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Database: UniProt
Entry: B4W0J6_9CYAN
LinkDB: B4W0J6_9CYAN
Original site: B4W0J6_9CYAN 
ID   B4W0J6_9CYAN            Unreviewed;      1218 AA.
AC   B4W0J6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=MC7420_930 {ECO:0000313|EMBL:EDX72261.1};
OS   Coleofasciculus chthonoplastes PCC 7420.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Coleofasciculus.
OX   NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX72261.1, ECO:0000313|Proteomes:UP000003835};
RN   [1] {ECO:0000313|EMBL:EDX72261.1, ECO:0000313|Proteomes:UP000003835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX72261.1,
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; DS989865; EDX72261.1; -; Genomic_DNA.
DR   RefSeq; WP_006104538.1; NZ_DS989865.1.
DR   AlphaFoldDB; B4W0J6; -.
DR   STRING; 118168.MC7420_930; -.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG2905; Bacteria.
DR   HOGENOM; CLU_268932_0_0_3; -.
DR   OrthoDB; 415806at2; -.
DR   Proteomes; UP000003835; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd04620; CBS_two-component_sensor_histidine_kinase_repeat1; 1.
DR   CDD; cd17774; CBS_two-component_sensor_histidine_kinase_repeat2; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 2.
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; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
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; IPR013655; PAS_fold_3.
DR   InterPro; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF01590; GAF; 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   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00116; CBS; 3.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 2.
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); 3.
DR   PROSITE; PS51371; CBS; 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50046; PHYTOCHROME_2; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003835}.
FT   DOMAIN          110..173
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          177..255
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          264..320
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          409..545
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          618..682
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          733..803
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          807..859
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          860..933
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          934..986
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1004..1218
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          559..611
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          970..1000
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1218 AA;  138200 MW;  BA9C42A88106A375 CRC64;
     MSLLDLSLSS LPLEAVIDPY PLSVAPDTTL SEVIRLIAQE AGCDCTLGLS DTSTKSCHPL
     PDWRLMKQAR TSCVLVMQGM QLLGLLTEQD FVRLAALDIN LDALTAADVM TRKLVILNAS
     DCQDVTIILN LFQQHGIHHL PIFNESGYLL GIVTPQRMRH LLQMTDVMGL HSVAEVMTTQ
     VICAPPTAPV QKLAQLMATH GVGYVVIVRQ REQGTGETVT DLDFSSVLSF RQFPIPMGIV
     TADDIVQFQT LPLDFQQLDA QTVMSSAWFS IRADDFLGTA YQRMQQWHTQ QLIVLGNQGE
     WQGMIDQDSL LRAINLNSKT FSFLNPILPS ISPANAELTP KTDTQSQLIL SQGGFCTNDT
     INSDKKIPKP APTNQVPYEG GEGSTLNTQH SAKEHLLYSI SSRIRQSLHL EDILKTTLQE
     VREWLQVDRV LIYRFHSDWS GTVMVESVGA EWDSLSGVVV HDPCFEKTSV ESYKNGRFQA
     TADIYTAGLT PCHVELLASL QVRANLVISI IKDDELWGLL TAQQCHAPRQ WQTSEIELLQ
     QLAVQVGIGI QQSSLFEQVQ TELIQRKRVE LELQQAKQEL ERRVEERTAQ LQQSNQKLQH
     EIAERQQVEI QLRQKLAAIE ATTEGIAILN AKGEYTYLNP AHVQLFGYDT SEALLGKSWR
     HLYPPEEITR FERDIFTILQ QQGYWRGEAV ALRQNGSKFA EEVSLTLTPE GNFICICRDI
     TQRQQTEAAL RTSEERFRST FEQVTVGITH TGWDDRFLRV NQTFCDIVGY TVDELLTKTF
     VDITHPDDVD GDKYYVNQLL AGEIKTFSME KRYIRKDGSI VWVNLRGSLV RKSTGELDYF
     VGVIEDIRDR KRTEAALQES EQRFRQLAEN IHEVFWITDV AKSQMIYVSP AYQQIWGRSC
     QSIYDNPLSF VETIHPEDRE RVMAAFAKQA RGEYHEDYRI IQPGGEQRWI RDRAFPVYDT
     SGQVYRIVGI AEDITEYKQA EQEIRQALAR EQELNELKSR FISMTSHEFR TPLTTILSST
     ELLKYYSSKF TEEKKQIHFE RIQSNVHHIT QMLNDILLLG KAEAGKLDFN PAQMDVRQFC
     QQLVEEFQQG IGHRHSLCFT HQGQLTPVSL DEKLLRHILG NLLSNALKYS PIDRPVCLEL
     TCRHNELIFR IKDQGIGISE TDQQRLFESF HRGTNVGNIS GTGLGLSIVK KAVDRHGGTI
     NLESKLGVGT TFTVVIRL
//
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