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Database: UniProt
Entry: A0A1E2WUN6_9NOSO
LinkDB: A0A1E2WUN6_9NOSO
Original site: A0A1E2WUN6_9NOSO 
ID   A0A1E2WUN6_9NOSO        Unreviewed;      1461 AA.
AC   A0A1E2WUN6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A4S05_26545 {ECO:0000313|EMBL:ODH01976.1};
OS   Nostoc sp. KVJ20.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=457944 {ECO:0000313|EMBL:ODH01976.1, ECO:0000313|Proteomes:UP000094607};
RN   [1] {ECO:0000313|EMBL:ODH01976.1, ECO:0000313|Proteomes:UP000094607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KVJ20 {ECO:0000313|EMBL:ODH01976.1,
RC   ECO:0000313|Proteomes:UP000094607};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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   -!- 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:ODH01976.1}.
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DR   EMBL; LSSA01000051; ODH01976.1; -; Genomic_DNA.
DR   RefSeq; WP_069072777.1; NZ_KV757671.1.
DR   OrthoDB; 434700at2; -.
DR   Proteomes; UP000094607; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
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; 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; IPR013656; PAS_4.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 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; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 4.
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; 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; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ODH01976.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        267..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          336..379
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          413..462
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          459..531
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          679..731
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1049..1315
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1340..1458
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          575..602
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1389
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1461 AA;  161061 MW;  A2BA2111D7D9A029 CRC64;
     MLNVNRLRLQ DILKIPGNSL VAKVASAIPI LVGSLVLVGW WLGIEVLKRG FPGSPATMKV
     NTALCFVLCG LSLWLFLRTE EQGSSKERII QNYPHNSTAR NAKGGSLNRL TLLISRVCAI
     AVTTIAVLTL CEYVFVWNLG IDELVFRDSP TSIATSHPGR MGVNTALNFM LVSVGVQILI
     HPKTQRSYWY AQILALVATL ISFQALMGYA YKVQVLYGLA PYTTSMALHT AVLFILLSIG
     ILWARAEQGF MRVVTGDTYG GLLARRLLVA AIAVPFVLGW LIVEGQRAEK YGPAFAVSLF
     AIILIVIFTI LVWQSASVIE RLSHQRDLAQ EVVRTYEAKL GSFVDSNVIG ILFGDVYGGI
     HKANDEYLRM IGYTREDLLA GRVSWSNLTA PEYRYLDERG VAEAQGNANA ACTPYEKEYI
     RKDGSRIPVL VGYVLLGENR EESVAFILDL SDRKQAEAEQ QKLVSLVENS SDFIGITTLE
     GQLLYINDAG QKLVGLASLD EARQKAVFDY VMPKDKAYLQ EHILPTVLLQ GRWQGEFGFR
     HLQTGQPIPV DYNIFTVTDK NTGQPIALAT VTRNISEQKQ AKEQILQLNR DLQRRITELQ
     TLLDVIPIGI GIAEDPECQN IKVNPAFAKQ LGISSDTNAS LSAPSDERPT AFKIYREGRE
     LSAEELPMQY SAAHGVEVLD FEIDVIHENG KLVRLLEYVA PLFDEDGKTR GCIGAFLDIT
     ERKQAEEILL NQHKWLENVL NLMPRPLLFI EPGTARVTFA NRSADELAGG EFPKGVPAAE
     YHTVYHYTDA AGDRIPNEQM PGVRVALGER LDGLEIDWHT PTGVHSLLIF ADTLPAMHGH
     PATCILVFQD ISNLKEAQKA LSLGYKRLKL LFDTANDLLS SQQPVILIDS VYRKLADQIG
     LDVYFNYLVE DSSQVIRLGS YSGISPELAK EIESLAYGEA ICGTVAQERC AIALENVQQS
     TDPKTELLRS LGITAYYGYP LIAQGRLLGT LSFGSRTRLS FTENQKGMMQ AVCDQIAIAM
     ERASLIASLQ LQTEQLQEAN RMKDEFLGIL SHELRSPLNA ILGWAQLLQR SKLNETQMAR
     ATETIERNAK AQTQLIEDLL DISRMIRGKL RLNVRTCNLV SMIESSLETV SLAAQSKEID
     LRFSLIPSKE TPNSDCGLGI NGENLESREV QSQSNQHSEN GKLAENPQFL VSGDFERLQQ
     IIWNLLSNAI KFTPTGGRVE VQLSVVSGQE KQQTTDQYAQ IQVIDTGIGI NPDFLPYVFD
     RFCQADSSST RSYGGLGLGL AIVRHLVELH GGTVHADSPG KEQGATFTVK LPLLKSSPLC
     PCAPLPLCPP ASPPSLLGVR VVVVDDQADT REFITTVLEQ CQAEVKAVGS VPEALQVITQ
     WKPDVIVSDI GMPQEDGYSL IRKLRSQPPE LGGNIPAAAL TAYARAEDRM RAIQEGYQLH
     LPKPIEAAEL ATVVASLVGR T
//
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