ID A0A0D6KWJ0_9CYAN Unreviewed; 378 AA.
AC A0A0D6KWJ0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=FDUTEX481_02229 {ECO:0000313|EMBL:EKF03819.1};
OS Tolypothrix sp. PCC 7601.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF03819.1, ECO:0000313|Proteomes:UP000032761};
RN [1] {ECO:0000313|EMBL:EKF03819.1, ECO:0000313|Proteomes:UP000032761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX PubMed=25953173;
RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA Kehoe D.M., Weinstock G.M.;
RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT PCC 7601.";
RL Genome Announc. 3:0-0(2015).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKF03819.1}.
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DR EMBL; AGCR01000017; EKF03819.1; -; Genomic_DNA.
DR RefSeq; WP_045869048.1; NZ_JH930358.1.
DR AlphaFoldDB; A0A0D6KWJ0; -.
DR STRING; 1188.FDUTEX481_02229; -.
DR PATRIC; fig|1188.3.peg.2239; -.
DR HOGENOM; CLU_000445_114_72_3; -.
DR OrthoDB; 418136at2; -.
DR Proteomes; UP000032761; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.250.690; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; 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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EKF03819.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EKF03819.1}.
FT DOMAIN 11..128
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 150..376
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 60
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 378 AA; 42506 MW; 95BA7E05D1FBB43D CRC64;
MSVAENSKVF RILAVDDTQD NLILVQTILE SEGYEIELVS DGLSALKKVE QSSFDLILLD
VMMPGMDGYE VTRRIRGNPE LKKIYIPILL ITAFHESSVV EGLDVGADDF IRKPFDTDEL
LARVRSLLRL KESLDEQRKM ARQREDFVSR LTHDLRTPLV AADRMLYLFQ EEAFCKISPE
MKQAISVMIR SNQNLMQMVN TLLEVSRFEA GKKTLNWESC DLKETAQEVV SELNPLAMEK
QLTLKVDTHK LDSLGDKAGV VMGDSLELRR VLSNLVGNAI KFTDTGGVEI RLREEPYGPQ
KQTYLTIEVE DTGYGIAPED QATIFERFRQ GKNKRSGSGL GLHLSSRIVE AHGGKIEVTS
VLGQGSKFTV HLPKNTEE
//
