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Database: UniProt
Entry: S3K9C2_MICAE
LinkDB: S3K9C2_MICAE
Original site: S3K9C2_MICAE 
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
//
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