ID B8HW94_CYAP4 Unreviewed; 778 AA.
AC B8HW94;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Cyan7425_2315 {ECO:0000313|EMBL:ACL44673.1};
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC Cyanothece.
OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL44673.1};
RN [1] {ECO:0000313|EMBL:ACL44673.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL44673.1};
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; ACL44673.1; -; Genomic_DNA.
DR AlphaFoldDB; B8HW94; -.
DR STRING; 395961.Cyan7425_2315; -.
DR KEGG; cyn:Cyan7425_2315; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_020162_0_0_3; -.
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; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 1.
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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACL44673.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ACL44673.1}.
FT DOMAIN 397..461
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 551..777
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 503..544
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 778 AA; 86954 MW; 34B6F32AC8598EFF CRC64;
MGIVVVVHIE VRAPMVVDRP LLSCPPLLTG ITEAAHQLLT IPAWETALSK AFETLATHTG
CDRLRLWEIT VSPESNTVQP CHIFPPDTAQ LPVRLDCPSS GCLQDWWEHL QCGVPFQAGR
GEVSALEEEW LIEQGILAVL VLPIQIEQNL THILSLEYTQ CPYCWSEAEI NLLRSFAVHL
GGVMELRRRS AQLLWRSFAI ARQQQQISQQ QCRQISESRL RRQNQVLVEL ARRKNLHRGD
FSAALQEITS VAAETLEVER TSVSIYNPER TRIYCLDLYE RSQDCHSQGL ELQASLYPDY
FRALEQERTI AAHDALNDPR THEFSESYLS PLGIASMLDA PIWLGGQMVG VVCHEHIGEK
RQWTMEEQQF AASIADLVSL AMEARDRYQA QEELRASEER LKSFFNATFE AVFIHDQGRI
LDVNHAAETL FGYTTTELIG MLATDLAMPE CRPLLVERIQ QPSDLPFEAT GLRKDSSTFI
AEVSGKSIIY KGRPARVVGI RDITERKRAE AALEALNANL EQQVEERTAQ LQQKMQELQE
LNQLKDVFLH AVSHDLRTPV MGTLLVLNNL LNPPGQSAEA PANPPATVSL SRGVIERMIA
SQKRQLTLID TLLETHASDV QGMVLHQEPI QLGILAQGIV DDLEPLLSKN QAIVRNLIAP
NLPTVEVDAI QLRRVYENLI TNALKHNPPG LTLTLTATQD SNALICTVQD NGVGISPEQS
KHLFDLYFRG SNSRHLKGIG LGLYLCRQVI QAHKGEIGVI STPGEGATFW FSLPLPPA
//
