ID C8X0E0_DESRD Unreviewed; 596 AA.
AC C8X0E0;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Dret_0468 {ECO:0000313|EMBL:ACV67765.1};
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:ACV67765.1, 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:ACV67765.1, ECO:0000313|Proteomes:UP000001052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5692 {ECO:0000313|EMBL:ACV67765.1,
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; ACV67765.1; -; Genomic_DNA.
DR RefSeq; WP_015750923.1; NC_013223.1.
DR AlphaFoldDB; C8X0E0; -.
DR STRING; 485915.Dret_0468; -.
DR KEGG; drt:Dret_0468; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_2_7; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000001052; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR031967; PhoR_single_Cache-like_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF08448; PAS_4; 1.
DR Pfam; PF16736; sCache_like; 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; 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.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACV67765.1};
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 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 192..244
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 374..594
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 596 AA; 66903 MW; 503CBE2CD7A304AB CRC64;
MSLRTKLLSV LLGLLFLASF VPLFLSKQVL HEELLAAAKR EAVLKLGHMQ WLMRKGLAQE
GPAGLNEQFR QIGKQLDVRI TYIRQDGTVL ADSSLPLRKV RQLENHKQRP EVQEAMQRRF
GSSLRYSETL KTDLLYVART MEATSEIPEG FIRMAVHLSA VDKRLDGLFQ QYLILFVIGL
AVCAVVSFWL ASRVSRAMLR MGQTADAIGN GEYDKRIAFT PAREFLPLAQ AINRMARRIQ
SHITTISDQN RQFESILNGM HEGVMVLDRQ GKVSMVNTEL KNILEVTSPV GRAPIELIRS
PELQGACEAM VAATVGKQSM EPAQLQVETM QERIYDVNLL PLPAESQDIS AIVVFHDITE
LKRLERVRRD FVANVSHELR TPLTSIKGYA ETLLDMGQVE TEAVHAYMQV VVKNANAMSR
LLEDLLQLSK LESNAGDREL GPVLLTNAIQ AAWKYCQPMA EEHHVSLNQS QIPAGVCVWS
EYDPLVQVLR NLFENAIKFS PENTEVRIEA EQDGPIWQIS VVDSGPGVGQ REQERIFERF
YRVQHGSKQV AGTGLGLAIA RHIVRNHVGR IWVESPVPGQ IEGSAFRFTL RECSSA
//
