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Database: UniProt
Entry: A0A2R5FF82_NOSCO
LinkDB: A0A2R5FF82_NOSCO
Original site: A0A2R5FF82_NOSCO 
ID   A0A2R5FF82_NOSCO        Unreviewed;       728 AA.
AC   A0A2R5FF82;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=NIES4072_07990 {ECO:0000313|EMBL:GBG17150.1};
OS   Nostoc commune NIES-4072.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=2005467 {ECO:0000313|EMBL:GBG17150.1, ECO:0000313|Proteomes:UP000245124};
RN   [1] {ECO:0000313|EMBL:GBG17150.1, ECO:0000313|Proteomes:UP000245124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4072 {ECO:0000313|EMBL:GBG17150.1,
RC   ECO:0000313|Proteomes:UP000245124};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) 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:GBG17150.1}.
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DR   EMBL; BDUD01000001; GBG17150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R5FF82; -.
DR   OrthoDB; 2079555at2; -.
DR   Proteomes; UP000245124; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd00731; CheA_reg; 1.
DR   CDD; cd16916; HATPase_CheA-like; 1.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 2.40.50.180; CheA-289, Domain 4; 1.
DR   Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR004105; CheA-like_dim.
DR   InterPro; IPR037006; CheA-like_homodim_sf.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01584; CheW; 2.
DR   Pfam; PF02895; H-kinase_dim; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM01231; H-kinase_dim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 2.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50851; CHEW; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:GBG17150.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245124};
KW   Transferase {ECO:0000313|EMBL:GBG17150.1}.
FT   DOMAIN          2..106
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          218..422
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          424..558
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   DOMAIN          580..719
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          136..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   728 AA;  79620 MW;  52354BC91EA66586 CRC64;
     MELNEIDDDI EAFLVESYEN LNQIEGDIIE LEKTSANGEA LVRIYRSLHT LKGNCGFLPF
     PNLESLAHAG ENLLSCLRDR TIAITPDIIS ILLQTVDGIR QILSQIQATK QDGNRNYSAL
     IATLTRLSEA KQTLKPSQSL VNTQTPQIDA EAPDTAGSDV NNELTEISTT TSESAYIRVN
     VNLLDQMMNL VGELVLARNQ VIGFSTKFKD NSFTATCQHL SQLTAELQEE VMKTRLQPIS
     SIWQKFPRVT RDLAIASGKE VKVEMEGADT ELDKSIIETI KDPLTHLVRN CIDHGIELPA
     ERVACGKPSL GRLFLKAFHE SGKVNIEIGD DGRGLNLEQL KGRAQQLGLV NAVQAATMSQ
     SEAMDLIFLS GFSTAEQVTH LSGRGVGMDI VKSNIEKING TIEIYSQQGQ GTTFKIKIPL
     TLAIIPALIV TSGGDCYAIP QASLQELVRL ETLNSIEILY DVPVYRLRGN LVPLIYLNEV
     LQQDSVSNLE TLSLVIVQVD NYSFGLVVDT IEDIQDIVVK PLGKQLKMLS LFAGATVLGD
     GTVALIIDVV GLANRTGIIA KQKQLLNENA ANSQEQAGDR QTILLFEGPQ GARMGIPLAI
     AYRLEEIFAS AVEKVANQNV YQSYGQILPL IDLYKIFGVG DRFNDEALAT VAETLQIIIV
     SPYPELSVGL VVDRILDIVE EPLTIKGIPS RPGVLFCAVI QGQITEIIDI ETVIRIANPY
     LLQLATHG
//
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