ID S3K9C2_MICAE Unreviewed; 1025 AA.
AC S3K9C2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MAESPC_02594 {ECO:0000313|EMBL:EPF21549.1}, MAESPC_02657
GN {ECO:0000313|EMBL:EPF21490.1};
OS Microcystis aeruginosa SPC777.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=482300 {ECO:0000313|EMBL:EPF21549.1, ECO:0000313|Proteomes:UP000014617};
RN [1] {ECO:0000313|EMBL:EPF21549.1, ECO:0000313|Proteomes:UP000014617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPC 777 {ECO:0000313|Proteomes:UP000014617}, and SPC777
RC {ECO:0000313|EMBL:EPF21549.1};
RX PubMed=23908289;
RA Fiore M.F., Alvarenga D.O., Varani A.M., Hoff-Risseti C., Crespim E.,
RA Ramos R.T., Silva A., Schaker P.D., Heck K., Rigonato J., Schneider M.P.;
RT "Draft Genome Sequence of the Brazilian Toxic Bloom-Forming Cyanobacterium
RT Microcystis aeruginosa Strain SPC777.";
RL Genome Announc. 1:e00547-13(2013).
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:EPF21549.1}.
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DR EMBL; ASZQ01000219; EPF21490.1; -; Genomic_DNA.
DR EMBL; ASZQ01000217; EPF21549.1; -; Genomic_DNA.
DR RefSeq; WP_016515848.1; NZ_ASZQ01000219.1.
DR AlphaFoldDB; S3K9C2; -.
DR PATRIC; fig|482300.6.peg.2901; -.
DR OrthoDB; 2079555at2; -.
DR Proteomes; UP000014617; 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 CDD; cd00156; REC; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 2.
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; 2.
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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:EPF21549.1}.
FT DOMAIN 330..565
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 739..856
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 895..1012
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 789
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 945
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1025 AA; 113126 MW; 72A2FC0305BF3DE6 CRC64;
MMKPDWDHFF NEDLEQLLES LEDKDTEGNE ALDELSFLFE QISPPAARYG ASLDQTLSFL
PLEPELEELF GDSINWEETA TNDLHSTRGT AAKSEAEDWD DLESLLLENA TVQDSEAIIT
ISNPNFYDSL EDLEAFLEKP TPPAQSLLPD IFESLEVFLW ESTAGEPLAA TEPLQRLESL
EIATESSPEP EFKDLEKLLE ETNPPVGLNN LRPLVGKAFE QTMRVPIKQL DNLSNLIGEL
VVKRNRLEQE QDRLRLFLDN LLTCVQNLSD VGVRMQDLYE RSLLEGALLA SRNAGGAIGY
DGVQGKNQGN STMTGELDAL EIDRFTDFHL LSQEMIELIV RVRESASDLQ FVVDETDQVT
RSLRQATTQL QEGMTKSRMV PFSQTADHLP RAIHDISLKL HKQAKLKVEG GGVLIDQMIL
ENLNSPMIHL VNNAITHGIE SPEERLAKGK PVHGTISVRA FLQGNQTVIT VSDDGAGIDV
NLVKLKAIEK GLISDREAQN LSTQEVYEIL FHPGFSTKDQ ADDFAGRGVG LDVVRTSLID
VRGTITIDSV LGQGTTFTLR LPLTLSICKA LCCVSNHARI GFSMDGVEDV RDFRARDIQM
DREGRRCVFW QNTLLPFQPL SDLLSYNRQL SRGSFYTGKQ RKDSFAIVIL RGGNNLLAVQ
VDQVIGEQEI VIKQIEGPIP KTAGIAGATV LGDGTVMPVG DVLELIDIAS GRLRIDNGGL
WRQSVPPVDV EISQKSEAMV LIVDDSITVR ELLSLSFSKT GYRVEQARDG QEAWEKLRGG
LPCDIVFCDI EMPRMNGLEL LSNLQKDPRL ATIPVALLTS RGSERHRQVA AKLGASGYFT
KPYTEIDLLS AAERMIAGEV LLANSIKATS NQLSSSDTTI IDSDSANLLA QSSPLVLIVD
DSLIVREMLA ISLVKAGYRI EQAQDGLEAW EKLQAGLACD LILCDIEMPR LNGLELLSRL
QEDEQLQGIP VAIIAYQGTQ KMQHLAAAKG AKGYFVKSYI EDVLLSAAQR LIAGEVLIQK
ESSVD
//