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Database: UniProt
Entry: K9WHA2_9CYAN
LinkDB: K9WHA2_9CYAN
Original site: K9WHA2_9CYAN 
ID   K9WHA2_9CYAN            Unreviewed;       655 AA.
AC   K9WHA2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Mic7113_3415 {ECO:0000313|EMBL:AFZ19144.1};
OS   Allocoleopsis franciscana PCC 7113.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX   NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ19144.1, ECO:0000313|Proteomes:UP000010471};
RN   [1] {ECO:0000313|EMBL:AFZ19144.1, ECO:0000313|Proteomes:UP000010471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ19144.1,
RC   ECO:0000313|Proteomes:UP000010471};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL   Submitted (JUN-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};
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DR   EMBL; CP003630; AFZ19144.1; -; Genomic_DNA.
DR   RefSeq; WP_015183287.1; NC_019738.1.
DR   AlphaFoldDB; K9WHA2; -.
DR   STRING; 1173027.Mic7113_3415; -.
DR   KEGG; mic:Mic7113_3415; -.
DR   PATRIC; fig|1173027.3.peg.3759; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG3437; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_51_3; -.
DR   OrthoDB; 9788063at2; -.
DR   Proteomes; UP000010471; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 1.
DR   CDD; cd19920; REC_PA4781-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFZ19144.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010471};
KW   Transferase {ECO:0000313|EMBL:AFZ19144.1}.
FT   DOMAIN          10..126
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          155..203
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          227..279
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          292..515
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          536..652
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          121..155
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         59
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         587
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   655 AA;  73032 MW;  AA8DC41B371A4D3E CRC64;
     MSADPTNQSV ILIVDDTPTN LEMLFDFLGL AGFKVLIAED GESAIERAEY APPDLILLDV
     LMPEMDGFET CRRLKANELT KDIPVIFMTA LSETTDKVKG LNLGAVDYIT KPLQHEEVLA
     RVQLQLRLRN LMKTLQEQNQ RLEKEIQQRH LSEQKIREQA ALLDITTDAI LVQDLDNQIL
     FWNKGAEQVY GWTAEEAIGK HALKLLYREA LCDIENPSQL LAECGSWQGE LRHVTKQGKE
     IVVATRWTLV CDEQGVPTSI LTVNTDVTEK KQLEAQFLRA QRMESLGTLA SGIAHDLNNA
     LTPIMMTVQL LETKLHDEQS QEWLSIMETN VRRGADLVRQ VLLFSRGLEG RRSTLKVEKL
     ISEIEQIVKQ TFSRAIEIHT DLPAQNLWTI RGEATQLHQV LMNLCVNARD AMSEGGILKI
     SAANLWVDES YARINLDAKV GPYVVITVTD TGSGISREII DKIFEPFFTT KDLGKGTGLG
     LSTAIGIIKS HGGFVNVDSQ VGKGTEFKVY LPVTQSRETD GIQTDHHELL AGHGELILLV
     DDEESIREVS KTLLEANGYK VLVASDGIEA LALYTEHKEE IRAVLIDMMM PSMDGPTTIR
     VLQKMNPQVK IIGVSGLVSN HKMIELVGSC VKTFLPKPYT SNELLKNLQT VLSTH
//
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