ID D8G5R5_9CYAN Unreviewed; 1055 AA.
AC D8G5R5;
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_3570019 {ECO:0000313|EMBL:CBN57955.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN57955.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CACA01000321; CBN57955.1; -; Genomic_DNA.
DR RefSeq; WP_007357145.1; NZ_CACA01000321.1.
DR AlphaFoldDB; D8G5R5; -.
DR OrthoDB; 581426at2; -.
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; cd12913; PDC1_MCP_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 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; IPR033479; dCache_1.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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; 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; 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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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:CBN57955.1};
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..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 367..419
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 585..815
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 840..956
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 411..445
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 889
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1055 AA; 117993 MW; CCC0E3D3237366C0 CRC64;
MPSTAFSSRK LPLRFVLVGP FLLQIFAAVG LTGWLSLRNG QKAVNDVATQ LRSEISNRIE
QNLHTYLASA HQVNQSLAAT INLNLLDVQN QNGLERYFWH QLQVFESVNA IYFGNPLGGL
ALVQRHEDDK LFIRATEGFV SGKFFWYSTD SFGNRKKLEK VTPVFDARTR PWYKAALAAR
KPTWSAPFLV FGRNNLGITA SQPVYNSTGK LIGVLGTQLL DSETRDFLNS LKIGKSGKTF
IMERSGLIVA SSTSEKPFLV SKDGKVDRMK ATESSVPLIR VSSQYLIDNF GLSKINTNQQ
LTFNLGGKQQ FLQVTPFKDG RGIDWLIVVA VPEADFMDQI NANTRTTIFL CFLALLMAAT
IGIFTSGWIA EPILRLRNAS QAIASGKLNQ KVEIEGIGEL DILAESFNLM AQQLQESFTA
LENTNEELEQ RVNERTAALR ESEALLNQTQ RIAKVGGWEM NLETQELTWT EEVYHIYEVD
LDFQLTPESV MAFYPSESIE ILEKASLQAM ANKEPFDVEL QFVTAIKNQR WVHVLGQPHY
KNDIPFKLKG TFQDITDRKN AEVTLQEAKL AADAANQAKS EFLANMSHEL RTPLNGILGY
AQILQRDSSL TPKQLAEINI IYKCGSHLLT LINDILDLSK IEARKMELYP SSFYFLGFLQ
VVSEICRIKA EQKGISFICN FDAALPYVVE ADEKRLRQVL VNLLGNAVKF TDAGAVTFKV
AVVDLISVES TTSTLTNINT IRFQIEDTGV GMTSEQMQKI FQPFEQVGDT RRMVEGTGLG
LAISLKIIEM MGSSIKVASK SQAGSQFWFD LALPSSGEAE TLLTTEPTQT ILGFTGDKRK
ILIVDDRWEN RSVIVNLLKP IGFIVAEAAN GLEGLDRVRE LSPDVIITDL VMPKMDGFQL
VRRLRESPEF REIVVIVSSA SVFETDQYNS LDAGADAFLP KPVQISDLFG LLEQFLGISW
LYRDSVELPS PTAKTIKENL ALSPTVIIVP PPSEKIDILY DLIMKGNLKE ILKQAENLKA
LDANFIPFAD RLCEFAKKFQ EKQLKSFISQ YTQKD
//
