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Database: UniProt
Entry: L8N0T6_9CYAN
LinkDB: L8N0T6_9CYAN
Original site: L8N0T6_9CYAN 
ID   L8N0T6_9CYAN            Unreviewed;      1119 AA.
AC   L8N0T6;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Pse7429DRAFT_2395 {ECO:0000313|EMBL:ELS32345.1};
OS   Pseudanabaena biceps PCC 7429.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC   Pseudanabaenaceae; Pseudanabaena.
OX   NCBI_TaxID=927668 {ECO:0000313|EMBL:ELS32345.1, ECO:0000313|Proteomes:UP000011201};
RN   [1] {ECO:0000313|EMBL:ELS32345.1, ECO:0000313|Proteomes:UP000011201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7429 {ECO:0000313|EMBL:ELS32345.1,
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:ELS32345.1}.
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DR   EMBL; ALWB01000099; ELS32345.1; -; Genomic_DNA.
DR   RefSeq; WP_009627531.1; NZ_ALWB01000099.1.
DR   AlphaFoldDB; L8N0T6; -.
DR   PATRIC; fig|927668.3.peg.2858; -.
DR   Proteomes; UP000011201; 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   CDD; cd00130; PAS; 2.
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; 3.
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; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
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; 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); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ELS32345.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ELS32345.1}.
FT   DOMAIN          16..130
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          166..206
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          240..292
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          293..363
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          366..418
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          592..664
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          734..970
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1000..1116
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         1049
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1119 AA;  125512 MW;  AAB30DA24E37E4E4 CRC64;
     MKNIGNLKRS NIPTTKILLV EDDLDDRLFF VQASEQVGLF YDYVMAASFT EAIAILSQHE
     FAIAIVKSQL RDGEASQLLP ILQNINCPCI ITITNGEEET ATKLIAQGSA NYLIRDSDRY
     YLKMLPAIIK ATISSHQTIV KLQEQNQALN IELQERIAAE KNLRDREDRY QQILDSIPDL
     ILVKESGSRV VWGNKTFRDF YGISLECLKE NIETQFNFPF DTRQYICDDN FVFSTGQTLH
     ISEESATRRD GSVRLMSTIK TPIFDEDGEV RKIVVISHDI TARKEATNSL QESERRFKTL
     ATVVPVGIFR TDKNGNCIYV NERWSEIAGL SLEEALGEGW TTALHPDDRD KINNEWYLSA
     QQNRPFKLEY RFLRKDGSTS WVLGQSLAET DLSGQIFGYV GTITDISDRR KAELTLQKLV
     EGTAALTGLE FFPAVVSHIA EALAIPFVSV TELIGDHLHT LSFWAKGSLQ PSIAYPVRDT
     PCEYVLKDGE FYCESQLQTY FFNDPYLAEM QADSYLGIAL KDNLGNVIGN LCIIDTQPLD
     KSKYNESIAI LRIFGARVAA ELERKAATEA LYRLNQDLEI RVERRTQALQ ESEIRFRRMF
     DSNVVGMLFA DFDGNILDAN DRFLQMIGYS REEFNTGKIF WHNLTPPEHV PADYAAMGKL
     MEHGFIHPWE KEYYRKDGSR IPVLIGAAFL PGTENQTICV VIDISDRKQY ETQLKQTNAE
     LAIATRLKDE FLANMSHELR TPLNAILGMT ESLQEEVFGS INENQKKSLK LIENSGFHLL
     KLINDILDLA KIESGQVELD LASSNIEVLC QSSLAFIKQQ SHKKHIQIET KISPDLPNVS
     IDERRILQVL INLLSNAVKF TPEGGRIVLE VSDRQQATLN HSDQTVEVPS LQKYLQIKVI
     DTGIGISPEN IDKLFQPFIQ IDSALNRQYE GTGLGLSLVK RIVELHGGQV SLVSEVGVGS
     SFTITLPCAD CQIASPAPET QPEALTATDE NGSEFKNPFK ILLVDDNEAN LMTVASYLSA
     KGYDMILATN GEESITLAQL QAPDLILMDI QMPGTNGLET IKQMRQIPSL ANQPIIALTA
     LTMQGDREKC IAAGATEYLA KPVKLRQLVL TIQQLQTAS
//
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