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Database: UniProt
Entry: B8HRH4_CYAP4
LinkDB: B8HRH4_CYAP4
Original site: B8HRH4_CYAP4 
ID   B8HRH4_CYAP4            Unreviewed;      1330 AA.
AC   B8HRH4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Cyan7425_1795 {ECO:0000313|EMBL:ACL44162.1};
OS   Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC   Cyanothece.
OX   NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL44162.1};
RN   [1] {ECO:0000313|EMBL:ACL44162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL44162.1};
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};
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DR   EMBL; CP001344; ACL44162.1; -; Genomic_DNA.
DR   STRING; 395961.Cyan7425_1795; -.
DR   KEGG; cyn:Cyan7425_1795; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_252135_0_0_3; -.
DR   OrthoDB; 5555607at2; -.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 6.
DR   CDD; cd17580; REC_2_DhkD-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; 7.
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; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 3.
DR   Pfam; PF08448; PAS_4; 3.
DR   Pfam; PF13188; PAS_8; 1.
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; 5.
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; 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; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 4.
DR   PROSITE; PS50112; PAS; 6.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACL44162.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ACL44162.1}.
FT   DOMAIN          30..85
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          137..209
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          213..265
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          291..361
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          364..416
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          417..491
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          486..545
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          553..622
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          814..885
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          890..943
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          968..1186
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1207..1325
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          790..817
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          934..964
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1256
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1330 AA;  150215 MW;  574BA30CA593E2EA CRC64;
     MTAEGPFTSP VHQSSLAEEA FFFDLSLDLL AVVGLDGYFK RINPMFSQTL GYSATELLTS
     PFLDFVHPDD RAATLAEMEQ LKGGTPTLAF ENRYLTREGD YRWLSWTASP QLDRAVIYCV
     ARDVTQQKQT EIALRVSEER WQLALRGSND GIWDWNVQTN EVFFSARWKT MLGYEEDEIS
     HHLEEWAKRV HPDDLAWVMQ AIQDHFAQKT PFYVAEHRVQ CKDGGYKWIL DRGQAIWDQD
     GKVLRMVGSH TDVTERKTLE AALRTANETL EQRVAQRTAE LEQINRSLQA SELKFRTAIE
     HIPDVFVIYD AHRRIQFVNR AGLALSGGSL PDFLGRRDEE IFPVEVTQTY LPLLQQAVAT
     KRYQTGECTI ALPNREPYTI VVQYVPLLDG NGEIQQIFGI SHDITRRKQA EDATRRSEQQ
     IRRILDSLFS FVGVMTPDGI LIEANRTALE AAALRPADVL GKPFEDTYWW SYSPELQTQL
     RQAITRAAQG EMVRYDAIVR VREDQLITID FTLGPIFDEA GRVKYLIPSG IDITERKQAE
     IALQQSQSQV QRQLAEIETI YQSAPIGLNI LDTDLRFVRI NQRLADMNGF SVEEHLGKTI
     RDLLPDLADT AEALLRPILA TGEPLLNVEI RGETPAQPGV QQIWLESFLP LKQDDRIIGI
     STVCEEITER KQAEEALRRS EERYRTLFET MEDGFCVIEI LFDANQTPID YRFLEINPAF
     EQQTGLHQAV GKTARQLIPN LEDFWFETYG RVALTGEPLR FENGSAVMNR WFEVYAFPVG
     QPEHHKVALL FKEISERKRL EAERQQAEIA LRENEDRLRM AIASAQLGTW DWNIVTGKLK
     WDTGCKAMFG LGPDAEINME TFFAGVHPQD REQLKAMVQS RLNPASGGSF DTEYRTIGLQ
     DKVERWLRSK GQAYYDANGN PLRFSGTVLD ITQQKQAEAH REQLLQQEQA AREAAERANR
     IKDEFLAVLS HELRTPLNPI LGWSKLLQSP QISAQKLQQG LATIERNAKQ QVQLIDDLLD
     TSRIIRGQLS LNLAVINLSE PILAALETVR LSAETKEIKL EVKLGSWLGQ IRGDVGRLQQ
     VVWNLLSNAI KFTPPGGRIT VRLSQVDRWA QIQVRDTGKG IQPQFLPHVF ELFRQEDSST
     TRSFGGLGLG LAIARQVVEA HGGTIMAASQ GEGQGATFTV LLPLIPAAIT NVPADPQPQP
     LNIEQLRVMV VDDEADSLEV VKVVLEQQGA IVQALPSAPK ALQLLTEVPF DLLVSDIGMP
     EMDGYTFIRQ VRTLPSSLNR NIPAIALTAY ASDMDQHQAL STGYQFHLAK PLEPEALVRA
     ITRLGLPRPD
//
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