ID G0HRB1_HALHT Unreviewed; 748 AA.
AC G0HRB1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=htlD {ECO:0000313|EMBL:AEM57096.1};
GN OrderedLocusNames=HAH_1487 {ECO:0000313|EMBL:AEM57096.1};
OS Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182
OS / NCIMB 2187 / VKM B-1755).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=634497 {ECO:0000313|EMBL:AEM57096.1, ECO:0000313|Proteomes:UP000005629};
RN [1] {ECO:0000313|EMBL:AEM57096.1, ECO:0000313|Proteomes:UP000005629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 /
RC VKM B-1755 {ECO:0000313|Proteomes:UP000005629};
RX PubMed=21994921; DOI=10.1128/JB.05953-11;
RA Liu H., Wu Z., Li M., Zhang F., Zheng H., Han J., Liu J., Zhou J., Wang S.,
RA Xiang H.;
RT "Complete genome sequence of Haloarcula hispanica, a model haloarchaeon for
RT studying genetics, metabolism, and virus-host interaction.";
RL J. Bacteriol. 193:6086-6087(2011).
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; CP002921; AEM57096.1; -; Genomic_DNA.
DR RefSeq; WP_014040322.1; NC_015948.1.
DR AlphaFoldDB; G0HRB1; -.
DR STRING; 634497.HAH_1487; -.
DR GeneID; 23804970; -.
DR KEGG; hhi:HAH_1487; -.
DR eggNOG; arCOG02333; Archaea.
DR HOGENOM; CLU_000445_114_58_2; -.
DR OrthoDB; 8127at2157; -.
DR Proteomes; UP000005629; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
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; SSF55781; GAF 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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 136..206
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 253..326
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 329..381
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 553..741
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 526..553
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 60
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 748 AA; 82623 MW; 7376C71BFF83D92C CRC64;
MTDIAGTMRI LHVDDEPGFA DMTATFLERE DDRLDVQAAT SVAAGLEILT DTDIDCVVSD
YDMPDRNGIQ FLETVREEYG SLPFILYTGK GSEEIASDAI SAGVTDYLQK QSGTDQYAVL
ANRITNAVES QRVKRERNRQ LDAIETAQEG ISILDEDGTF IFVNEAYADL YGYEPDEMVG
EHWELLYQAE DIPRIYDEIV PTVDETGYWS GTTTGLRADG STFTEDHVLA RTDRGELVCT
VRDISDQRDG EEELSRIKRA MDEAPVGITI TSPEQDDNPI TYANRQFLEL TGYTESEVYG
RNCRFLQGEE TESEPVDAMR AAIDADEPVS VELRNYRKDG TMFWNQVTIA PVRDDDGTVV
NYVGFQQDIT ERKEHEHRLR ALSESVQNLL QADTREEVAE IGVDTACTVL GLEANTIHLY
DEGDRTLEPV AASDAIYDLL DDLPTFTPGG SIAWRVYESG DALAVDDVHA DPDIYNPDTP
IKSELYLPLG EHGILLAGSE TAAAFDQRDV VLGEILAGHV TSALKQVEGT EQLRDHQQEL
EQHNDRLEAF TSVVSHDLRN PLTVAEGRLE LAREECESEH LAAVERAHER MDTLITDLLT
LAQDGETVTD REPVALASLV EDCWTNVETA DATLVTDIDR TVLANESRLK QLFENLVRNA
VEHAGADVTV TVGAVDDGFY VADDGPGIPE ADRDTVFEVG YSTSTEGTGF GLSIARKVAE
AHGWEINVRD SADGGARFEV TGVSFDEV
//
