ID B8HYG0_CYAP4 Unreviewed; 2693 AA.
AC B8HYG0;
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_4301 {ECO:0000313|EMBL:ACL46614.1};
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC Cyanothece.
OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL46614.1};
RN [1] {ECO:0000313|EMBL:ACL46614.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL46614.1};
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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; CP001344; ACL46614.1; -; Genomic_DNA.
DR STRING; 395961.Cyan7425_4301; -.
DR KEGG; cyn:Cyan7425_4301; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG3920; Bacteria.
DR HOGENOM; CLU_227367_0_0_3; -.
DR OrthoDB; 432643at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 13.
DR Gene3D; 2.10.70.100; -; 3.
DR Gene3D; 3.30.450.40; -; 2.
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; 15.
DR InterPro; IPR011006; CheY-like_superfamily.
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; 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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 14.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 9.
DR Pfam; PF08448; PAS_4; 4.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 13.
DR SMART; SM00091; PAS; 15.
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; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 15.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 13.
DR PROSITE; PS50112; PAS; 9.
DR PROSITE; PS50046; PHYTOCHROME_2; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACL46614.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..127
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 170..237
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 510..562
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 563..635
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 640..692
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 762..814
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 815..872
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 889..940
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1018..1070
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1071..1141
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1144..1196
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1197..1269
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1272..1324
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1332..1391
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1411..1464
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1540..1592
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1593..1644
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1666..1717
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1718..1782
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1790..1842
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1862..1998
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 2042..2087
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 2090..2142
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 2236..2288
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 2308..2448
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 2489..2688
