ID D8FVA6_9CYAN Unreviewed; 1945 AA.
AC D8FVA6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OSCI_780024 {ECO:0000313|EMBL:CBN54296.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN54296.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
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; CACA01000075; CBN54296.1; -; Genomic_DNA.
DR RefSeq; WP_007353523.1; NZ_CACA01000075.1.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 9.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 6.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 7.
DR Pfam; PF18947; HAMP_2; 3.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 10.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 4.
DR PROSITE; PS50885; HAMP; 10.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 102..159
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 199..251
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 291..343
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 383..435
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 475..527
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 567..619
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 659..711
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 751..803
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 843..895
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 935..987
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1260..1493
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1558..1671
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1680..1796
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1826..1943
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1153..1250
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1607
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1729
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1876
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1945 AA; 211843 MW; F8B2FCDC631C046B CRC64;
MSTAQITKVN SDNLYAKQLL RTLVAVKKGD FSVRMPIDQT GLAGKIADTL NDVIELNERM
AAELDRIGTV VGKEGKIAQR ATIGNAEGSW SASVNSVNTL ITDLVQPTSE TARVIRAVAK
GDLSQTIALE IEDRPLKGEF LQTAQIVNTM VDQLSSFASE VTRVAREVGT EGKLGVQAEV
RGVAGTWKDL TDSVNSMAGN LTAQVRNIAE VTTAVANGDL SKKITVDVKG EILELKNTIN
IMVDQLSSFA SEVTRVAREV GTEGKLGVQA EVRGVAGTWK DLTDSVNSMA GNLTAQVRNI
ADVTTAVANG DLSKKITVDV KGEILELKNT INIMVDQLNS FASEVTRVAR EVGSEGKLGG
QAEVKGVAGT WKDLTDSVNF MAGSLTAQVR NIAEVTTAVA KGDLSKKITV DVKGEILELK
NTVNTMVDQL NSFASEVTRV AREVGTEGKL GVQAEVQGVA GTWKDLTDSV NSMAGNLTAQ
VRNIADVTTA VANGDLSKKI TVQVKGEILE LKNTINVMVD QLNSFASEVT RVAREVGSEG
KLGGQADVRG VAGTWKDLTD SVNFMAGSLT AQVRNIAAVT TAVANGDLSK KITVDVKGEI
LELKNTVNTM VDQLNSFASE VTRVAREVGT EGKLGVQAEV RGVAGTWKDL TDSVNSMAGN
LTAQVRNIAE VTTAVANGDL SKKITVDVKG EILELKNTIN IMVDQLSSFA SEVTRVAREV
GTEGKLGVQA YVRGVGGTWK DLTDNVNLMA GNLTAQVRNI AEVTKAVANG DLSKKITVDV
KGEILELKDT INVMVDQLNS FASEVTRVAR EVGTEGKLGG QAEVKGVAGT WKDLTDNVNS
MAGNLTAQVR GIAKVVTAVA NGDLKRKLML EAKGEIATLA DTINEMIDTL ATFADQVTTV
AREVGIEGKL GGQAKVPGAA GTWRDLTDNV NELAANLTTQ VRAIAEVAIA VTKGDLTRSI
SVAAEGEVAI VKDNINQMIA NLRETTQKNT EQDWLKTNLA KFTRMLQGQR DLETVSKLIL
SELTPLVSAQ HGVFFMMDSV EHDPFLKLLS TYAYRERKNL GNKFNLGEGL VGQCALEKER
ILLTEVPDNY VKISSGLGES TPLNVVVLPV LFEGQVTAVI ELASFRRFSE IHLTFLDQLT
ESIAIVLNTI AASMRTEELL KQSQSLAEEL QAQQKELTET NKRLEQQAQS LRASEELLKS
QQEELQQTNE ELEEKAELLA LQNQEVERKN REIEQARRSL EEKAEQLALT SKYKSEFLAN
MSHELRTPLN SLLILARLLS ENTDGNLTLK QVDYTRTIYS AGTDLLGLIN DILDLAKIES
GTMSVEIEQV LFTDLRDHLD RTFRQVAQDK KLSFLIELSG AVPKGLYTDA KRLQQVLKNL
LSNAFKFTER GEVKLSVEVA REGWSLEIET LTNSATVLAF SVSDTGIGIS PEKHRVIFEA
FQQADGSTSR KYGGTGLGLS ISREIANLLG GEIQLTSRPG EGSTFTLYMP QTYQESRMMN
NRTLGTNDRQ TAQLPSANYS VLPVISSAAT SPNFQLPAPY PSPSISDDRE NIEDGDRVLL
IIEDDVNFAR ILLDMAREHG FKGLVALRSD IGLVMAREFK PTAIMLDLNL PVMDGWTVLD
RLKHDPNTRH IPVHIVSVEE GRQRGLQLGA IAYLQKPVSS EALSKALTDI KGFVERQVKS
LLVVEDDETQ RFSIIDLIGN HDVYTTAVGT GAEALTILNS GHFDCIVMDL GLPDMSGFEL
IELIKQDANL KSLPIIIYTG KELSRAEEIQ LKRMAETIII KDVRSPERLL DETALFLHRV
QANLPEPKRQ MLEQLYQTDS TLIGKKVLIV DDDVRNIFAL TSMLERHQMQ VMYAENGRDG
ITVLQNSPEI DIVLMDVMMP EMDGYETMQA IRNIPQFSSL PMIALTAKAM KGDREKCIDA
GASDYITKPV DTEQLISLLR VWLYR
//
