ID K9WWC4_9NOST Unreviewed; 1869 AA.
AC K9WWC4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cylst_1842 {ECO:0000313|EMBL:AFZ24099.1};
OS Cylindrospermum stagnale PCC 7417.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Cylindrospermum.
OX NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ24099.1, ECO:0000313|Proteomes:UP000010475};
RN [1] {ECO:0000313|EMBL:AFZ24099.1, ECO:0000313|Proteomes:UP000010475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ24099.1,
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; AFZ24099.1; -; Genomic_DNA.
DR RefSeq; WP_015207355.1; NC_019757.1.
DR STRING; 56107.Cylst_1842; -.
DR KEGG; csg:Cylst_1842; -.
DR PATRIC; fig|56107.3.peg.2046; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2204; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_002201_1_0_3; -.
DR OrthoDB; 442759at2; -.
DR Proteomes; UP000010475; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd00156; REC; 3.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 5.
DR Gene3D; 6.10.250.690; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
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; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 4.
DR Pfam; PF00486; Trans_reg_C; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
DR SMART; SM00448; REC; 5.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 5.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 5.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU01091};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022519};
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 Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..116
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 124..223
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000259|PROSITE:PS51755"
FT DOMAIN 252..359
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 368..484
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 493..609
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 702..754
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 937..1009
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1012..1064
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1072..1142
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1236..1288
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1314..1364
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1368..1585
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1609..1723
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1731..1847
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DNA_BIND 124..223
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01091"
FT REGION 226..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 299
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 417
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 542
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1658
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1780
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1869 AA; 208584 MW; C0BCC0458EECE822 CRC64;
MKILVVEDDE LNAYALTAVL TDQNYAVEVA SDGDVAWDLI ETYNYDLILL DVMLPKLDGI
SLCRQIRASG RQVPILLLTG CGSSHEKATG LDAGADDYVV KPFEQEELVA RVRALLRRGG
VTSQPVLEWS SLRLDPSSCE VTYADDLLSL TPKEYALLEL FLRNNRRVFS CGMILEHLWS
YEDTPGEEAV RTHIKGLRQK LKAVGAPGDL VETVYGIGYR LKSQEEEGAK ISPGKSSGTK
QPESDLPKQQ QTLAAIGGIW QRFRGRVDEQ VKVLEQAAVA VGQKCLNLEL RSQATQEAHT
LAGSLGTFGL AWANDLARRI ELLLKSGKTL SASEISNLQT WVKLLRQEIE VNAEKAVFLP
PTVEENPLVL VVEGDTTLGE QLATESANWG LKVKIATSLD AARTQLYQKP PSVVLLDPSV
AAHQEDSGNF LGELCQCQPP IPVLVFTDQT DFTNRLQVAR NGRHTFLQKP MPTAQVLEAV
TQVLQNAPHA EAKILVVDDD PKILALLQTL LSPWGLKVIA LNDPRQFWET LEAVTPDMLI
LDVEMPYTNG IELCQVVRND PRWSELPILF LTVHSDAEIV NQVFSIGADD FVSKPIIGPE
LVTRIINRLE RIRLRRRITQ TPKTPVAEQE NHWRAIFDAE PECVKMVAAD GTLLAMNPAG
LAMIEANSST TVIGKSVYSL IAPEYQEAFR KLNESVCQGN HESMQFEIIS FQGNRRWLET
HAVPLRNKAD GKIVQLAITR DITQNKRAET EIGRMNRTIQ TLSACNQALV RAQDESELLQ
QICQIIVEVG GYRLAWVGLA EHDAEKHIRP AAQAGYEDGS LQSLNLSWGD TIHGQCPAGL
AIRTGKTSII QNIFTDPNYQ IWECQASNSG YTSSIALPLT ADNQAFGALN IYAAIADAFD
ADEVKLLKEL ADDLAYGIVA LRNQRDRQLA QMALRESEER LSLALEAVNL GSWDWNITTN
QIIWSDSNAR LYGLAPGTFN GTYEAFCACV LPEDREALQQ SITLACQQKI DYSHEFRVVW
PDGSIHWIER KGRFYYNAAG EPIRMLGTSK DISERQAALH ERKQVESALQ QSESSYQQLV
ELCPEAIFIQ NEEKFVFLNS AAINLFGATQ AEELLGKQIL DFVHPSSQAV VQERITYLRE
IKQPVPLLEQ KWMRLDNTVM DLEVVAAPFV YQGKPAAQVV ARDITQRKQM EADIYNAKNE
LELRVAERTG ELIKVNQQLQ SELDERQRTQ EALRISQTRF EGILSIADDA IISIDGNQCI
TLFNQGAEKI FGYSAQEVIG QRLDLLLPLR FSQVHRQHVV DFGKSPSLAR RMGERRELFG
RRRDGTEFPA EASISKLDVG QEAVYTVILR DITERKQIER MKDEFVSVVS HELRTPLTSI
HGSLGMLASG LLPTDSEQGK RLLQIATDST ERLVRLINDI LDIERIESGE VKMERESCNV
LDLIGSVVNI LQPLADKAKV TLAMNSLSIQ LWADPDRIVQ TLTNLLSNAI KFSASGSTVW
LTAQRQEDEI LLMVKDTGRG IPAEKLDSIF ERFQQVDSSD SRNHEGTGLG LAISKSIVQQ
HGGRIWVESV LGEGSSFYFT IPIIEPPQSA ELETAQIQVS ELVTQDSPLV LVCDDDSLIR
TDLRTLLEQR GYRVVAVATG EEAIAQAVSQ NPDVILLDLL MPGMNGWETM AVLKEREDTK
DIPILICSVY KPCQSNQPGA DFVDWLSKPV EESYLLQSLR QLISEPSKRV RILIVEDDND
LADLLITIFE RHEIETFLAK TGREAIRLSQ RVNPDVLILD LILPESDGFT VVDWLQQHNQ
LCSIPVFVYS AKDLDASERQ RLKLGHTEFL TKGRVTIQEF EQRVMDLLGR LTHNQQAEGD
NGSKTNSSG
//
