HIK2_SYNY3
ID HIK2_SYNY3 Reviewed; 434 AA.
AC P73276;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sensor histidine kinase Hik2 {ECO:0000303|PubMed:15471853};
DE EC=2.7.13.3 {ECO:0000269|PubMed:25714549, ECO:0000269|PubMed:26904089};
DE AltName: Full=CSK {ECO:0000303|PubMed:31925322};
GN Name=hik2 {ECO:0000303|PubMed:15471853};
GN OrderedLocusNames=slr1147 {ECO:0000312|EMBL:BAA17304.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION IN HYPEROSMOTIC STRESS RESPONSE, REGULON, PROBABLE SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=15471853; DOI=10.1074/jbc.m410162200;
RA Paithoonrangsarid K., Shoumskaya M.A., Kanesaki Y., Satoh S., Tabata S.,
RA Los D.A., Zinchenko V.V., Hayashi H., Tanticharoen M., Suzuki I.,
RA Murata N.;
RT "Five histidine kinases perceive osmotic stress and regulate distinct sets
RT of genes in Synechocystis.";
RL J. Biol. Chem. 279:53078-53086(2004).
RN [3]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF GLN-22; PRO-114; GLY-123; ARG-129;
RP TRP-134; GLN-141 AND ASP-156.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=24283389; DOI=10.1111/1574-6968.12346;
RA Kotajima T., Shiraiwa Y., Suzuki I.;
RT "Functional analysis of the N-terminal region of an essential histidine
RT kinase, Hik2, in the cyanobacterium Synechocystis sp. PCC 6803.";
RL FEMS Microbiol. Lett. 351:88-94(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=25714549; DOI=10.1093/femsle/fnv030;
RA Vidal R.;
RT "Identification of the correct form of the mis-annotated response regulator
RT Rre1 from the cyanobacterium Synechocystis sp. PCC 6803.";
RL FEMS Microbiol. Lett. 362:0-0(2015).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH RPPA
RP AND RRE1, AUTOPHOSPHORYLATION, DOMAIN, PHOSPHORYLATION AT HIS-185, AND
RP MUTAGENESIS OF HIS-185; GLY-359; GLY-361; GLY-386; GLY-388 AND GLY-390.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=26904089; DOI=10.3389/fpls.2016.00137;
RA Ibrahim I.M., Puthiyaveetil S., Allen J.F.;
RT "A Two-Component Regulatory System in Transcriptional Control of
RT Photosystem Stoichiometry: Redox-Dependent and Sodium Ion-Dependent
RT Phosphoryl Transfer from Cyanobacterial Histidine Kinase Hik2 to Response
RT Regulators Rre1 and RppA.";
RL Front. Plant Sci. 7:137-137(2016).
RN [6]
RP SUBUNIT, AND AUTOPHOSPHORYLATION.
RC STRAIN=PCC 6803 / Kazusa;
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).
RN [7]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP CYS-19; CYS-35 AND CYS-153.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=31925322; DOI=10.1038/s42003-019-0728-4;
RA Ibrahim I.M., Wu H., Ezhov R., Kayanja G.E., Zakharov S.D., Du Y.,
RA Tao W.A., Pushkar Y., Cramer W.A., Puthiyaveetil S.;
RT "An evolutionarily conserved iron-sulfur cluster underlies redox sensory
RT function of the Chloroplast Sensor Kinase.";
RL Commun. Biol. 3:13-13(2020).
CC -!- FUNCTION: Member of possibly 2 two-component regulatory system(s)
CC Hik2/Rre1 and Hik2/RppA. Transduces PQ (plastoquinone) redox signals to
CC photosystem gene expression machinery during the adjustment of
CC photosystem stoichiometry. Reduced PQ suppresses its
CC autophosphorylation activity (i.e. kinase activity is higher under
CC oxidizing conditions) (Probable). Member of two-component regulatory
CC system Hik2/Rre1, controls expression of sigB (sll0306), sll0528,
CC slr1119, slr0852 and ssr3188 in response to hyperosmotic stress
CC (Probable). Activity responds to high salt (with a linear response as
CC concentrations rise to 0.5 M NaCl); detects Cl(-) levels
CC (PubMed:24283389). Autophosphorylates and transfers phosphate to Rre1
CC (PubMed:25714549, PubMed:26904089). May transfer phosphate to RppA in a
CC possible Hik2/RppA two-component system (Probable).
CC {ECO:0000269|PubMed:24283389, ECO:0000269|PubMed:25714549,
CC ECO:0000269|PubMed:26904089, ECO:0000305|PubMed:15471853,
CC ECO:0000305|PubMed:26904089, ECO:0000305|PubMed:31925322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:25714549,
CC ECO:0000269|PubMed:26904089};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000269|PubMed:31925322};
CC Note=The 3Fe-4S cluster is redox-responsive, binds 1 cluster per
CC monomer. It is coordinated by Cys-19 and other non-Cys residues.
CC {ECO:0000269|PubMed:31925322};
CC -!- ACTIVITY REGULATION: Autophosphorylation is inhibited by Na(+) but not
CC by Cl(-) (PubMed:26904089). Reducing agents dithionite, duroquinol and
CC decyl-plastoquinone, but not NADPH or ferredoxin inhibit
CC autophosphorylation. Oxidation of the Fe-S cluster (with potassium
CC ferricyanide) induces a conformational change that is conducive to its
CC autophosphorylation activity (PubMed:31925322).
