ID D8G2Y5_9CYAN Unreviewed; 1815 AA.
AC D8G2Y5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OSCI_3250002 {ECO:0000313|EMBL:CBN56975.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN56975.1, 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 + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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; CACA01000290; CBN56975.1; -; Genomic_DNA.
DR RefSeq; WP_007356179.1; NZ_CACA01000290.1.
DR OrthoDB; 573511at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:CBN56975.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000313|EMBL:CBN56975.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1140..1160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1172..1197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..278
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1560..1815
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1815 AA; 202273 MW; 24F7D14DFF6F124E CRC64;
MNPHPNLSGY QITEELYIGT RTLVYRGIRT NDQQPVVIKL LRNEYPNFNE IILFRNQYTI
TKNLDFSHII KPLTLEVYQN SYALVMEDFG GISLSTYRLM AKDASQINKI LPIAEFLQIA
IQLTVILHYL YQNRIIHKDI KPANILINPD TKEVKLIDFS ISSLLPRETQ EIQNPNVLEG
TLAYISPEQT GRMNRGIDYR SDFYSLGVTF YELLTGELPF VSADAMELVH CHLAKQAITI
HDINPQLPLL LSEIVSKLMA KNAEDRYQTA LGIKHDLEIC LEQLQTTGKI ETFKLGQRDI
SDRFIIPDKL YGREAEVKTL LQAFERVANP PIGGDRGVEI MLVAGFSGIG KTAIINEVHK
PIVRQRGYFI KGKFDQFQRN IPLSAFVQAF RDLIGQLLTE SDAQIQQWKT QILSALGDNG
QVIIEVIPEL EIIIGQQPPT PELSGSAAQN RFNLLFQKFT QVFTSAEHPL VIFLDDLQWA
DSASLNLMQL LIADIGHLLL IGAYRDNEVN PGHPLMLTLS EMQKKQATIN TITLAPLNQV
TVNQLIADTL KCPESSALPL SQLVFQKTKG NPFFATQFLK ALYQDGLIQF TPPTSSDRGE
AKGGWQCDIA QVNQLAVTDD VVAFMALQLG KLPTSTQKIL QLAGCIGNHF DLATLAIVSE
QSEVETAGDL WKALQEGLIL PLSDVYKFYQ EEENERLVVE NENTTKKIAK YRFLHDRVQQ
AAYSLIPSHQ KTATHLKIGQ LLQQNLSELE REKKLFDIVG HLNLGIELIT QPSECQALAQ
LNLQAGVKAR NSTAYAAARV YLQTGIKLLE TNCWQHQYEL TLNLYVMAGE IAYLNGDFEG
MEQIAELVLQ EALTIFDKIK IYEVQIAAQV LQSNVLEAIA VGRKALGELG VELPTEADAA
KTSKMLQILT TQLEGRQVED LIDLPLMTDP TTQAALEVLG ILFSPIIQGI PALLPWLSSM
MVSLSLRSGN TAASITGYGI HGMVLCAFLE DTSAGYAFGK LALSLLEKFH TQKIKPIVLS
LFGCFIQHSQ ERLDATAPTL KAAYRAGIET GDFLQAGFSL SGQSSNRFFS GEELHSLIQD
LADYDVALAQ VKQYSAQVYL NLGKQAAENL IELVSQPHCL IGNTYNETLM LPKHQQDHDL
IAIAQAYIYK LLLAYYFGNY PDARNYISQA KLCLMAVSAS IFVPIFHFYA ALTYLALFPT
QPESEQAELL DAATTHQKIL HQWAQNAPMN HLHKWYLVEA ERYRVLGEKF AASECYDRAI
NLAKEHQFVQ EEALANELAA KFYFDWGKQR IAGEYMTNAY YGYTRWGAKA KVTNLETYYP
QLLAPILQQI RSPLSTHETL FTLGSVTYTN GVTSSNSSVS VALDLAAILK ASQTISGEIE
LSKLLSSLLS IVIENAGADK CVLMLLRDDR LLIKGSITVG TQPVVLQSLP VDDSQDIPLK
LIYKVKHSRQ TVVLFDATID PTLANDPYII RQQPQSILCS PILNQGQLIG VLYLENNVTV
GAFTSDRIEV LNLICAQAAI SLENARLYEA AQQALVDLKH AQLTIVQSEK MSALGNLVAG
VAHEINNPVG FIAGNIQPAL DYINYLLGLI NLFQQEYPNY SAVIQKEIEA IDLEYIREDL
PKLIGSMQEG VKRIQDISTS LRTFSRADTN HPVACNIHDG IDSTIMILKH RLKANENRPE
IKVIKEYGNL PQIECYAGQL NQVFMNLLTN AIDAVEDSNQ GRKYTEINNK IIVKTEFLDD
KKQAIIRIKD NGIGMSAEVQ SKIFNHLFTT KAVGKGTGLG LAIARQIVEE KHQGSITVNS
LPSESTVFEI TIPVK
//
