HIK2_THEVB
ID HIK2_THEVB Reviewed; 385 AA.
AC Q8DMC5;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Sensor histidine kinase Hik2 {ECO:0000303|PubMed:29290041};
DE EC=2.7.13.3;
GN Name=hik2 {ECO:0000303|PubMed:29290041};
GN OrderedLocusNames=tlr0195 {ECO:0000312|EMBL:BAC07748.1};
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP SUBUNIT, AND DOMAIN.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=29290041; DOI=10.1007/s00709-017-1196-7;
RA Ibrahim I.M., Wang L., Puthiyaveetil S., Krauss N., Nield J., Allen J.F.;
RT "Oligomeric states in sodium ion-dependent regulation of cyanobacterial
RT histidine kinase-2.";
RL Protoplasma 255:937-952(2018).
CC -!- FUNCTION: Member of 2 two-component regulatory system(s) Hik2/Rre1 and
CC Hik2/RppA. Transduces PQ (plastoquinone) redox signals to photosystem
CC gene expression machinery during the adjustment of photosystem
CC stoichiometry. Reduced PQ suppresses its autophosphorylation activity
CC (i.e. kinase activity is higher under oxidizing conditions). As part of
CC a two-component regulatory system with Rre1, controls expression of
CC sigB and several other genes in response to hyperosmotic stress. May
CC transfer phosphate to RppA in a possible Hik2/RppA two-component
CC system. {ECO:0000250|UniProtKB:P73276}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P73276};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000250|UniProtKB:P73276};
CC Note=The 3Fe-4S cluster is redox-responsive, binds 1 cluster per
CC monomer. {ECO:0000250|UniProtKB:P73276};
CC -!- SUBUNIT: Hexamers; upon treatment with 0.5 M NaCl only tetramers are
CC seen. The tetramers are probably inactive.
CC {ECO:0000269|PubMed:29290041}.
CC -!- DOMAIN: Oligomerization seems to be mediated by the histidine kinase
CC domain (residues 142-386) which forms tetramers and hexamers. The DHp
CC subdomain (dimerization and phosphotransfer, residues 142-270) forms
CC hexamers and octamers. NaCl treatment reduces the histidine kinase
CC domain to tetramers and the DHp domain to hexamers, suggests the DHp
CC domain senses NaCl. {ECO:0000269|PubMed:29290041}.
CC -!- PTM: Autophosphorylates, possibly on His-161.
CC {ECO:0000250|UniProtKB:P73276}.
CC -!- SIMILARITY: Belongs to the chloroplast sensor kinase protein family.
CC {ECO:0000305}.
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DR EMBL; BA000039; BAC07748.1; -; Genomic_DNA.
DR RefSeq; NP_680986.1; NC_004113.1.
DR RefSeq; WP_011056050.1; NC_004113.1.
DR AlphaFoldDB; Q8DMC5; -.
DR SMR; Q8DMC5; -.
DR STRING; 197221.22293916; -.
DR EnsemblBacteria; BAC07748; BAC07748; BAC07748.
DR KEGG; tel:tlr0195; -.
DR eggNOG; COG2205; Bacteria.
DR OMA; PNRRWYP; -.
DR OrthoDB; 1827824at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3Fe-4S; Iron; Iron-sulfur; Kinase; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Two-component regulatory system.
FT CHAIN 1..385
FT /note="Sensor histidine kinase Hik2"
FT /id="PRO_0000453141"
FT DOMAIN 11..131
FT /note="GAF"
FT /evidence="ECO:0000255"
FT DOMAIN 158..381
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 142..270
FT /note="DHp domain, may sense NaCl"
FT /evidence="ECO:0000305|PubMed:29290041"
FT BINDING 13
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P73276"
FT MOD_RES 161
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 385 AA; 42417 MW; E5CECA7FBC275E6B CRC64;
MLWPASEEFA ALCRTQLELV VNSLGASSLA VYLSETLNDS PSWSPVAVYP EAASLLSLAI
PPTLPPPTQV PETSLSHYPQ QVVSSLANQL ILPLMYQNWV LGVLVAQRQH RPWLAAEQAQ
LQQVAQTLAI ACVLDQRQQW LSHSPAQPLD QRQQRFDDLL HQLRNPVAAI RTFVKLLLKR
LEPDHKGRPL AEGIAKETER LMALLEDYRQ QRNDIPALTG SQPLPLAGKP LDLAETLLPL
ISAAQARAEM EGKTFVVEIP PQLPPIWLEE RVLQEVVGNL LDNAFKYTPK GGTIGLRLML
SSPALELTVW DTGCGIPKEA QPRLFERGYR GVQADSGIEG SGLGLAIAQD LLRPYGLSLR
VTSPYAGDRG TAFTLAIPWQ MKVEP