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 140..167
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 418..445
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 61
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2693 AA; 310289 MW; 3AAA043CEA76B90F CRC64;
MRKPAILCVD PDSSGLERLK IELQGALGDR ALVATAQSGL EALERLKKLQ QTYDLALVIA
DDRLPNLSGD ELLCQVHTLS PHTLTILISG QADLQAVSRA LEGAGLYRLI VKPWHPQDLS
KTVVAAIEHY LRDRQLADQT TILQQRLREL ETQNQTLQAE LQTQTGGAGY RLLFDSNPNP
MWIYDLETLA FLAVNNAAIQ HYGYSRDEFL GMTIADIRPP EDIPALLANI KAVTEGLDQA
GRWRHLKKDG SVIWVEITSH TLTFAGRSAE AILIKDVTET VRLEAERQER EILLHQKEET
LRKLSEQVPG VIYQYRLYPD GHSCFPYASE AIRVIYEVSP AQVQESAAAV FAILHPKDLE
RISDSIYTSA RTLQLWHEQY RVILPDKGLR WLEGHAMPER LPDQSTLWHG YIWDITDRKQ
LEITRQQAEE KLREQQVQLD LVVQAAKIGF YISDLETQTS QVSPAYKAQL GYDADCPEAS
PADWKERLHP DDLERAIAVY QAFLRGEADY SIDFRLRHRD GSYRWIYSNA LLLRCSEGQP
LKVIGTHIDI HDRKQLEIAL QKSEEQFQLA ATAVNGYIYD WDVQHNRVYR TPRFFELLGY
SPDQVAETSD WWIERIHPED LAQISSQWQA ILADANQNAF CTEYRVRHRD QHYLYIYDCE
SIVRDQTGQV TRVVGYAFDI SDRKQLELNL RQYERIVSAT PDWMSLVDRN YIYQIVNQPY
LNWSRKSWDQ MVGHSVSEFH PPQTFEETVK PNLDRCLAGE TINYELWIED PDGNPQFVGV
CYAPYVEADG SISGVVVNSR NLTALKRAEM ALEKSHRQYA TVVNSVRSII WEVDPQTVNF
TFVSPEAERI LGYPLAEWLQ PNFWLDHLHP DDLWAVNFCF TSTQKHQNHD FEYRMIAANG
NIVWLHDIVT VVIENGQVVK LVGSMTDITE RKRLEAERQS AENFLRQYER IVSATPDCVS
LLDRNYTYRI INQSHADWTE KSQEEIVGHS FSELLGEEFF QTVAKPYLDR CLAGEGEQRI
EAWMDRPDGE RRFLQATYTP YIEPDGTISG VVINVHDLTE LKRSEQALAA SEERFRTLSA
AAPIGICLTD PDGICLYTNT RWQEMSGLSF EESLGKGWQQ VIHPEDRHTV STAWEAYVRG
EGDRLSDFRL LTPMGEVRWV SVCVAAIKSP TGEILGYVST EEDITARKQN EIALAESEER
FRLAVDAAQM GTWDWNILTN EVIWSESMER LMGMAPGTFD RRMQTVIEMI HPEDLSRVQA
ALQNSIDQDA VYEIEFRFIK PDGSVRWAIG QGNVLRNQQG QAIRMLGVDV DITDRKRLEL
ERQASAAALR ESQEFVQRIV DSSPNLIYIY DLLHQRNVYV NREIYDYLGY TTEESLVLFS
QGFSDVVHPD DLPHIYTHFV HLSTLPERVT AEIEYRMRHK NGEWRWFSSR DTVFKRDEQG
NVTQIVGSAL DITKRKLAEL ALRESEANLQ EAQRIAHLGN WKFDLLSNRL SWSAEVFRIF
GLAGPTEPTP EEKIQFYHPD DRPILSQYLQ HTIATGEPFE FDGLRLIRPD GQLRYLQARG
EAQRNEQGEV TLLFGTIQDI TDRKVIESAL IESHQRLAMI LDNSPLPIFI KDLEGRYIAC
NPAYEQLTHL SREQWLGSSD YDFLPRDFAV ICQLSDRLAV TSNQPITFEE ALPFADGTHT
LVITKFPLTD SQGESYAVCG ILLDITERKR MEIALRESEQ QYRRIVETAA EGIWMLDSDR
HTSFVNPRMA DILGYSIAEM LGQPLSVFLD EEDQAIATNL LEHRHQGISE QHDFKFRRKN
GSTLWALVST NPILDQESNY IGSLAMVTDI SDRKAAELTL QRRAEQEALI RVMTDRIRQS
LDLDVILNTT VSEVRQWLQN DRVIIYRFHP DWSGTVITEA VSDPQFAMLG QFINDNCFGQ
NHAVAYQAGK ISLFRDLEQA QIQPCHRDLL RSFGVRANLV VPILNQNQLW GLLIAQHCRG
PRSWSTEEVE LLQQLASQAG IAIARAELVE NLRESEEQRR LALEFGQIGS WDWNLLTQSL
DWNAWHFTIL GYSPDQVEPS YQAWFDRVHP DDCQRIEQAV HHALTTQTDY EQEYRILLPS
GQIKWVLGKG RAIYNPEGQP ERMLGILLDI SERKSAEIVL QRVNQELEER VQRRTLALRQ
SEEMFRQMAE NITEILYVDS ADRQQTLYIS PAYETVWRRN REALYQHPQS WLESIHPEDH
ERVTASYYRK TDEYDFAEEY RILRPDGTIR WIFDRSSPIW SETRQILCHV GIAEDITDRK
QAELLLKQQA EQERLLRLIT EQIHQSLELD QILATTVQET RTILQTDRVA IYRFSPDWSG
AFISEAVGEE WVKLVAENVQ TVWEDTYLQE NQGGRFSHHE TYIVEDIYAL ELTTCHRDIL
EQFQVRAFVI VPIVVREQLW GLLAVYHNRG TRCWQTDEVE LLQKIAIQLA ISIQQSTLYT
QLQTELSERR QTEVKLQTSL REKELLLKEI HHRVKNNLEM VASLLMLQAG NTEDPYILKL
LKDSEERIAA IALVHEYLYQ SPNLGRIALN EYIRNLVEQI FSSYATSQLE LKLALIPFTI
NIETALPCGL ILNELVTNAL KYAFPNEQSG WLEIALQQDQ QIITLTITDN GVGFPPQLNW
QQSPSLGLQL VRDLVRQLQG TIDISSLCTK PDHEPAGTVV KISFRELNYR QRL
//
