ID D8FWK7_9CYAN Unreviewed; 1008 AA.
AC D8FWK7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OSCI_1060015 {ECO:0000313|EMBL:CBN54747.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN54747.1, 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};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR EMBL; CACA01000103; CBN54747.1; -; Genomic_DNA.
DR RefSeq; WP_007353972.1; NZ_CACA01000103.1.
DR AlphaFoldDB; D8FWK7; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBN54747.1};
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 321..373
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 396..475
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 524..756
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 793..906
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 914..1008
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 842
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1008 AA; 111531 MW; E73CEA1B963B22FA CRC64;
MKFWKRSLLN QLVSYFSVLS VVTVSIVAWA AYTRAKDALQ QSVQDRLTVA TSLKEFQLNQ
WVETQRKDVL LMSQLPEIQQ QIAILLTVDN LDPSYKIAVE RLTKYFSDII AVKPSLQSVL
ITTNGGFVVF VYGENTNIQG KFRPLGDPTT YFTREGANAV VPNFYASNGK SAITFATPIL
DRNGVKMGAI AVNLDLKGVD DLIREKTGLG KTGETYLVGR ANNRNIFISG DEKNTNSDEG
VNSFGIDAAL AKNNGQGLYK NYKKVPVISN YRWLTNQNLA LLAEMSQAEA FEPANRLARE
ILLIGLSSAG ILLVAVYLMS RRITQPILAI ANTAIEVASG NLNSSAPVLT EDEIGILAQA
FNQMTGQLKL SNQKLSNYSQ TLEQRVTAAT AELQDTMSYL ASIIDTIADG LLVTNYNGRI
TRFNPALTNM FALDRLDLTG KFTEEIFGSE VSKLIDNTKQ PPHEISTVEL ALQGGRFAKG
SAVAILKKSA SDSQAPTYIG SVILIRDITA EKEVDQMKTD FISTVSHELR TPLTSVLGFA
KLIQKKLEEN VFPIVVTEDK KVQRAVKQVG DNLQIIVSEG QRLTDLINDL LDVAKMEAGK
IDWKMQPMKV DDLIDRAIAA TFALFENKGL EPIKDIEENL PELVGDRDKL IQVMINLLSN
SIKFTDKGFV TCQAKKIGDK IKISIIDTGM GISEADQPKV FEKFKQVGET LTDKPKGTGL
GLPICKQIIE HHGGKIWVES ELGKGSNFSF ILPLKPAEEA ESSLKKLDMT TFLKQLRDRV
SNATLGGNEQ KKTILVVDDE ANLRQLLRQQ LEAEGYIVKE AKDGKEAVVM AKQELPDLII
LDVMMPEMNG FDVAAILRND PMTMSIPIVI NSGIEDKERG YRIGVDRYFV KSSDSEPMLQ
EIGWLLSQGS SKKKVLIVDE NVSEVRSLAD VLKARGYSVT EALTGEEFRN KAMSVKPDLI
IANADVWQKS EILQALRFEK DLENTFFLML GENKGDTIQI DIKTNEPN
//
