ID A0A1Z4LQJ7_9CYAN Unreviewed; 837 AA.
AC A0A1Z4LQJ7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=NIES267_29950 {ECO:0000313|EMBL:BAY83506.1};
OS Calothrix parasitica NIES-267.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1973488 {ECO:0000313|EMBL:BAY83506.1, ECO:0000313|Proteomes:UP000218418};
RN [1] {ECO:0000313|EMBL:BAY83506.1, ECO:0000313|Proteomes:UP000218418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-267 {ECO:0000313|EMBL:BAY83506.1,
RC ECO:0000313|Proteomes:UP000218418};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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; AP018227; BAY83506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4LQJ7; -.
DR OrthoDB; 9788063at2; -.
DR Proteomes; UP000218418; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR007891; CHASE3.
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; 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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAY83506.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:BAY83506.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 288..340
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 337..407
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 409..461
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 474..696
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 717..833
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 198..225
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 768
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 837 AA; 94378 MW; 82CFF6190DB10719 CRC64;
MMKSFSRNKL KILLLLALCL VFSGAVISCG SIIKLNANQK NVNNSNEIIL RLDKTISEFT
NAHTARYKYL KSTNTDYLKF YISAREKIDA NIQSLKKLTK DNYQQQQKVF LLEKTIFNQL
NIFEEGFYIK QKNKLNLSNK LVSKKPIERL IDSIEKNEKS LLLNQIEISQ LSLKKATIAF
LIAGLINLGL VLQFYYLLKN YITKLKKTES ALRQSENRLR AIIDAEPASI KLIHTNSNIL
EINASGIEMM EVENADALVG KSIYTAVPPE YQTAYKLMHE SVCSGNKETL EFEIVGFKGT
RRWMETYAIP LPNENDSGFL HLAITQDITQ RKASEQKLQE QAALLDVVTN AILVKDIQNK
ILYWNKGAEN IYGWSASEVY GKKSSRLLHR EYSSQQDDAL LSVINVGQWE GELHQITKEG
KDIIIQSRWT LLRDEKERPK YILAENTEVT QKKKLETQLL RTQRLESIGT LAGGIAHDLN
NVLTPILMSV QLLERKLQDS QYIQLLKTLE NNAQRGAGLI KQLLSFARGI EGKKSLIQTK
YLIAEIEQVI RETFPKSIKL NINIPTNLSC VCGDATQLHQ VLMNLVVNAR DAMPNGGELD
ISAENLLIDE CYVQMNAYAK TGAYIVVTVT DTGVGIHPEI QERIFEPFFT TKELGKGTGL
GLSTALGIVK NHGGFVNVYS KLNKGTIVKI YLPIQQTEET NIDDCDELED LNGSGELILV
VDDEPAIRKI TKSSLEAYNY RVLTASNGLE ALDIYARYQQ EINLVLLDMM MPEMDGETTI
ATLQKINREV KIIAISGLVL NYNTVSPQSL CVKAFMSKPC TGKELLHTIA KVSRDFR
//
