes:UP000001946};
RN   [1] {ECO:0000313|EMBL:BAE85411.1, ECO:0000313|Proteomes:UP000001946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51 {ECO:0000313|EMBL:BAE85411.1,
RC   ECO:0000313|Proteomes:UP000001946};
RX   PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE85411.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q24RD1; -.
DR   STRING; 138119.DSY3622; -.
DR   KEGG; dsy:DSY3622; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_2_9; -.
DR   Proteomes; UP000001946; Chromosome.
DR   GO; GO:0016020; C:membrane; 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; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
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; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 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   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001946};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          198..250
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          255..296
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          315..368
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          372..588
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          242..269
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   592 AA;  66424 MW;  5F7C3197D2800574 CRC64;
     MKKKSSFLKR ILILMITTIA LYSFLITIFF WFTTNDMFRE LQTRELKPSA EAIADLVLKY
     QQGTMSKDDL EEHFNLNKGI WNFVVHVYDG QGNLIIKNEE ILTTLFRGKN AEIGLNLNPV
     LKEYFSSVLS GDSVVANKGP FLIVGQPIAH NDSIVGMVFL GKPQIEIFTA LSGLNRSIWI
     SALGVLLLLS FPLYRAARYI AHPLKQMRDV AISMANGNLK EQANEKYGGE IGELAHSLNY
     LSARLSETIS ALELERNRLK QTIDGLAEGI VAIDNEGNFT HINPSIQRIF GKNPGEGRMS
     LIPSQELWED FDAVLAQGYT IVRSLQWKQM LLRVTICPLE DETHHIAGVV GLFRDITESE
     RLEQTRREYV ANVSHELRTP VSALRALSET LADGMVSDEE TKNRYYNHML HETMRLTRLI
     NDLLTLSRLQ SHTEQVHTEA FLINEVTGSV AERYKPLAQK KGLRFDYSPL VHDLKVMSNM
     DLVEQVLIIL LDNAIKYTQS GGRISLGTVL DKDRVKVSVA DTGMGIAPED LPHIFERFYK
     ADKAHSTQGT GLGLAIAFEI SQRLGEEIYV ESHLNEGSTF TFTLSCSGAS AS
//
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