ID Q8YUG7_NOSS1 Unreviewed; 1344 AA.
AC Q8YUG7;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=all2379 {ECO:0000313|EMBL:BAB74078.1};
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690 {ECO:0000313|EMBL:BAB74078.1, ECO:0000313|Proteomes:UP000002483};
RN [1] {ECO:0000313|EMBL:BAB74078.1, ECO:0000313|Proteomes:UP000002483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576
RC {ECO:0000313|Proteomes:UP000002483};
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000019; BAB74078.1; -; Genomic_DNA.
DR PIR; AD2103; AD2103.
DR RefSeq; WP_010996535.1; NZ_RSCN01000002.1.
DR STRING; 103690.gene:10494409; -.
DR KEGG; ana:all2379; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2905; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR OrthoDB; 9788063at2; -.
DR Proteomes; UP000002483; Chromosome.
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; cd04620; CBS_two-component_sensor_histidine_kinase_repeat1; 1.
DR CDD; cd17774; CBS_two-component_sensor_histidine_kinase_repeat2; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
DR CDD; cd00156; REC; 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; 2.
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; 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; IPR013656; PAS_4.
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; 5.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00571; CBS; 4.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00116; CBS; 4.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 5.
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; 2.
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); 5.
DR PROSITE; PS51371; CBS; 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002483}.
FT DOMAIN 16..81
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 90..150
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 157..216
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 225..283
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 347..401
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 466..538
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 541..593
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 594..667
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 670..723
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 724..794
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 797..848
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 845..915
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 982..1207
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1226..1340
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 284..361
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 577..604
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1277
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1344 AA; 150678 MW; 3C10218C2A6D4885 CRC64;
MPSLYPVDLP TIEQVMECYP LTVLPDTLLV DVIALMNPVS RCTIDSASDF SSCVLVVEEK
NLVGIFTLRD IVRLTGVGVN ISRKKISEVM TQPVISLTQA AAQNALTALA FMRQHHIRHL
PVVDEQGQLL GLITQDRIRQ VVQPAHLLKL RCVTEVMVTQ IIHALPTTSV LELSQMMSDR
RISCVVIVAP QETKLIPVGM ITEKDILKVH LQGLDIAQTP AQTVMSSPVF SISPSESLWT
VNLLMQARGV RRLVVVGEQG QLQGLVTQTN LLQVLDPLEI VNVIQALEAK VAEQTFQLQQ
TNQQLEAEIK QRHQVEESLR QVQQELELRV AERTAELVQA NARLRRREQQ LQALFDQALD
AILIADDEGC YVDVNAAACE LFGVSREELL ASTIADFAAP EFNFTQAWQQ FREQEQMSGE
FQLHRPNGTV RATEFAAVAN FIPHRHLSII RDVSDRQQAK ANLQNSEQRL QLALSASSTG
MWDWNLQTNE VVWSESMCSL FNIDPQTFNN RFESFVNFIH PEDREFVEQH LMQSIDQNTI
CNIEFRVVWL DGTVHWASGK GNVFYDEVGK PIRMIGVHQD ITERKQAEAK LQKSEQRLKL
ALWAGNTGTW DWNLQTNEVI WSDHLFSLFG LTPDTFDVSY ENFLNLIVHP EDREFLHQSA
LRAIEQQVPH DIEFRFLYPD GTVGWSLCKG QVLYDDITGE PLQMIGVNMD ITERKNAEEA
VRESNQRLQA IIDNCPAVIY VKDMQGRHIL VNSEFERITH LTREQVKNKT NVKVFSPKTA
QSLSVNDQEV LSSRTPVQFE EEIQFEDGLH TYLTVKFPLC DATGEPYAIC GVSTDITERK
QAQEQIRQQA ALINVATDAI FVRDLANRIL FWSRGAENLY GWTAEETVGK LAHELFHKES
SSQLEAAVTT TLEQGSWHGE LEQTTKNAQE IIVASRWTLV HNQFGDSPSI LVVNTNITEK
KQLELQFYRV QRLESIGTLA SGIAHDLNNV FAPIVMIAQL LPSRCKNVDI RTQELFKTLE
TSSKRGSDLV KQILTFARGT EGQRIFLQPG HLLKELAKVI QQTFPKSIEI ITDIPTNTLW
MVQADPTQLE QVFMNLAVNA RDAMPNGGKL TITATNRVID STYARMHLES EVGDYIVVTI
SDTGTGIPPE ILERIFDPFF TTKEVGKGTG LGLSTVLGIV KNHGGFVEVA SQVGQGTEFQ
VFLLRGKGTA TETIAKTELP RGNGELILVV DDETIIQQTA QEALADYNYK ILVANDGIEA
IALYVEYQPE ISAVLLDMLM PNMDGLTAIR TLRTINPNVK IIATSGLPAN EQKAIVAGAD
RFISKPYTTT DLLTTLSDVI GVTE
//