ID B4VSR8_9CYAN Unreviewed; 864 AA.
AC B4VSR8;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MC7420_821 {ECO:0000313|EMBL:EDX74947.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX74947.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX74947.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX74947.1,
RC ECO:0000313|Proteomes:UP000003835};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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; DS989851; EDX74947.1; -; Genomic_DNA.
DR AlphaFoldDB; B4VSR8; -.
DR STRING; 118168.MC7420_821; -.
DR eggNOG; COG3437; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_3; -.
DR Proteomes; UP000003835; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd19920; REC_PA4781-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; IPR013656; PAS_4.
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; 3.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
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; 3.
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:UP000003835}.
FT DOMAIN 12..128
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 161..231
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 234..286
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 361..413
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 414..486
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 489..542
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 583..844
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 121..164
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 544..571
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 61
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 864 AA; 98793 MW; A159B42760266C96 CRC64;
MTLESIPLYK GTILTIDDTP DNLHLLTEML SAQGYKIRII PNGRLALKSI ANNPPDLILL
DIIMPDMDGY QVCQQLKASP KTQNIPVIFL SGLNETFDKV KAFEVGGVDY ITKPFQVQEV
LARVESQLRL QRLQKQLTEQ NIQLQQEIQE RQQVEIALSE SEKKYRHLVE ASQDLIWSIN
QDGTYTFVNP IVHHLYGYSP EEMLGRSFTE FLSPERREAD INLFERLLQG QSVFQYETTH
LTKAGEPIQL LLNAIAVVDD QGQVVGITGT ASDITERQQA QEALRLSEIR YRELVEFQEQ
VLVCRWKPDT TLTFVNQSYC RFFAKSQTEL IGTKYVDLLP DFIEDQISDF VKLLVNHECP
ETSEHIMISH QGKLHWFKWK DQPILDEQGQ VIEVQSFGID ITTRKQAEEK LRLSEENLAQ
AQRIAHIGNW EFDVITNQII WSAELFRIFG LEPNHTEPTY QQLLDFIHPD DCSEFEETVK
QAIEQGLCYE LDFQIVPKNR TTVRHLEVRI EPIFDQHHRV IKLFGTALDI TQRQKAETAL
RQSEARERER AHQLQRTLEE LKRTQSQLVQ TAKMSSLGQM IAGIAHEINN PVSFIVGNLT
IGRQYFNDLL RLINIYQETY PNPSSSIQDI AEAIDLQFIQ EDWHKLLNSI QEGSERIHQI
ILSLKNFSRL DEADLKSVDI HQGIDSTLFI LQHRLKSPGN RQEIQVIKEY GQLPPVTCYA
NQLNQVFMNI LVNALDAIES HSSPGVIRIS TEVADAHQQP PPKNGNQQTD VVIIRITDNG
IGISEEVQPQ IFDPFFTTKP VGSGTGLGLS ISYQIIVEKH QGQLSCLSTP GEGTTFMIEI
PIKPRSQQPR KISLNDMDLA KEIS
//
