ID   U9VLS8_9CYAN            Unreviewed;       621 AA.
AC   U9VLS8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=N836_02005 {ECO:0000313|EMBL:ESA33565.1};
OS   Leptolyngbya sp. Heron Island J.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya group; Leptolyngbya.
OX   NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA33565.1, ECO:0000313|Proteomes:UP000017515};
RN   [1] {ECO:0000313|EMBL:ESA33565.1, ECO:0000313|Proteomes:UP000017515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Heron Island J {ECO:0000313|EMBL:ESA33565.1,
RC   ECO:0000313|Proteomes:UP000017515};
RX   PubMed=24503993;
RA   Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA   Fromme P.;
RT   "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT   Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL   Genome Announc. 2:e01166-e01113(2014).
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:ESA33565.1}.
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DR   EMBL; AWNH01000098; ESA33565.1; -; Genomic_DNA.
DR   AlphaFoldDB; U9VLS8; -.
DR   STRING; 1385935.N836_02005; -.
DR   PATRIC; fig|1385935.3.peg.5899; -.
DR   eggNOG; COG2205; Bacteria.
DR   Proteomes; UP000017515; Unassembled WGS sequence.
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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13492; GAF_3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ESA33565.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017515};
KW   Transferase {ECO:0000313|EMBL:ESA33565.1}.
FT   DOMAIN          376..607
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          339..372
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   621 AA;  68835 MW;  2280CD9DB06F6AE5 CRC64;
     MFLIRTGKTR KQLSIGLEIP DETMRSQLIV DPEPMAVPAT VDNSSLKVIH DPYGRIVSIS
     WPRSIQVNSS RYLHESISQL FGPVAVGPYL QRMAQVLVDG QSQQFQCVVR CGPHPVGLDF
     TLSTVDWPDD PDHQYLQGEG SILTVAGTAS MPHHLSTMGI IADPPANTAQ AGLLANISNY
     HGVLTSIASN IRKTLELETI WQQTVDGLGT LLDLHRCLVC DYSVAMQTLN VVAEFHQPEL
     QPCLGQTFEL TNKADFRCTI NTLKPVLSDF EREDNDAGPY TVLTVATCYR DEPNSVLLLQ
     MPPERPWHPL EIELVNELTD QVGTAIAHAK LFEASRTLAD DLQKANEKLI DKNDELEEAR
     RYAEEASRLK SEFLANTSHE LRTPLNGMIG FLRLVLDGMA DDPEEQEEFI AEAHKSALHL
     LNLINDVLDI AKIEAGKMEI DLTAVSLQEL FCDVENFTRP QAEQRGLYFN MKMPATLDEI
     KLYGNYQRIL QVLLNLIGNA IKFTPEGGVT ISAEVKPQSV RFQGQVWPGH IKISVEDTGI
     GVSLEKQNRL FQTFSQVDGE RTRQYGGTGL GLAISQRLIE AMGGKVQFIS MGEGLGSTVT
     FTAILYQEPV IMAESEGKQP V
//