ID   Q118H3_TRIEI            Unreviewed;      1130 AA.
AC   Q118H3;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Tery_0662 {ECO:0000313|EMBL:ABG50101.1};
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG50101.1};
RN   [1] {ECO:0000313|EMBL:ABG50101.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101 {ECO:0000313|EMBL:ABG50101.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC       {ECO:0000256|ARBA:ARBA00005381}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000393; ABG50101.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q118H3; -.
DR   STRING; 203124.Tery_0662; -.
DR   KEGG; ter:Tery_0662; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG2114; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_114_10_3; -.
DR   OrthoDB; 9815750at2; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd12913; PDC1_MCP_like; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR033479; dCache_1.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00304; HAMP; 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; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          385..437
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          459..681
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          720..837
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          877..1003
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   COILED          429..459
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         770
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1130 AA;  127094 MW;  B23761E8B27A427E CRC64;
     MAKKSLKQLN KKTNFLEEIP LTYFLVIPFL LQLLIVVGLT GWLSFRNGQK AINALASKLR
     KQVAIHIVRE VDNYLQIPHQ INQLTAYAIN EDNLSIFPVR GQGLFWLQMN LFKSIQWIYC
     GSPEKGEYMG VTRLPQKSEY MGEQRLGKND MLWLAFSNEL TNFFRYEYAL DSQGNMTNLV
     IQGSKKFDSR NRPWYQAGES AGKATWSEIY KDFATGKLTI TATLPVYDRE NNLKVICGVD
     IFFSEELSLF LKTIEIGDTG EAFILNNKGI LIASSVVEDK DKLGFQKAID SNNQLIKSAT
     QYLIEQYKNL SQIETTKKLN FIQDGEKIFM QVSPYKDKHG LHWLTVVVIP ENEFMAQINE
     NTKSTIRLCI LALAIASGLG LLIVNWITKS IKKLSTAAYA ISHGEINQNV SIQGFKELVI
     LAESFNKMTK ELAESFNHLE RKNQELQHLD QLKDEFLANT SHELRTPLNG IIGIAESMMD
     GATGNISELQ NKNLSMIVVS GHRLANLVND ILDFSKLRHH SIKLKMSSVG MREVTEVVLT
     FSRIILKEKD VQLINAISSD LPPVEADENR IQQIMHNLVG NAIKFTEVGV ITISAELIDL
     KNNPKMAITV SDTGIGIPED KHEAIFASFE QGDGSTERRY GGTGLGLPIT KQLVELHGGT
     ISVKSNPGVG SEFTFTLNIS KEPVHSFSLK NVNNLIEGVE TSVDINKNEN HLIPNNGNFH
     ILVVDDEPIN IQVLNNYLKA NNYQVTQALS GKEALAALEN NHNFDLILLD IMMPNMTGYE
     VCSQIREKYP AQSLPVLMLT AKNQIADLVM GFQFGANDYL TKPFAKDELL TRIQTHIKLS
     KITKAYERFV PHEYVELLSK ESIINVKLGD RVSTEMAIFF SDIRSFTTIS EQMTSQETFA
     FVNGYLKEVC PEIRDRNGLI IKFLGDGIMA VFPDGADDAL EAAIAQLKRL QEYNQFLLST
     GWMPIKIGIG IHWGHIMVGI VGEKGRMSGD AFSNNVNLTA RLEGLTKFYG VSLLISESAF
     NYLKNPQKYQ IRFLDRASVK GIDEPINVYE VLDGEVDEIR ELKLQTQVDF ALGLESYRVG
     ELVDAKDYFE KVLAVNSSDK TAQLYLERID DLMVTGVPKN WNGVWAFTQK
//