ID L8MWQ3_9CYAN Unreviewed; 1154 AA.
AC L8MWQ3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Pse7429DRAFT_2947 {ECO:0000313|EMBL:ELS31911.1};
OS Pseudanabaena biceps PCC 7429.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=927668 {ECO:0000313|EMBL:ELS31911.1, ECO:0000313|Proteomes:UP000011201};
RN [1] {ECO:0000313|EMBL:ELS31911.1, ECO:0000313|Proteomes:UP000011201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7429 {ECO:0000313|EMBL:ELS31911.1,
RC ECO:0000313|Proteomes:UP000011201};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(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:ELS31911.1}.
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DR EMBL; ALWB01000129; ELS31911.1; -; Genomic_DNA.
DR RefSeq; WP_009627985.1; NZ_ALWB01000129.1.
DR AlphaFoldDB; L8MWQ3; -.
DR PATRIC; fig|927668.3.peg.3362; -.
DR OrthoDB; 475707at2; -.
DR Proteomes; UP000011201; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd04620; CBS_two-component_sensor_histidine_kinase_repeat1; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 4.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00116; CBS; 2.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Kinase {ECO:0000313|EMBL:ELS31911.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ELS31911.1}.
FT DOMAIN 17..92
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 101..162
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 383..455
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 459..512
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 596..648
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 649..721
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 725..778
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 854..906
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 924..1149
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1154 AA; 131621 MW; AEBA3451E2067355 CRC64;
MSNHADDFTL NELRSAIVRN ILTVSPETPV IEAIAQMLSF DSDHTDGNDG IDEDYIHQEA
RSRCVLVVDK EKVIGIFTER DVFRLSVHQR SLEQLTMQAV MTSPVIAIQE SEFTDFLAVM
HLLQKHRIRN LPILDDSDRP LGLLTQESLW QLSLSQLLIH QTAQKEVIGI SKIAISRQQA
AIQKLKSAEQ ALKIQRDFNQ LIAEISSRFI DVSPHNLDVE IVSALQLVCK ATNSDTSYLI
KYDIAEPSDD AISSLPEGTV SVTHAWSKPE YSQQMTLVKN IPLTLFPWSH TQLLQRQIVN
IPNVADVPVE AAIDRSHWQK FHLVSNLSVP LIQKSVVKGL IGFASFSHVT HWDGESIRLL
QVMGQAIANI QERIQSEYNL QVSENRLRLA LCAANQGLYD LDLLSGSVIV NAEYAMMLGY
DPDTFQETNA KWMERMHPDD RDRTLEIYTN YIAGVLPDYE VEFRQRTKTG EWKWILSLGK
IVARDEWDNP VRMIGTHTDI SDRKKAEAEK LLAEQVRKEL KLLESLFDII LAGYWDWDIQ
TNEEYLSEGF KKMFGYEDAE LPNSPETWQN LIFAEDLVKV LESFDRHVES HGALPYRNEV
RYRHKDGSTV WVICLGKVIE WDGDRPLRMI GCHIDISDRK KSEEALRLSE ERLNLALEAA
GDGLWDWNIP TGDLYLSPQW AEMIGFESNE LAADVSVWEQ LIHPDDKPWV MECLNAHFAD
ATVPYKFDYR VRTKSGKYCW IANYGKVVRR DAEGNPLRMI GTHRDMTISK QTEEKLRKSD
THLKTAQRIG KLGSWEFDPH KGRILWSDEM FQIFGRDPQL GTPSFEELQQ LIHPDDREFH
QQLVQSAISE IQPYNLEIRF YRFDGSLGYL QSRGEPIVDE VGHLLLLIGT ALDITDRKQS
EAKLRQTTAQ LAASNHELEA FAYSVSHDLR SPLRAIDGFS KALIEDYGDK FDDDAKDYFD
RIRRNVSRMG TLIEDLLRLS RVSRSEMQYG QVNLSQLVQE QLDELKALEP DRQVEIAIAD
GVVVLADLAL MRIAISNLIQ NAWKFTSHHP IARIEFGVIA SHGDRANIAN IQDDQLVYFV
RDDGAGFDMN YANLLFGVFQ RLHNTNEFAG TGIGLATVQR AIHRHGGQVW AEGAVEKGAT
FYFTLADLSL VQEL
//
