ID B8HRN3_CYAP4 Unreviewed; 1432 AA.
AC B8HRN3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Cyan7425_3579 {ECO:0000313|EMBL:ACL45900.1};
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC Cyanothece.
OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL45900.1};
RN [1] {ECO:0000313|EMBL:ACL45900.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL45900.1};
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; ACL45900.1; -; Genomic_DNA.
DR STRING; 395961.Cyan7425_3579; -.
DR KEGG; cyn:Cyan7425_3579; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_000445_114_15_3; -.
DR OrthoDB; 442746at2; -.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 6.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 2.
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; IPR013767; PAS_fold.
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; 6.
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; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 5.
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; 7.
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; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 6.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Kinase {ECO:0000313|EMBL:ACL45900.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ACL45900.1}.
FT DOMAIN 80..140
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 165..241
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 243..295
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 375..426
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 427..499
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 502..554
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 760..812
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 813..887
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 891..943
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 940..1009
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1011..1063
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1076..1297
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1316..1431
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1367
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1432 AA; 160646 MW; 230F992FFEC59163 CRC64;
MSPDLVFPTQ PQLDQIINYS PLVVSPETSA LEVIGSMHPS HSCALIMAGG QLSGIFTSQD
VVKATATCID LAATSIAEVM TQPVVTVTWS EELTIQRALS RMAEQQVHHL PILDAEHQLL
GIITQEQLLQ AIGRPEQWKV GNCLQQQLQW QTQNCDQLER VLQASAINLK DMLNSANAAI
ASVRFFSDHL FEYDYCSAGN AQVFGYSAQE FISNSSLWRS RVHPDDRDQI EAAIANTMAA
EPNTLEYRFY RKDGNLAWVS TTYTSRRDDE LDCWIVTAIS TDITDRKQLE LSLQASERKL
NYILDNVVAS IVTMRVFADR DWEYDYHSAG YERLFGYSDE ELKVDKTLWL SRVFPEDRAT
ILMPLFEAFF SEINVTVEYR FYHKDGSLLW ISSSYASERI APDCWIVTAL SHDITDRKTT
EIALKESEER FRLAVEAARM GTWDWNILTN EVIWSESMEG LMGMAPGSFD RRMETVVEMI
HPDDLVRVQA ALNNSLAHGA DYVIEFRFIK LDGSVRWAMS RGNVLRDGHD RAVRMLGVDV
DVTDRKAAEL ALQESETKFR RLTENVPGMI YRYVVHPDGH DAFTYVSPRC QEIYELDAET
ILQDSRVLWS MVDPEDVPRL EAGIAISAQH LSPFFVEHRI HTPSGMKWIQ AISLPERMEN
GDLVWDGLII EVTEHKRLAR ALQESEERRR LALDLTETGS WEFDVVTGEA IWSDSHYRLM
GLMPGELPSN YQTWRDRVHP EDLVWVEAVC SHALATHALL NVEYRVVYPN GTVRWVLNKG
QGVYDTSSQA VRMLGVMMDI TDRKAAEKAL IESEARYRLL CESLPVGIFR NDLQGNNTYS
NPKTLEMVGL SFEESLGDGW AKYLHPNDRD RMYAAWSNFV EQINRGEAAS YQLELRYLYP
NGSLRWVLAQ AVPEYNGSGQ LTGFVGSAVD ITPQKIAEQT IRSQAALIDI TSDAMSVRSL
DNEILFWNRA AEKIYGWTAN EVLGQHATHL LYRDPAQLEP AFQAVLAEDS WQGELSAVTK
TGQELTIASR WTLMRNGEGQ PEAILIVDTD ITEKKQLESQ FLRAQRLESI GTLASGMAHD
LNNMLTPILA SSQLLQKQFP EGRSQEILKI IEANARRGAD LIRQVLTFAR GTEGKRIPLQ
VKHLLTEIQQ ICERTFPKSI TIVLDVVSTL STILADPTQL HQVLMNLCVN ARDAMSVGGQ
LQLRLEDFFI DENYARLLAL QSGAYIVITV ADTGTGIAPE VLERIFDPFF TTKAVGQGTG
LGLSVAEGII RSHGGIITVE SEVGHGSQFK LYLPAATTSP AQTLPEQNNS LGQGELILVV
DDEANLLTIT QTILEDHNYR VITASNGIAA ISTYVQHQHE IRVVLMDMIM PEMDGATTIA
VLKKINPQNK IIACSGLSSL LLQDDLSVGI NASLAKPYTA DELLTIVAQV LR
//
