ID A0A261KJR1_9CYAN Unreviewed; 806 AA.
AC A0A261KJR1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AFK68_28565 {ECO:0000313|EMBL:OZH51797.1};
OS Hydrocoleum sp. CS-953.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Hydrocoleum.
OX NCBI_TaxID=1671698 {ECO:0000313|EMBL:OZH51797.1, ECO:0000313|Proteomes:UP000215798};
RN [1] {ECO:0000313|EMBL:OZH51797.1, ECO:0000313|Proteomes:UP000215798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-953 {ECO:0000313|EMBL:OZH51797.1,
RC ECO:0000313|Proteomes:UP000215798};
RA Willis A., Parks M., Jameson I., Burford M.A.;
RT "Comparative genomics of marine benthic cyanobacteria including Hydrocoleum
RT sp. CS-953 from Moreton Bay, Australia.";
RL Submitted (JUL-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZH51797.1}.
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DR EMBL; LGSU01001442; OZH51797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261KJR1; -.
DR OrthoDB; 569347at2; -.
DR Proteomes; UP000215798; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd12912; PDC2_MCP_like; 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; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000215798};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 275..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..564
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 589..705
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 638
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 806 AA; 90765 MW; 72D46A06A43F9516 CRC64;
MRLLVGSTTL LVSVSAFYSY KVVRNLILDN LKENALLEVQ LGVDEIDQWL ASRKVETRTT
ANTPTFRTMN WLIVEPFLKS KQLESEDFLF FAMINPDGSY YTSKVGKAKA NIKDRKHIKL
AIAGKVNLSD PVNSRTLNTL MVFVVAPVWS DSPNIKDPIG IMAGAIPVDR MREVVNGLEY
GPNSYAFALN SQGKTIFTPQ QDISTNTKNQ ISNFLSSENL NQQNIAIKMV AKERGMELVE
IDRQKFYIAY IPIKEADWSL GLIIPRANIE SQLRALNLMA LVVIGLTVTM IIVLLKVQSF
EQKQLKKTKE AAEIANQAKS EFLANMSHEL RTPLNGILGY TQILHRSHYW GEKERSGIEI
IHQCGNHLLT LINDILDISK IEARKLDLQP YDFHFPSFLQ GVVEIIRIKA DQKGIQLIYQ
SDPNLPQGII ADEKRLRQVL INLLGNAVKF TDTGKVVFQV NMDNSSHSTK LSDSNQQTIS
TTDSHLSTTI KFQIQDTGVG IPENKIDNIF NPFEQVGDQV KQSQGTGLGL AISSKIVKLM
GSKIKVESQL DVGSTFSFAV KFPLSRNWVQ SVSHVEGQKI IGYEGGEKTI LVIDDRWENR
SVLINLLQPI GFITAEAENG AEGLAKIGKL QPDLIITDLY MPLMDGFKMV RQLRESDELK
HLKVIISSAS VSNIDRQYSL DAGGDDFLPK PVNAEQLFKM IEQHLEIEWK YLQTENLENM
QIISQSSVSD ADNDNSKIVF PPPEELEILL DLARRGSLKK LTETAEKIQQ LEPKYIPFTK
PILQWADDFQ ADKIEDFIID FLDKKE
//
