ID C8X172_DESRD Unreviewed; 760 AA.
AC C8X172;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Dret_0878 {ECO:0000313|EMBL:ACV68169.1};
OS Desulfohalobium retbaense (strain ATCC 49708 / DSM 5692 / JCM 16813 /
OS HR100).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfohalobiaceae; Desulfohalobium.
OX NCBI_TaxID=485915 {ECO:0000313|EMBL:ACV68169.1, ECO:0000313|Proteomes:UP000001052};
RN [1] {ECO:0000313|Proteomes:UP000001052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5692 {ECO:0000313|Proteomes:UP000001052};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Desulfohalobium retbaense DSM 5692.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACV68169.1, ECO:0000313|Proteomes:UP000001052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5692 {ECO:0000313|EMBL:ACV68169.1,
RC ECO:0000313|Proteomes:UP000001052};
RX PubMed=21304676;
RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Desulfohalobium retbaense type strain
RT (HR(100)).";
RL Stand. Genomic Sci. 2:38-48(2010).
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; CP001734; ACV68169.1; -; Genomic_DNA.
DR RefSeq; WP_015751327.1; NC_013223.1.
DR AlphaFoldDB; C8X172; -.
DR STRING; 485915.Dret_0878; -.
DR KEGG; drt:Dret_0878; -.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG3850; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_89_29_7; -.
DR Proteomes; UP000001052; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.290; -; 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; 2.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 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); 2.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACV68169.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 222..275
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 349..400
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 401..472
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 533..757
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 760 AA; 85683 MW; 942538CC86F2C9DF CRC64;
MRHFWHFLRH SLFAKIILSA GATLLAGCLL LILLHTRYHK HVVFDFVHTG GERLSTTIKQ
GTHYAMMLNS REDIAQTIAN ISKQEAITAI RIFNKQGAIK YSSHPGEVDT HVARTAPVCS
SCHHNGGLKP DSDISQRTRI LPATENTPRR MGIVTPIENQ PSCSQASCHV HPATDNVLGI
LEVVMSLKNT DQELASFNQR TLLFGTLVFA LTGVAIFWTI YRFVKRPVRD LIRYTRRISS
GAPPTAILSL DQSDEIGELA SAVSTMHEKI NEKHKELLHQ KEEYQTLFDH VPCIVTVQDR
NFQLISYNRE FSDKFNPSAG DFCFRAYKGR HEKCPDCPVE RTFADGCSHS SEESVVRDGQ
EVHWLVTTSP ICDAEGRIVA AMEMCLDITP RKRLERQLAM SEKKYHAIFN NIPNPVFVLD
PEKLFILDCN DSVQAVYGYT REEILNRPFA DLFFDDDRDH YLPRLHECLV INQARQQTKD
KRRIFVTIRV SPSQYPGQQV LLVTTSDITK RLEAEQQLIQ ASKMATLGEM ATGVAHELNQ
PLSVIKTAST FFVRKIDKNE PIAPETLASM AREIDGHVDR ATKIINHMRE FGHKSEHKLY
PVQVNTVLQR AFEIFSQQLK LRQIEISWNL ETALPHIQAD PDRLEQVFIN LLINARDAIE
TRHASAPEKA EKRITLASRF ADDQVQVCIT DSGIGIAPGD RDKIFEPFYT TKEVGKGTGL
GLSISYGIIQ ECGGRITVFS HGPGHGATFS LHFPPHPTSA
//
