ID I4I9I2_9CHRO Unreviewed; 877 AA.
AC I4I9I2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MICAI_1540004 {ECO:0000313|EMBL:CCI30956.1};
OS Microcystis sp. T1-4.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=1160279 {ECO:0000313|EMBL:CCI30956.1, ECO:0000313|Proteomes:UP000004501};
RN [1] {ECO:0000313|EMBL:CCI30956.1, ECO:0000313|Proteomes:UP000004501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T1-4 {ECO:0000313|EMBL:CCI30956.1,
RC ECO:0000313|Proteomes:UP000004501};
RA Genoscope - CEA;
RL Submitted (APR-2012) 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};
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:CCI30956.1}.
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DR EMBL; CAIP01000062; CCI30956.1; -; Genomic_DNA.
DR AlphaFoldDB; I4I9I2; -.
DR Proteomes; UP000004501; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 356..569
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 743..860
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 70..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 234..268
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 793
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 877 AA; 96700 MW; 48F1FC871922EDEB CRC64;
MIKPDSDHLF NEDLEQLLES LEDKDSDGDE ALEELSFLWE QSSPPASGAS LRQTLSSWTW
EQELEELFGG SINGEEAPSN DLYSTRGAAP KLEPEDGDDL ASLLLENVAV QESEAVITIG
HPNFYDSLED LEAFLEKPTL PAQSPLPDIF ESLEVLLWES TEGDHPQGLE SLEIAPESLL
EDEFRDLEKL LAETDQVMAA NPAASFGSPV GSNNLRPLVS KAFEQTMRVP IKQLDNLSNL
IGELVVKRNR LEEEQDRLRL FLDNLLNQVQ NLSDVGSRMQ DLYERTLLEG ALLASRNAGD
TIGYGRVKGE NQGSSAMTGQ LDALEIDRFT DFHLLSQEMI ELIVRVRESA SDIQFVVDET
DQVTRSLRQA TTQLQEGMTK SRMVPFSQTA DRLPRAIRDI SLKLDKQAKL KVEGGDVLID
KMILEHLNSP MTHLVNNAIT HGIESPQERM AKGKPALGTI SVRAFLQGNQ TVITVSDDGA
GIDANLVKLK AIEKGLISDP EAQNLSPQEV YELLFHPGFS TKDQADDFAG RGVGLDVVRT
SLIDVRGTVT IDSLLDKGTT FTIRLPLTLS ICKALCCVSN HARIGFSMDG VEDMKDFRAR
EIQIDREGRR CVFWQNTLLP FQPLSELLSY NRQLSRGSFY TGKQEEDSFS IVILRGGNNL
LAVQVDQVIG ELEIVIKQIE GPIPKTAGIA GATVLGDGTV MPIGDVLELI DIARGRLRTD
NGGPWRQPLP PVAVKTRQKS GAMVLIVDDS ITVRELLSLS FSKAGYRVEQ ARDGQEAWEK
LRGGLPCDIV FCDIEMPRMN GLELLYNLQK DPQLASIPFA LLTSRGAERH RQVAATLGAS
GYFTKPYTER DLLSAAERMI AGEVLLANSI KATPNPS
//
