ID D8G0I5_9CYAN Unreviewed; 1132 AA.
AC D8G0I5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OSCI_2780033 {ECO:0000313|EMBL:CBN56125.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN56125.1, 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};
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; CACA01000243; CBN56125.1; -; Genomic_DNA.
DR AlphaFoldDB; D8G0I5; -.
DR OrthoDB; 9758522at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; 4.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
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; 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 NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 3.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 5.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532}.
FT DOMAIN 71..221
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 252..307
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 325..377
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 378..448
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 451..503
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 504..576
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 579..632
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 672..746
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 748..800
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 935..1129
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 7..41
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 648..675
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1132 AA; 129657 MW; B667A2AE1827E368 CRC64;
MGDVMDRVEM YRTIETLQQR VKFLEAEITQ LLDSRKRELE QQVLERTVWQ QQVKRERLLA
STAWGIRQSL NLEEILSGVV KEVRNLLQCD RVVVYQFGSR MDGTIVAESV APGWSKTLGN
YIPDTYLQEN QALKYRWGHK QAIADISQAG FKDCHRELLE RLQIRAQLSV PISIERHFPL
ASQETQNSTP LLWGLLFANQ CSAPRLWRES ELELLDELGV QIAIAIQQNC LFGELHAELT
KRQQLEIALT ESEERFRSIA NSLPVLLWMS DPTGERNFFN QTWLNFTGRT LEQEINHSWM
RGLHPEDCQK SVETYLCAFH QRQSFQIEYR FRRADGKYRW LLDKGAPRFS SDGSFADYIG
SCIDITDRKW AEDGLYQSER LYATLTEVSP VGFFRTDVEG KNLYSNERSC EITGLEPGES
VGYGWTKNLH PDDRDRVLAE WHQAIQTEEI FSSEYRFLRP DDTVKWVFGQ AVAEREDNGT
VVSYIGTITD ISDRKQAEAK LQTAYQQLTF HVENSPLAVI EWDKHFRVKR WSKQAEKIFG
WQEEEVLGLH PNEWSIVFVD EIESVNEVLS RLLTGMESRN TSYNRNYTKE GAVIYCEWYN
SVLFDSAENL ISIQSLVQDV SDRKGAETAL QHLAGELEIR VQERTQELAT TVKLLQQEIA
EREQAQKELL VVKERLQYLL SASPTVIYSC KAEGNYATTF ISDNIAVLLG YKPTDFIEES
SFWINGIHPE DVPRIFNEMM SNFGGSKHIL EYRFLDAFGN YVWLQNDLTL VRDSAGNPLE
IVGSMIDITA KKLAESALLA AKEQLQAVID AVPGFVSWIG ADLRFLGVNR QLALMFNLSP
DTFVGKEVGS IDCNFNCTDF ISDFFTASDT STSQEITLAL ASDRLLPQSR TYLVVAQKYN
QEQAAIFVGI DITERKQGEE QIKASLKEKE VLLKEIHHRV KNNLQIISSL LKLQSKYIKD
PESMVLFLDS YNRIRSMALI HENLYRTTDL ARIDTAEYIR KLVSNLSSSY GCSSRLIEVK
LEIESICLDI DTAIPCGLII NELVSNAFKY AFPQGQKGKI LVSFKLENNT NFVLRVSDSG
VGFPENFDWE QTESLGLQLV VNLTEQLGGN IELDRSRGTD FQVYFAKNTR TK
//
