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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//