ID K9WTP0_9NOST Unreviewed; 1168 AA.
AC K9WTP0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cylst_1471 {ECO:0000313|EMBL:AFZ23755.1};
OS Cylindrospermum stagnale PCC 7417.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Cylindrospermum.
OX NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ23755.1, ECO:0000313|Proteomes:UP000010475};
RN [1] {ECO:0000313|EMBL:AFZ23755.1, ECO:0000313|Proteomes:UP000010475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ23755.1,
RC ECO:0000313|Proteomes:UP000010475};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Cylindrospermum stagnale PCC 7417.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003642; AFZ23755.1; -; Genomic_DNA.
DR AlphaFoldDB; K9WTP0; -.
DR STRING; 56107.Cylst_1471; -.
DR KEGG; csg:Cylst_1471; -.
DR PATRIC; fig|56107.3.peg.1661; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG2461; Bacteria.
DR HOGENOM; CLU_257991_0_0_3; -.
DR OrthoDB; 9768069at2; -.
DR Proteomes; UP000010475; 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; 5.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 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; 5.
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; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 3.
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; 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; 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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000010475};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 138..197
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 222..271
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 287..334
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 340..390
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 391..463
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 466..518
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 519..589
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 591..643
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 644..717
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 719..771
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 796..1015
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1047..1165
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 114..141
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1096
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1168 AA; 130491 MW; 9AAF6DCFD659C8D0 CRC64;
MGTVPSASCT KGEATLKGIR SRLKFYAVAV LAVCIALLLT LLLQPLLNPT IFILFFAAVA
VSAWYGGMEA GLLATALSTL AVSYFFLKPV FPLSVHALDS MIRLGLFVLV TILISSLNSQ
LRTAKKRLEL SMQQLQASEA RFRRLTESNI IGVITADING GIVEANDAFL KMVGYTREDL
LAGRVRWRDI VSPEDLEMCA LRSASLKENR SVTELDSRGV CQPFEKEYIR KDGSRIPLLT
GSALLENNPE QVIGFVLDLS IRQQAQNALR ESQSRFSALA DATIEGVIIH ENGKVLDANR
AFAKMFGYEI DEVIGMSAAD FLTPEGQKIF RENICNGDEK LYEMTGVKKD GTTFFLEIVG
KSCIYQGRTV RVSASRDITE RKQAEQALQD SQKRFSRLVE SNIFGVAVSD FEGGIEYAND
YFLNMVGYSR EEMLAGEVRW DVMTPPEYID LDQKAIAELL KHGVANPFEK EYIRKDGSRV
PILIGIVLLQ EPYNRQQEQI AFCLDLSQRK RAEKTLHQRE EELSLITNAV PVLISYIDTQ
HCYRFNNKGY EELFGIPASE TYGKHIREVL GESGYQFVRP YIEAVMSGEQ VSFENQVIDK
HGRYRDVSTT YIPQFSQHGQ VEGFVALVRD ITEQKQAEAA LKQSEERFRK LTEKVHVIPW
EANPTTGQFT YVGPQTVEIL GYPSTDWYTD NFWVEHIHPE DREWTTKYCV ERSLSLNNYE
FEYRMLAADG RIVWLYEIVN VVRGEEDQPQ LLHGFMIDIS DRKQAEQERE QLLAREQMAR
TEAEALNCIK DEFLGTLSHE LRTPLNAMLG WTQLLKSRKF DETTTAKALE TIDRNSRSLA
QLIDDVLDVS RIIRGELRLN LHRVELIPVV ESAIDTIRPA ADAKEIWIEC RFDSALGAVI
GDANRLQQVM WNLLTNAVKF TPKGGRVEVQ LERMDSGVVQ IRVSDNGGGI TAEFLPHVFE
RFRQADSSTT RSHGGLGLGL AIVRHLVELH GGTVSVESPG IGKGTTFVVK LPMKAAPIEE
SSTPKQIAPT ASAEVTKNSL PILEGVRVLV VDDEADTRHL LKTILGQYGA QVMAVASTFD
ALKALQQFHP NILVSDIGMP EEDGYALIRQ LRALGQEQGG RIPAVALTAY ATAEDRTQAL
LAGFQLHIPK PVNPAELAAV VANLAGRT
//
