ID B0JT90_MICAN Unreviewed; 731 AA.
AC B0JT90;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MAE_43710 {ECO:0000313|EMBL:BAG04193.1};
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=449447 {ECO:0000313|EMBL:BAG04193.1, ECO:0000313|Proteomes:UP000001510};
RN [1] {ECO:0000313|EMBL:BAG04193.1, ECO:0000313|Proteomes:UP000001510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 {ECO:0000313|EMBL:BAG04193.1,
RC ECO:0000313|Proteomes:UP000001510};
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(2007).
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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; AP009552; BAG04193.1; -; Genomic_DNA.
DR RefSeq; WP_012267004.1; NC_010296.1.
DR AlphaFoldDB; B0JT90; -.
DR STRING; 449447.MAE_43710; -.
DR PaxDb; 449447-MAE_43710; -.
DR EnsemblBacteria; BAG04193; BAG04193; MAE_43710.
DR KEGG; mar:MAE_43710; -.
DR PATRIC; fig|449447.4.peg.3968; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_17_3; -.
DR BioCyc; MAER449447:MAE_RS18965-MONOMER; -.
DR Proteomes; UP000001510; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 178..321
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 373..597
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 616..729
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 665
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 731 AA; 83355 MW; A185D61CC8CE83C4 CRC64;
MNASPAYVCC QVLSSTHLEQ IRSWWGQLAI QVTAPRISLS ERELPPQTGE IYQLLLSTDL
QALLLASPQG HNFQYEVRIS FEANTIKNFL QGLSVKSLHN PKIQQGYQIL NLPLSINVSS
FQNKILVKIL SIISSPSADR DCSRIFSVCQ PVEAALSQQI QQERLLNQVI TQMRQSLELP
VILETVVREA REFLQVDRLL IYQFFPSTSE VKGKITSESR ISEQINSVLN LTPEDDCFSY
IPQYKEKYRQ GLILAVDDVD ANYSSSFCLS EFLRQHQVQS KLIAPIVVQE ELWGLLIAHQ
CQEKRQWLPQ EKKFLGQIGE HLAIAIYQAQ LYSQVQEQKD IFERRVIERT QELQDTLMAA
EAANLCKSEF LNNISHELLT PLTCIIGLSS TLQKCSAANN FLPPDKQKHY LKVIQDNGNK
LLELINDLLN FSQVSAGKAV LDIKQFSLKY LCNHVLEIIK TEAETKEINL ILEMKITEKE
HYFYADYDRV QQILLYLLKN ALKFTPEQGA VTLRLWKEGS QVIFQVEDTG IGIPAQKIPL
LFEKFTQLDG SRKRRYGGVG LGLALTKQLV ELHRGTIEVE SCLDKGSIFT VRLPQQKPPK
PQPSDNNPHF NHHHPTIVLI ESDEEIANLI CELLMVAHYQ VIWLIDSVSA IKKIEIVQPG
IIIVDRKMPD IYHLCHLLKK SRQTQASKVL ILNDTPEISV NFLGRHGIDD YLLKPIQPSL
LLEKIRYLTA L
//
