ID Q8YSJ3_NOSS1 Unreviewed; 1290 AA.
AC Q8YSJ3;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=alr3092 {ECO:0000313|EMBL:BAB74791.1};
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:BAB74791.1, ECO:0000313|Proteomes:UP000002483};
RN [1] {ECO:0000313|EMBL:BAB74791.1, 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};
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DR EMBL; BA000019; BAB74791.1; -; Genomic_DNA.
DR PIR; AE2192; AE2192.
DR RefSeq; WP_010997243.1; NZ_RSCN01000001.1.
DR STRING; 103690.gene:10495128; -.
DR DNASU; 1106690; -.
DR KEGG; ana:alr3092; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR OrthoDB; 5555607at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0016020; C:membrane; 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; cd00130; PAS; 4.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 6.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
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; 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; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 6.
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; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 6.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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:UP000002483};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..191
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 196..248
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 249..285
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 329..381
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 472..524
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 549..597
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 601..653
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 654..725
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 728..777
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 778..848
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 851..904
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 929..1147
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1168..1286
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1217
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1290 AA; 144892 MW; FC0BDC7CBDE8E2B2 CRC64;
MSNIQRSHLQ RYCISIVSVL LALLLGLTLG RYLKVEISPL FFASVVFSSW YGGLAPGLVA
TVLAILVKNY FFITPFNSIA VSQGNDLLNL IVFASVAVLI SSLNLQVLTA REVSEAKLGK
LKVNYRQLLE TAYEGIWIFD SEGKTEYVSP QLAQILGYSV ERIGEFSIFN FLEPQARLEI
EQWLEQQQKY NHQTKQQFDL RLQRRDGASL WVIVSLSSIL DKHRRFSGAV AMLTDITEHK
HEQAEPDLER QRLRAILDIL PMGVVISDAK GQLLEINPGV KAIWGEDAPL LDNTSQYHQY
KGWWPDTGQP LTAAEWTLAR TLATGEAIIG EEIDIATFDG KRKTILNSAV PIYDATGAIV
NAVTVNVDIT ERKRVEAALR QSEALAKARA EELETIMETV PAAVWIAHDP LCHSMSVNRA
AYDMMRVPPG SVMTATPASG GYPFPFKIQK NGQDIPLNEL AMQQAGLTGQ EVEAEVEFFF
SPEDVRHIYG KAIPLCDPDG NVRGVIGAFL DVTERQQLMS LLQQKQEWLD LAQKSGKIGS
FDWKLTSNIN VWSQELEEIY GLQPGEFGGT FADWAKHVHP DDLARVEVEL RELLNTGSKE
FFSDFRIIRQ DGSICWLQSR ARVFYDDHGQ PLRMVGVNVD VTERKQAEAA LQQSEARLKR
LLQSSIIGII EADPERINFA NDAFLKIVGY THEDLLTGKL RWQDMTPPEY SELDQAKVEE
VINSGFCIPF EKEYIRKDGS RVPILLGAAR LSSSPLTWVC FILDLTERKQ AQAALQQSEL
MFRTLADTMP QMFWITQPNG YHEYFNQRWY DYTGTTLEQT QGAGWQNILH PDDVQRTIEQ
WQDSLDTGKD YDIEYRLRRA ADGEYRWHLG RAFPLRDENG RILKWFGSCT DIHDQKLAIE
ERAQAWEQER AARIELERAN RMKDDFLAIV SHELRSPLNP ILGWAKLLKS RKLDALKTNQ
ALEVIERNAK LQARLIDDLL DVSRILRGKL SLNVCTVDLV TTIEAALETV RLTAESKSIH
IQTELTSHVC RVEGDPNRLQ QVVWNLLTNA VKFTPEGGQI EVSLERVGSL AHIQVRDTGK
GISLDFLPYV FERFRQADEV TTRKFGGLGL GLAIVRHLVE LHGGAVQVTS PGEGLGTTFT
VKLPLIAVSQ IYEEHFVADT TPNLQGLRMV VVDDDADTLE LLSFILEQYG VEVKAVNSAN
EALEAIAHTK PDLLLSDIGM PEVDGYMLIK QIRSMEVASG TKLPAIALTA FAGETNFQKI
MSAGFQRHLT KPVEPSELAT AIANLIQSNS
//
