ID D8FUP3_9CYAN Unreviewed; 727 AA.
AC D8FUP3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-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_560001 {ECO:0000313|EMBL:CBN54083.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN54083.1, 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; CACA01000053; CBN54083.1; -; Genomic_DNA.
DR RefSeq; WP_007353310.1; NZ_CACA01000053.1.
DR AlphaFoldDB; D8FUP3; -.
DR OrthoDB; 9772100at2; -.
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; cd00082; HisKA; 1.
DR CDD; cd12913; PDC1_MCP_like; 1.
DR Gene3D; 1.10.287.130; -; 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; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBN54083.1};
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..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 368..420
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 469..727
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 412..446
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 727 AA; 81676 MW; D9C48AE3A268064F CRC64;
MKTRHSSKEQ AFSLQLVLII PFVLQIFGAV SLVGYLSFRN GQKAVNELAN QLMERTNSMV
NQHLDSYLSI PHKVSQINAD AIRMGLLDVR DRKTVGKYFW HQMQAYDLTY IGIGLTTGEG
AGAGSYDGKT VVIDDWSAKL PNNCYTYATD DRGNRTKLAT ITDWDNFTMP WYTEPVKAGK
PVWSGIYTWN YPNYPFIVAS AGRPIYDAQN RLLGIVGADI HLLKLSDFLR SMKVSQSGQV
FILERNGMLI ANSAKEQPFV LVKNEIQRLK AIESGNPLVQ GIAKQLQQRF KNFQNITEAK
QLKFDLKEEP YYLHVTPWRD KYGLDWLVVV SVPESEFMAE INANTRTTIF LCLGALGVAS
AMGIFTSRWV VQPILRLNQA SKAMASGNLD QAVEDSGIKE LNTLAQSFNY MAKQVGESFT
ALEKSNEELE NRVEVRTVEL KNALSELHST QAQVIQSEKM SSLGELVAGV AHEINNPVNF
IHGNLTHAED YIQNLLYFVQ LYQQQYPQPT PEIQTVAEEI DLDFLQEDLP RILSSMRIGT
DRIRQIVLSL RNFSRKDEAD IKAVDIHEGI DSTLMILQHR LKGQSGRPEI ETIKDYGTLP
LVECYAGQLN QVFMNILTNA IDAIEEGNAN RTFEEVEVNP GRIKIRTSVT ADQWVQIAIA
DNGPGIPEDI QQRIFNPFFT TKAIGKGTGM GMSISYQIIT EKHRGKLKCS STLGQGTEFA
IEIPIQQ
//
