ID K9TB34_9CYAN Unreviewed; 1500 AA.
AC K9TB34;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Ple7327_4528 {ECO:0000313|EMBL:AFY79628.1};
OS Pleurocapsa sp. PCC 7327.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC Pleurocapsa.
OX NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY79628.1, ECO:0000313|Proteomes:UP000010382};
RN [1] {ECO:0000313|EMBL:AFY79628.1, ECO:0000313|Proteomes:UP000010382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY79628.1,
RC ECO:0000313|Proteomes:UP000010382};
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 genome of Pleurocapsa sp. PCC 7327.";
RL Submitted (MAY-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};
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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; CP003590; AFY79628.1; -; Genomic_DNA.
DR RefSeq; WP_015145923.1; NC_019689.1.
DR STRING; 118163.Ple7327_4528; -.
DR KEGG; plp:Ple7327_4528; -.
DR PATRIC; fig|118163.3.peg.5063; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_248708_0_0_3; -.
DR Proteomes; UP000010382; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd04620; CBS_two-component_sensor_histidine_kinase_repeat1; 1.
DR CDD; cd16921; HATPase_FilI-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 6.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 3.
DR Gene3D; 3.10.580.10; CBS-domain; 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; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 6.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 5.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00116; CBS; 2.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 6.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 6.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010382}.
FT DOMAIN 14..69
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 78..136
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 155..226
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 227..281
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 300..347
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 361..412
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 413..485
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 489..541
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 617..670
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 671..741
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 745..797
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 798..870
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 874..926
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1102..1238
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 1272..1496
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1500 AA; 171463 MW; AD5539055E7460A3 CRC64;
MERLLDKLAL EQVIERSPLT ISPDISVVDA IALLARTQVS CIPVVEDSKL VGVFSPKDVV
RLVASGEDLS GVRIDRVIEQ PVMALKLSDS DNLSTALSLL HQQGTCSLPV LDERERFVGL
VSACQLWGTL RQKIERQVDE RTDELAWTNT LLQKRERQLK LALQAAKLGF WELDLKTEEL
SSSSQCKANF GLPPEADLSN ARLFELIHPD DRDRVRESLR KAIEQQTDYE AQYRNIWLDG
SIHWVLARGR GTYEADGTPT SMLGVTFDIT ERKQTEEALR ESETRLQKLA ANLPGVIYTF
VIYPDGSMKF EYISEACREI QEVEPEEVLR NAAILYEQIH PEDLQKVLAA NAMSAQTLEP
FACEWRIITK SGKLKWVRAI SRPERRDNGQ TVWYGTLLDI SDRKLVEQQL RQSEARFQIL
ARATNDAVWD WNLLTNEIWW NEAVQTLFGY SKEQVGTEVS WRYENIHPED RERIVSEIHG
IIDRDRQYWS NEYRFRRADG SYADIFDRGY IVRDNTGKPV RMLGAMMDIS DRKRAEEALR
QSEATLHSFF DSAPTMMGIV ELRDNDIVHL IDNAVTAQLF GRTPAAMQNQ LDSQLGIPQE
HISLWLDRYR EAKRTGIPVR FEYFHPVPDG VRWLSAIVSA IAGGSESHPR FAYIAEDITE
RKRAEAALRE SEKRFYNAFE YAAIGMALVA IDGRWLKVNR ALCEIVGYSQ EELLATSFQA
ITHPEDLESS IAYMQQLLAG EINTYQIEKR YLHRQRHTVW VLLSVSVVRD DRGQPLYFIA
QIQDITARKQ AEASLRESEE RWQLAIRGTN DGIWDWNVKT NEVFFSPRWK EMLGYEDGEI
ANHLDEWLKR VHPDDLGWVT QALEDHFNQK TPFYITEHRV RCKDGTYKWI LDRAQALWDE
RGNVARMSGS HTDITNRKQR EELLENIARG VSAEIGEAFF QSLVKYLSKA LKVEYAFISE
IVDPESNLAR TVAGYSDGRA IENFEYALTN NPCGDVIGKQ ICVYPQNLQQ QFPHNEILQQ
LGAESYLGVP LFDSSGRTLG GISILSRQPL RDARLMEETL KIFAVRAGLE LERRQAEAEL
VRQNQRSHLF SEITLKIRQS LQPEEILQTA VTEVQKLLSA DRVLVFRLWD DGSGTVVQEA
VLPDFSEILG QQIYDPCFSR DYQQKYRQGR VSAIADIRNA GIESCHVELL ERFGVKANLV
VPILQWEKCW GLLIAHQCDR PRQWSRFEIE LLQLLANQIG IALAQAQLLE REVRQRQELA
RSNAELQQFA YVASHDLQEP LRMVTSYLQL LAKRYQGKLD ARADEFIAYA VDGSNRMKTL
IDDLLSYSRV STRAQPFELV DCNVILEMAI ANLQVTINET GTAITRAPLP QVMADATQLM
QLFQNLLSNA IKFRTEGVPP QIHIGAVRRQ EAASSPASSS KEWLFWVRDN GIGIEQQYAD
RIFAIFQRLH GRGKYPGTGI GLAICTKIVE RHGGRIWVES ESGKGATFYF TIPERTGNLS
//
