ID A0YVE7_LYNSP Unreviewed; 663 AA.
AC A0YVE7;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 93.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=L8106_21534 {ECO:0000313|EMBL:EAW34935.1};
OS Lyngbya sp. (strain PCC 8106) (Lyngbya aestuarii (strain CCY9616)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX NCBI_TaxID=313612 {ECO:0000313|EMBL:EAW34935.1, ECO:0000313|Proteomes:UP000000737};
RN [1] {ECO:0000313|EMBL:EAW34935.1, ECO:0000313|Proteomes:UP000000737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC8106 {ECO:0000313|Proteomes:UP000000737};
RA Stal L., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2006) 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 -!- 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:EAW34935.1}.
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DR EMBL; AAVU01000036; EAW34935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0YVE7; -.
DR eggNOG; COG5002; Bacteria.
DR OMA; LNQDAMV; -.
DR Proteomes; UP000000737; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF26; SENSOR HISTIDINE KINASE RCSC; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAW34935.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 195..247
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 403..648
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 235..266
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 376..403
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 663 AA; 74634 MW; BE0E93323F0499D2 CRC64;
MSWMRLFGIR RVSLATKLTL AMTSLVIVAV VSVTWLSLRR EQQTFRKELE QQARILLDAL
AVTTADSLYT LNADFMEEIM EQLGADQVLS AGRIYERQGR IVADAYSDSV LVHRVKADPF
GQTLVQSDKT IFLWEEDQLL AGKAVKVGRQ RLGAVSVGLS TDPLEAKMAA VRNQGLIVAL
TAATAGTALA LILSRSITEP LKQMTSATQR LAKGDLTQKI TIQTQDELEL LADSFNRMTD
QLRELIESKE KLIQSLEHRA EALRQSEAKN RALLNAIPDL MFRFSREGIF LDFKVPRNED
LLKSLSKYLN KTVYDLFPEH VAKQYMEYVL ESLRTNEIQI FEYEWFIKGK RHHFEARIVV
SGRDEVLAIV RDITDNKLAQ IELQQAKEAA EAANQAKSEF LASMSHELRT PLNAIIGYSD
LLREDAEDYG YTDFVPDLEQ IKSSGLHLLS LIQDILDISK LESGEMNLYL EHFDIATLIN
EVQAIIQPLV NQNQNQFKID CVQPIGSMYA DRTKVKQALL NLLSNAAKFT KEGTVTLKVT
RTLFPLQNGQ THSDPKSINH SHHSEKRLSE DWVTFSVEDT GIGMTPEQVE KIFDPFVQAD
NSTTKQYGGT GLGLSISQRF CEMMMGKITV ESTIKVGSTF SIKLPAVVPE FLTKKEKKKL
ASH
//