ID A0A345DZZ5_9EURY Unreviewed; 842 AA.
AC A0A345DZZ5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DU500_03170 {ECO:0000313|EMBL:AXG05517.1};
OS Haloplanus rubicundus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloplanus.
OX NCBI_TaxID=1547898 {ECO:0000313|EMBL:AXG05517.1, ECO:0000313|Proteomes:UP000253273};
RN [1] {ECO:0000313|EMBL:AXG05517.1, ECO:0000313|Proteomes:UP000253273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBA1113 {ECO:0000313|EMBL:AXG05517.1,
RC ECO:0000313|Proteomes:UP000253273};
RA Kim Y.B., Roh S.W.;
RT "Genome sequences of Haloplanus sp. CBA1113.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; CP031150; AXG05517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345DZZ5; -.
DR KEGG; haj:DU500_03170; -.
DR OrthoDB; 8127at2157; -.
DR Proteomes; UP000253273; Chromosome.
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; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; 1.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 378..441
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 626..833
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 733..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 842 AA; 91819 MW; CAD7152AB1362C7C CRC64;
MGPGTDPIRV LHVDDDPAFL DVAATLLERK DDRIEVVTAT SADEGLERLD DADIDCIVSD
YDMPGLNGID FLERVRASGD GRPFVLFTGK GSEEVASEAI SAGVTDYLQK APGSEQYEIL
LNRIVNAVEA ARIRARATRQ ERINTLIRES NRRLVAADTV EDIEGAVCRT LTNATPFRFA
WIGEPEANGE IVPRTSAGDA DDYLDEVTIY HDDRPRGQGP GGRAIRTDEL QVAQNIPDDP
SFAPWHDVAE RYGYESVTVV PLSYGGGRTG ILAIYADSPH AFDEVELSVL EELGETIGRA
LEAAETRRRL ESRRAAERTR KEGHYRTLVD ALPNGAIALF DTDLRYTVVG GAVFDDLDLS
PEDMEGEALT AVHSTAFCEA YLQHYRAVLD GAERTFEFEY ADRTFEAHVA PVRDETGAVD
GGIAMTQDVT DRVRRQRELR RRERVLRETY EVIADPSLSV EEGVRRLLAI GADVLDVRYG
ILSRVDGDEY AFEVVHAPDE DGKAVGDGGP AEGDTVALTA TNCERVVRSG ETVAVADVSD
DPDCDARTPA AESDLACYVG APVVIDGETD GTFCFYDTDP HDGAFSEWEL TLVDLLSRWV
GVALDRHETN ARLRTQNERV REFTSIVSHD LRNPLTVLGG ALELAEATGE TEQFDRCRRA
LDRMGSLVDD LTTLTREGAV VTDAEPVALG WAARACWETV ETGTAELRLD GDAPILADEA
RLRQLLENLF RNSAEHGSTD NRRGDAGDSV EHGSTDDDGL TVRVGVLDDG FYVEDDGVGI
PEDERARVFE RGYSTTATGT GLGLSIVEKM AAAHGWTVAV SESDAGGARI DVRGVEMDDG
RE
//