CC {ECO:0000269|PubMed:26904089, ECO:0000269|PubMed:31925322}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -15 mV. {ECO:0000269|PubMed:31925322};
CC -!- SUBUNIT: Exists as monomers, tetramers, hexamers and other higher-order
CC oligomers; all are able to autophosphorylate. Upon treatment with 0.5 M
CC NaCl only tetramers are seen, which are probably inactive
CC (PubMed:29290041). Interacts with both RppA and Rre1 (PubMed:26904089).
CC {ECO:0000269|PubMed:26904089, ECO:0000269|PubMed:29290041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15471853}.
CC -!- DOMAIN: The N-terminal GAF domain activated by Cl(-).
CC {ECO:0000269|PubMed:24283389}.
CC -!- PTM: Autophosphorylates, probably on His-185.
CC {ECO:0000269|PubMed:25714549, ECO:0000269|PubMed:26904089,
CC ECO:0000269|PubMed:29290041, ECO:0000269|PubMed:31925322}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:15471853}.
CC -!- SIMILARITY: Belongs to the chloroplast sensor kinase protein family.
CC {ECO:0000305|PubMed:31925322}.
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DR EMBL; BA000022; BAA17304.1; -; Genomic_DNA.
DR PIR; S77457; S77457.
DR AlphaFoldDB; P73276; -.
DR SMR; P73276; -.
DR IntAct; P73276; 5.
DR STRING; 1148.1652382; -.
DR PaxDb; P73276; -.
DR EnsemblBacteria; BAA17304; BAA17304; BAA17304.
DR KEGG; syn:slr1147; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR InParanoid; P73276; -.
DR OMA; PNRRWYP; -.
DR PhylomeDB; P73276; -.
DR BRENDA; 2.7.13.3; 382.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
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; Cytoplasm; Iron; Iron-sulfur; Kinase; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..434
FT /note="Sensor histidine kinase Hik2"
FT /id="PRO_0000453140"
FT DOMAIN 16..152
FT /note="GAF"
FT /evidence="ECO:0000255"
FT DOMAIN 182..432
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOTIF 357..361
FT /note="G1 box"
FT /evidence="ECO:0000305|PubMed:26904089"
FT MOTIF 386..390
FT /note="G2 box"
FT /evidence="ECO:0000305|PubMed:26904089"
FT BINDING 19
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000305|PubMed:31925322"
FT MOD_RES 185
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000305|PubMed:26904089"
FT MUTAGEN 19
FT /note="C->S: Binds less Fe(2+) and S(2-)."
FT /evidence="ECO:0000269|PubMed:31925322"
FT MUTAGEN 22
FT /note="Q->E: Loss of Cl(-) response."
FT /evidence="ECO:0000269|PubMed:24283389"
FT MUTAGEN 35
FT /note="C->S: Binds less Fe(2+)."
FT /evidence="ECO:0000269|PubMed:31925322"
FT MUTAGEN 114
FT /note="P->A: Loss of Cl(-) response."
FT /evidence="ECO:0000269|PubMed:24283389"
FT MUTAGEN 123
FT /note="G->A: Loss of Cl(-) response."
FT /evidence="ECO:0000269|PubMed:24283389"
FT MUTAGEN 129
FT /note="R->K: Loss of Cl(-) response."
FT /evidence="ECO:0000269|PubMed:24283389"
FT MUTAGEN 134
FT /note="W->F: Loss of Cl(-) response."
FT /evidence="ECO:0000269|PubMed:24283389"
FT MUTAGEN 141
FT /note="Q->A: Loss of Cl(-) response."
FT /evidence="ECO:0000269|PubMed:24283389"
FT MUTAGEN 153
FT /note="C->S: Binds less S(2-)."
FT /evidence="ECO:0000269|PubMed:31925322"
FT MUTAGEN 156
FT /note="D->A: Loss of Cl(-) response."
FT /evidence="ECO:0000269|PubMed:24283389"
FT MUTAGEN 185
FT /note="H->Q: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:26904089"
FT MUTAGEN 359
FT /note="G->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:26904089"
FT MUTAGEN 361
FT /note="G->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:26904089"
FT MUTAGEN 386
FT /note="G->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:26904089"
FT MUTAGEN 388
FT /note="G->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:26904089"
FT MUTAGEN 390
FT /note="G->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:26904089"
SQ SEQUENCE 434 AA; 47575 MW; C456BAA9F3F216EF CRC64;
MAGSISSMYS PSAGLISLCQ SQVRLLQQGL RVDWCGVYLN QEETEQGLVP LVVSHGSTLV
ESESYGLISL PQGEVSPPMD DFSLPAVPVG VGQLSRRSRL EPPPFDADKR LVLPLVYGEE
MVGLLVIHRS QGQWHGEEMM QLEAIAKSLA VACLLDQQQD WYRQAWEEQN QQYQWERQHW
ADLLHQLRNP LTALKTFSKL LLKRWHGDNK SQQVVEGIVR QGEHLQELLQ SFEASQSQGP
EAVPLLSSSP VTTIQVLPPA DRVETMPLAN FSLGEVLPPI LLAHQAIAAE RNITLTAQIA
LIDTVVMANR LALREVVNNL LDNGIKYTPN GGLVEVSLAL EKVSSSGMDW ATLAIADTGY
GIPPEDQQKI FERNYRGVQG RGSINGTGLG LAIVADLVAQ MGGKITVTSP NGLSRDPDQP
GSTFTLWLRS GEQV
