ID V5TMD4_HALHI Unreviewed; 859 AA.
AC V5TMD4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HISP_11045 {ECO:0000313|EMBL:AHB66506.1};
OS Haloarcula hispanica N601.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=1417673 {ECO:0000313|Proteomes:UP000018572};
RN [1] {ECO:0000313|EMBL:AHB66506.1, ECO:0000313|Proteomes:UP000018572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N601 {ECO:0000313|EMBL:AHB66506.1,
RC ECO:0000313|Proteomes:UP000018572};
RX PubMed=24625874;
RA Ding J.Y., Chiang P.W., Hong M.J., Dyall-Smith M., Tang S.L.;
RT "Complete Genome Sequence of the Extremely Halophilic Archaeon Haloarcula
RT hispanica Strain N601.";
RL Genome Announc. 2:e00178-14(2014).
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; CP006884; AHB66506.1; -; Genomic_DNA.
DR RefSeq; WP_014040887.1; NC_023013.1.
DR AlphaFoldDB; V5TMD4; -.
DR GeneID; 25154780; -.
DR KEGG; hhn:HISP_11045; -.
DR HOGENOM; CLU_000445_114_58_2; -.
DR Proteomes; UP000018572; Chromosome 1.
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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
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; 4.
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; IPR001610; PAC.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 9..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 217..269
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 270..340
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 342..394
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 391..461
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 466..518
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 515..585
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 590..642
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 646..859
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 755..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 859 AA; 94813 MW; 1E6BD15B3B7A3606 CRC64;
MSGHGGEISV LHVDDDPDLG DLVAVHLEQT HNDISVCTVR SAADGLQRLS ERTFDCVVSD
HDMPGMDGLE FLKVVREEYE ELPFILFTGK GNEEIASDAI SAGVTEYLQK GVGTDQYTVL
ANRIERAVGE RRAKVALEES ERMLSTLISN LPGMVYRARN VPDWPMEFVS DGATELVGYS
SEALESGDVS WGTLIKESET ERLWETVQTC IAADEPFEVS YQIETADGET RWMWERGRVV
GTDDDGVEIL EGFITDVTAR EERERELANQ RAFTEKLIDS VDDMFYVVGP DGSLVRWNDT
VSSVTGYTNE KLASMGIGEL IVDSDHEKLW RVFEETLETG YGTVEAGVET ADGRALQYEF
KGSLIEDERG DLFGIAGIGR DITERKRRER ELREYRTLVE NVGDPMYVLD TDGTVEMVNE
AMAAHLGYDR SEIVGSEPVR FMPETDVERA TALICNLLDD DERTWGAYEM RTISADGTVR
INEDRIAPLF DEDGNFDGSV GVMRETTERK QRERELERYE TIIEAVGDPV YTLDDEGVFT
YVNEAIEQLT GFEPDELIGE HISTIMTGED INRGSELIRT ILSDPTRQNV TFETDIVDQT
GNHTPIEIHI ALLPAADGEF NGTAGVIRDI SDRKDRERQL AEFASVVSHD LRNPLNVVKG
RISVARTSGD VSHLEAAESA ADRMDELIND LLTLARQGDT VGETTMVDLA ALASQAWIDV
ETGEATLEKH GTAAVEADAA RLRTVFENLF RNSVEHGSTS SRTESDDSVE HGRCADGAAP
VTVSVGTTDD GFYVADDGVG IPPEERDDVF ERGYTTSDTG TGFGLAIVVE VAQAHGWSVS
VTESEDGGAR FEFTTSSER
//
