ID D8G3X0_9CYAN Unreviewed; 1231 AA.
AC D8G3X0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OSCI_3400013 {ECO:0000313|EMBL:CBN57310.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN57310.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|EMBL:CBN57310.1, ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|EMBL:CBN57310.1,
RC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CBN57310.1}.
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DR EMBL; CACA01000304; CBN57310.1; -; Genomic_DNA.
DR RefSeq; WP_007356512.1; NZ_CACA01000304.1.
DR AlphaFoldDB; D8G3X0; -.
DR OrthoDB; 569347at2; -.
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 CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 3.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 3.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 3.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 3.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CBN57310.1};
KW Membrane {ECO:0000256|SAM:Phobius};
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, ECO:0000313|EMBL:CBN57310.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 548..712
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 753..993
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1020..1136
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 125..152
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1069
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1231 AA; 139289 MW; 3EA1210CEDD76448 CRC64;
MLTIFEEFFS SGQFIPHGNS YLWQPQLLWL HILSNLSIAI AYFSILAMLI YFVYKRRDVP
FLRIFILVGV FTLLSGTGHL LEILTLWHPL YWLSVVEQAM TGLVFCYTVA QMVTLLPKFF
ALRNSEQLET INQELEHEIA ERQKAEEALK SIVAATASVT GEKFFSALTQ YLAKALDVRY
AFVAEIVSKE SQKLKALAFW NGNNIEDNFE YILSDTPCEL AIEQASLQYF PERVQELFPK
AIDLKKMEAI CYLGVPLLSA KGEVIGILCI NSDRPLVNEE SAKAIMRVFA GRATAELQRQ
RAESAKNRAY EDLENRVQER TAELVETNAI LETEIREKVV AESALRKSDI RLRKQQDGLL
KLAKKQSIYE GNIQGALREI TEVAARTLSV ERASVWFYSE GKSEIYCADL YEVTPNRHSQ
GTKLSATDYP NYFQGLETDR VIVANDAHTH PRTQEFSELY LTPLSIASML DTPINFKGQS
VGVICLEQVG TARNWAIEEQ NFSSYLAYMT SLAMESRDRK RAELALRETA EREKAIAFMM
QRIRQTLEID KIFSAATSEL RQAIDCDRVG VYRFNPDWSG NFVAESVASG WKVLLDSPIN
QPQRTETTIE KENCATKTLS ITGEPIEDTY LQANQGGFYQ QKTYYRSVPN IYQAGFDTCY
IDLLEQFQAR AYIITPIFCS SKLWGLLATY QNSDIREWRE AEIKMVVQIG AQLGVAIQQA
ELLAQTQKQA AELKIAKESA DAANSAKSEF LANMSHELRT PLNAILGFSQ LMNRDRSLST
EYIQYLNIIN RSGEHLLELI NDILEMSKIE AGRMVLYENE FDLYNLLDNL EDMLQLKAQS
KALKLTFQRD KTVPKFVKTD QSKLRQILIN LIGNALKFTE KGNVILRVKV AGRERSNNEQ
KENTNIPSSF FLLPSSFFLQ FEVEDTGPGI APEDFDKLFE AFGQTATGLK SGQGTGLGLP
ISQKFVQLMG GEITVSSQLG QGAKFTFDIQ ASSVDRIESE KAQAINKKIL GLAPNQLAHR
ILIVEDNPAN RLLLVRLVSS LGFEVREAEN GQQGIALWES WEPHLIWMDM RMPVIDGYEA
TKKIRAQSKS RETVIIALTA SVFEEEQQLI LSAGCDDMVR KPFKEQELLA KMSQYLGVNY
LYENDGEDLI TNSESEVCDF SRILQPETLQ LMPKEWIKQL YLAASQGSDS LIYQLLEQIP
AENSAIAKAI GDLVENFRFD KILELAQLTI S
//
