ID B4VJ32_9CYAN Unreviewed; 863 AA.
AC B4VJ32;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MC7420_7756 {ECO:0000313|EMBL:EDX78018.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX78018.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX78018.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX78018.1,
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};
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; DS989842; EDX78018.1; -; Genomic_DNA.
DR AlphaFoldDB; B4VJ32; -.
DR STRING; 118168.MC7420_7756; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_2_3; -.
DR OrthoDB; 453200at2; -.
DR Proteomes; UP000003835; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; 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; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003835};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 166..302
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 439..493
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 494..568
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 573..626
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 643..859
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 316..375
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 863 AA; 98010 MW; 977A1E47B8EBC5A8 CRC64;
MPKSIGIKVI IGGYCLALLI FIGASVISSS HLTQLMETSR WMDYSDKLQD SLQDLLSQLN
NASAIAQHQP WLLKQIPAQA QLLLQEQLGA VVTQIQRTQL SLILGDSLSI AILMVLGGLL
LKQHSRFKAE LELIRDRPLS ETTLEQMAQR EQLILSSAQR IRQTLDLDTI LETTVTEVRE
FLGVDRVLVY RIWSDGTGST VAESVTPDTA PILGQTFPAE VFPEQMHQLY CQGRIRTVVN
PETDGVTPCL VEFLQQLGVK SKLVVPILQQ EKLWGLLIAH HCSQPRQWQS LEIDLLYQLA
IQVTIAIHQS QLYQQLQTEL IERQSIENQL RQARDQLEIR VQERTAELMQ TNADLQTQIH
ERREAEAALR ISEERFRVAL HNSPITVFNQ DTNLRYTWVY NPASRINTDA LIGKSELEMF
APENAQKLMP IKHRVLTTGV GERQEISIIV DGKVRYYDLT VEPLRNHAEE VVGITCAATN
ITEIRIREQE LRESERFIQR IADAMPTALY LYDLIEKRHI YSNQQITQLI GYSPEEIQAM
APTFPQNLIH PDDQSKCTTA IKRFTTAKEG EIIETEYRIQ HKSGEWRWLY SREMVFTRTA
NGLPQQILGT AQDITEHKQA ELIRLALAQE QELRQLQLNF FSMASHEFRT PLSTILASVQ
LLKYYYPEGS DHKIRRNIDR IETTAKTMTQ LLNDILTINR AETGKLEFTP RPFELEKFCC
HLVEEMQVNA GSNYLINFIS QNQYIIVCLD EKLLRSILMN LLSNAIKYSP LGSQIDLILT
CSQSTATFQI KDSGIGIPIE DQKKLFGIFH RGTNIGNIPG TGLGLAVVRK CLDIQGGMIS
VNSEVGVGTT MTIMIPLHDQ SAV
//
