ID B8HRN4_CYAP4 Unreviewed; 1428 AA.
AC B8HRN4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Cyan7425_3580 {ECO:0000313|EMBL:ACL45901.1};
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC Cyanothece.
OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL45901.1};
RN [1] {ECO:0000313|EMBL:ACL45901.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL45901.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L.,
RA Sato H., Zhao L., Sherman L., Pakrasi H., Richardson P.;
RT "Complete sequence of chromosome Cyanothece sp. PCC 7425.";
RL Submitted (JAN-2009) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001344; ACL45901.1; -; Genomic_DNA.
DR STRING; 395961.Cyan7425_3580; -.
DR KEGG; cyn:Cyan7425_3580; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_252623_0_0_3; -.
DR OrthoDB; 442746at2; -.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd02205; CBS_pair_SF; 1.
DR CDD; cd04620; CBS_two-component_sensor_histidine_kinase_repeat1; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 7.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 7.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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; 7.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00116; CBS; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 6.
DR SMART; SM00091; PAS; 7.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 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); 7.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 7.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Kinase {ECO:0000313|EMBL:ACL45901.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ACL45901.1}.
FT DOMAIN 17..71
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 80..139
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 164..217
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 290..348
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 365..417
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 418..492
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 494..545
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 546..623
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 625..676
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 673..743
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 805..875
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 878..930
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 931..1001
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1004..1056
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1069..1291
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1310..1426
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 135..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1361
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1428 AA; 160092 MW; 44E4FCCEC079D88B CRC64;
MSFDLLFSPS LPLAQVIDPA PLCVPPETSV LEVIRLMHQT GKCALVIAET QLCGIFSHQD
VVRAAATGMD LTATPIAEVM TQPVVTLAWS AEMTLQTALS GMAEHQIHHL PVLNQDDRLI
GLLTQDALLQ GLARKPQPIP SLNPSPPAQS AQTYPDRGMD KDVLEQQWKA LFDHALDAIL
IADDQGCYLD ANPAACQLLG LSKAELLSSC VADFADPAVE ITQLWQKFIR QGQMLGEFRL
RCPDGTVRQT EFAAIANFIP GRHLSILRDI SARVELEAER KRTEVNLQAS EAKFRLLTEH
LRDAFFICSP NLERYLYISP AVEKIWGITT TEIYQNPRSW LEQVHPEDWD YFIANTSLDG
HFEDYDLEYR IIRPDGEVRW VHVRAYPLTS TQGQIEQMVG VCEDISDRKK AELELIEREA
FLSSIYDGAD QAVFVIDVTE SHDFYYVAFN RLAEQYAGMS SQEVAGKTPE QAFGPVTGAA
FRQNYERCLQ IGTLSYEEEV VLATHTVWTL TTLSPLRNQQ GAIYRIVGTA VDISDRKQLE
LSLQASERKL SQILDRTLAS ITIFRIFANR DWEYEYFSAG CEKLFGYKCQ ELIADKLLWM
SRVFPPDRET ILMPMFDTLL IEGNTTAEYR FYHRDGSLRW ISSAYAAEQI APDCWRITTL
CQDITDRKQA ELQLRELNNA LTNTVEGISR LDPQGHYTFV NQSYADMMGY TAAEMLGQHW
HITVYPDDRE AALAAYEQMR SWGKAKLKSR GLRKDGAVFH RRIVMVAVYD DQESFSGHYC
FMEDVTDKMQ LKTERAKVEL ALRESEERFR TLSAAAPIGI CQADLDGNCL YTNARWQEMS
GLSFEDSLGQ GWVQAIYPDD RSTLSAAWAA YVRGECDHLP DFRLLTPEGK IRWVSTCVGA
IKSSTGEIIG YVSTDEDITE RKQAEQALQD SQQRFQTILD NSPTAIYLLD PQNNFLLANR
VCAEHVSLTP EDLVGKSIYE FWPREIADVF AANNQTVFET GQLLQLEEVV PHLDGQQRTY
ITVKFPLRDL MGNPYAICGI STDISETKEL ESQFLRAQRL ESIGTLASGI AHDLNNMLTP
ILVSSQLLQR QLPEGRPQEL LKIMEANARR GADLIRQVLT FARGTEGKRM PLQIKHLLTE
IQQICERTFP KSIRIALDIP ADLAMISVDP TQLHQVLMNL CVNARDAMPE GGQLNLRAAD
FYADQTYRQM NLEAQVGAYV VITVEDTGMG MDSDVLERIF DPFFTTKGVG QGTGLGLSVV
QGIIRSHSGF IKVNSSIGQG TQFQVYLPAI MAKEEVASSE PELLLGRGEL ILLVDDEANL
LTITKTLLED CNYRVMTASN GVEAIALYAQ HQNEIGAVLM DMVMPGMDGA KTIGALRKIN
PLVKIVASSG LTARLQGQDL VSMEINATLA KPYTAHELLL LLDGLLRH
//
