ID D8G9B6_9CYAN Unreviewed; 1748 AA.
AC D8G9B6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OSCI_4080002 {ECO:0000313|EMBL:CBN59206.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN59206.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
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; CACA01000370; CBN59206.1; -; Genomic_DNA.
DR RefSeq; WP_007358377.1; NZ_CACA01000370.1.
DR OrthoDB; 432643at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd04620; CBS_two-component_sensor_histidine_kinase_repeat1; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 8.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
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; 9.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013655; PAS_fold_3.
DR NCBIfam; TIGR00229; sensory_box; 7.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 5.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 2.
DR SMART; SM00116; CBS; 2.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 6.
DR SMART; SM00091; PAS; 9.
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; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 9.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 8.
DR PROSITE; PS50112; PAS; 8.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532}.
FT DOMAIN 17..79
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 88..146
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 228..280
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 281..331
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 350..401
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 585..657
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 661..713
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 714..784
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 792..844
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 845..918
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 921..973
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 974..1044
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1048..1100
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1101..1143
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1177..1226
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1227..1301
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1307..1360
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1357..1429
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1501..1691
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1635..1748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 550..588
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1467..1494
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1678..1702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1703..1722
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1748 AA; 196549 MW; 11747F23538E31AB CRC64;
MISISIPLVQ KDLLSAIAPN PLMVSPDLTV MAAIASMREA GCSYVLVVES SGTHPENSGL
VGIVTERDIV RIITQSTPLD QLPIQSVMSH PVITVQDFAL SDIKAVLTLF QQHQICHLPV
LNGDRIIGLL TKDILTEILT QTVLQLSEGE EAEAILYQYQ RVVSTMTDGI ALLDNNYIYR
LVNQAYLDRT QKQWGDIVGH SVAHLHGETV FKTIIQPHFD RCLAGEVQEY EAWFDYQNAG
RRFIKVTYYP YIELDGKISG VVVTTQDRTA LKQTQAVLQE NEQFLRSIYE GVEQAIFTVD
VLEDGEFRFI GYNPTAERLT GKSNQEIRGT SPGKKVRQRY VDCIQAGVPI TYEECLIFRE
VPTWWMTTLN PIRDASSRIC RIVGTSINIT ERKQAESQLK IQNAILERIA KAEPLGEILE
TLLQAMETQL VDAICSIMLC DRDGKLHLGA AAQLPAAYLQ AIDGVAIGEG VGSCGTAAFR
QETVIVSDIA TDPLWQNFKE LALEHGLQAC WSVPVISNNG LVLGTFAVYH RHIHTPNQQE
LSVVALATNI AGIAIERQQA TQALEQLNQE LETKVEERTA ALHASEERWQ LALKGSNDGI
WDWNLKTNQI FFSSRWKQMR GFTDDEIPNS PDECLSRIHP DDYDRVMAAV DDHFAGKTEF
FEVEYRVKRK DNSYMWVLNR AQGLRDESGE IVRMSGSDTD ITQRKLAEAA LRESERRYAT
LAAAAPVAIF RFDSPLNCVY VSDRWSEMTG RPKESALGRG WMEALHPEER DFLLAKYAES
YAQSTSGQYL LHHSEGRHLR PDGSVNWFYV QVAQEIDAAG RTIGYIGTLT DISDRIQVEA
ELAKSRQNYY SLIQSVNGVV WEYDLNNNRF TFVSDKAEEL LGYPIEAWLS EPDFWRNHVY
AEDVVKAEKL FNDAIQNQNN CELEYRMVAA DGSWVWVYDI SSLNFDRNGK ATMSSGVLID
IRKRKQTEEA LQLSEERFRK AFDNTVVGMC LVSPEGKYFK VNASLCNFLG YTEAELLDLR
FQEITHPDDV ANNLKFANQI LAGEINSYNI EKRYFTKQGQ LVWGLLSVSL VRDVYGKPLY
FVSQIQDITD RKQAEIALQN SEIRFRRVFE SSVVGMIFAD FQGNILDAND RFLKMVGYSR
EELDAGTIIH WDTLTPTEYL PADFAAMERL MRSGAIEPWE KEYYRKDGSR ISVLIGMAFL
PDSGDQTICV VVDISDRKQA ELALQESQRF IQKIADSSPN ILYLYDLQTQ RNVYVNHEIS
SILGYQPEVI QAMGINFTQN LMHPDDLRSV LPAYSEQISM AQDGEIIDTE YRMRHSNGEW
RWLHSRDSVF SRDANGQVKQ IIGNAQDITE RKRLEQAQNR LIAILEASTD YILIADLTGN
AIWNNSALKK LRGLDADAVV TQQNAADYHP QWAVEMLEQQ AITIAIAKGS WLGENVLLDA
ENQQIPVSQL LLAHRSPHGE VEFFSTIMRD MRVYKEYEQQ LERTNAELIR ATRLKDEFLA
NMSHELRTPL NAILGMTEGL QDGVFGIVNE SQIKALETIE HSGTHLLELI NDILDIAKIE
SGQMELEYTS VSINYLCQSS LAFIKQQALQ KHLQVDIKIP LNLPDLWVDE RRIRQVLINL
LNNAVKFTPE GGHITLEVSR QRRTEGQGSG GAEGQGGRGD GEQGGGGAEG QEGTGVEEQE
GTGASEQGGT GTSERFPSSI SPAPSLPRSP APPLPILPRS PAPHLPRFLS ASTSRGVRSE
GLSANCHY
//
