ID A0A1J1LHI5_9CYAN Unreviewed; 751 AA.
AC A0A1J1LHI5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PL9214330001 {ECO:0000313|EMBL:CUR31939.1};
OS Planktothrix tepida PCC 9214.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=671072 {ECO:0000313|EMBL:CUR31939.1, ECO:0000313|Proteomes:UP000184315};
RN [1] {ECO:0000313|Proteomes:UP000184315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Regsiter A., william w.;
RL Submitted (OCT-2015) 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CZDF01000137; CUR31939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1LHI5; -.
DR STRING; 671072.PL9214330001; -.
DR Proteomes; UP000184315; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; 3.
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; 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; 2.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
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; 3.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184315}.
FT DOMAIN 6..58
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 84..147
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 163..216
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 244..290
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 293..345
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 370..593
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 634..750
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 49..76
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 336..363
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 683
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 751 AA; 85009 MW; 8DDC8DF07150EEC0 CRC64;
MAKGNHEVEF RNRTKSGQQI YISLRLSVIR DQEENIIYLI GCSNDISQQQ AALQERKKIE
KQLQQFNQEL ETRVEERTAE LQESQRFIQS ITDNTPNILY IYDLDEQRNI YFNRAIVDIL
GYSPEQIQGM ENQFLLDLVH PDDLDSMLIH LNNLHTLQNG EKRNCEYRLR DVNGEWHWLL
SRDAAFLYNK DGTLKQIVGT AQDITERKQS EEKLQNLSDR LSLAIKSGGF GIWEWDILQD
QLIWDEQMYE LYGLEKSDVL ETIYQTWANA LHPQDRERTE TAIQQALRSE KEYNPEFRVV
HPNGSIRYIK AYALVQRDNN GEPQRMVGVN FDITSAKEAE KQLRQVNERL TLTNAELDRA
TRLKDEFLAN MSHELRTPLN AILGMSEGLQ DGVFGNLSKQ QKQAINSIDR SGNHLLALIN
DVLDLAKVES GKLELQLAQV SINYLCTNSV TFVRQQALKK NIQLTTKIPE GLANIVVDEL
RIRQVLINLL NNAVKFTPDG GCIKLEVKVI FSTPQNLLQF SVIDTGIGLT PENASKLFQP
FIQIDSSLNR QYSGTGLGLA LVRRLVELHQ GTVGVTSELG KGSCFMVCLP YVVSKAPTVE
TTISPPNSIQ YKEFQPSKHS PILTISQRPS SSTTLLLVED NELNIATISS YLSSKGYKIE
IAKNGEEGVT LAKSLSPDLI LMDIQLPKVD GLEAIRQIRA EQRLTSTPII ALTALAMTGD
QEKCLNAGAN DYLSKPVKLK QLVEKIEDLL N
//
