ID D2RZ51_HALTV Unreviewed; 973 AA.
AC D2RZ51;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Htur_1083 {ECO:0000313|EMBL:ADB59975.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB59975.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB59975.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(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; CP001860; ADB59975.1; -; Genomic_DNA.
DR RefSeq; WP_012942284.1; NC_013743.1.
DR AlphaFoldDB; D2RZ51; -.
DR STRING; 543526.Htur_1083; -.
DR GeneID; 8741671; -.
DR KEGG; htu:Htur_1083; -.
DR eggNOG; arCOG02358; Archaea.
DR eggNOG; arCOG02369; Archaea.
DR eggNOG; arCOG02387; Archaea.
DR eggNOG; arCOG03567; Archaea.
DR HOGENOM; CLU_009094_0_0_2; -.
DR OrthoDB; 106630at2157; -.
DR Proteomes; UP000001903; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR025847; MEDS_domain.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF14417; MEDS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 3.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 3.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADB59975.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 758..971
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 110880 MW; D13A99BABC557C83 CRC64;
MNNEVERNDR RSASDRETEF EARSRGSTFR GPTGPVGDHD HSDDHLALLY GSRDEQFDAV
IPFVRRGLEA DERCLYLADE TDRDEIFEAL RDDGVDVDEA LESDALVIRD TEDAYLRDGS
LDLEASLDLL ETFVEESTAD SEGARVTAEE TWLLRAAEEA DEFMALEARV NERLGGEDCA
VLCQYDCERF PAHVLEDVIK THPYLVTDRT ISENFYYTPP ETFFDGEEPA TTVDRMIRTV
RERTDAKTAV REHRDYLRDL YEATANADLT FEERVERLLE LGCERFDLRG GALAHLPTWD
DNFRAEVTVG PDMGDLEGEL PIQPTEGNFC RQAIDWDEPT AVPDVVAAGW DDDPVFEEFG
FATYFGIRVT AGTEPYGTFW FYDTEPRDRP FTEAERTFLE LMGQWISTEL ERRRREEFLR
TSYEITSDPD LTFAAKIERL LEHGRKWFGC DVGYFTAVDA ETDRFEIVEA VGSHDRIRTG
GGGSLSGTYC KKVVEAGESI SVADAVDAGW EGDRAYDTYG LDAFLGTMLE VDGERFGTLC
FGSETPREGS FTETEYTFID LISQWVSTEL ERRRDERTQR ELYEITADPD RSFDEQLLAV
LDLGCERFDM ELGGIATVDP ATDRFEVETT NGDHEYLTPG KPYPLSETYC QAPVDEEGTC
TITDPVERGY DGKLCYERFG VRAYLGTHLE IEGSPDRTFW FVSTESREEF SEAERTLHHL
MGQWVKYELD RQQYERDLEE TVERLQQSND RLKQFAYAAS HDLQEPLRMV SSYLQLLDNR
YKGELDEEAR EFIDFAVDGA DRMREMIDDL LAFSRVEHAD GEFEPVDCTE VLDRVQDDLQ
VRIAETDAEI LVDSLPTVSA DVEQFEQLFS NLVSNGIKYN ESAVPRVEVS AADRDDRWEF
AVADNGIGIE SAKTDRIFEV FKRLHHDDEY PGTGIGLSLC QEIADNHGGD IRVESEPGAG
STFYITLPKR NFE
//