ID SASA_SYNE7 Reviewed; 387 AA.
AC Q06904; Q31LC5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=Adaptive-response sensory kinase SasA {ECO:0000255|HAMAP-Rule:MF_01837, ECO:0000303|PubMed:8370532};
DE EC=2.7.13.3 {ECO:0000255|HAMAP-Rule:MF_01837, ECO:0000305|PubMed:16882723, ECO:0000305|PubMed:34618577};
DE AltName: Full=Sensor histidine kinase SasA {ECO:0000255|HAMAP-Rule:MF_01837, ECO:0000303|PubMed:10786837};
DE AltName: Full=Synechococcus adaptive sensor protein A {ECO:0000303|PubMed:8370532};
DE Short=SasA {ECO:0000303|PubMed:8370532};
GN Name=sasA {ECO:0000255|HAMAP-Rule:MF_01837, ECO:0000303|PubMed:10786837};
GN Synonyms=sarS {ECO:0000303|PubMed:8370532};
GN OrderedLocusNames=Synpcc7942_2114;
OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1140;
RN [1] {ECO:0000312|EMBL:BAA03145.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND AUTOPHOSPHORYLATION.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=8370532; DOI=10.1016/0378-1119(93)90679-w;
RA Nagaya M., Aiba H., Mizuno T.;
RT "Cloning of a sensory-kinase-encoding gene that belongs to the two-
RT component regulatory family from the cyanobacterium Synechococcus sp.
RT PCC7942.";
RL Gene 131:119-124(1993).
RN [2] {ECO:0000312|EMBL:ABB58144.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Golden S., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH KAIC, SUBUNIT, INDUCTION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF HIS-161.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=10786837; DOI=10.1016/s0092-8674(00)80832-6;
RA Iwasaki H., Williams S.B., Kitayama Y., Ishiura M., Golden S.S., Kondo T.;
RT "A kaiC-interacting sensory histidine kinase, SasA, necessary to sustain
RT robust circadian oscillation in cyanobacteria.";
RL Cell 101:223-233(2000).
RN [4]
RP SUBUNIT.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=15347812; DOI=10.1073/pnas.0403906101;
RA Nishiwaki T., Satomi Y., Nakajima M., Lee C., Kiyohara R., Kageyama H.,
RA Kitayama Y., Temamoto M., Yamaguchi A., Hijikata A., Go M., Iwasaki H.,
RA Takao T., Kondo T.;
RT "Role of KaiC phosphorylation in the circadian clock system of
RT Synechococcus elongatus PCC 7942.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13927-13932(2004).
RN [5]
RP INTERACTION WITH LDPA, AND SUBUNIT.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=15775978; DOI=10.1038/sj.emboj.7600606;
RA Ivleva N.B., Bramlett M.R., Lindahl P.A., Golden S.S.;
RT "LdpA: a component of the circadian clock senses redox state of the cell.";
RL EMBO J. 24:1202-1210(2005).
RN [6]
RP AUTOPHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=16707582; DOI=10.1073/pnas.0508696103;
RA Smith R.M., Williams S.B.;
RT "Circadian rhythms in gene transcription imparted by chromosome compaction
RT in the cyanobacterium Synechococcus elongatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8564-8569(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=16882723; DOI=10.1073/pnas.0602955103;
RA Takai N., Nakajima M., Oyama T., Kito R., Sugita C., Sugita M., Kondo T.,
RA Iwasaki H.;
RT "A KaiC-associating SasA-RpaA two-component regulatory system as a major
RT circadian timing mediator in cyanobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12109-12114(2006).
RN [8]
RP FUNCTION IN OUTPUT PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=20133618; DOI=10.1073/pnas.0909924107;
RA Taniguchi Y., Takai N., Katayama M., Kondo T., Oyama T.;
RT "Three major output pathways from the KaiABC-based oscillator cooperate to
RT generate robust circadian kaiBC expression in cyanobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3263-3268(2010).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-161.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=22512339; DOI=10.1111/j.1365-2443.2012.01597.x;
RA Valencia S.J., Bitou K., Ishii K., Murakami R., Morishita M., Onai K.,
RA Furukawa Y., Imada K., Namba K., Ishiura M.;
RT "Phase-dependent generation and transmission of time information by the
RT KaiABC circadian clock oscillator through SasA-KaiC interaction in
RT cyanobacteria.";
RL Genes Cells 17:398-419(2012).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=23541768; DOI=10.1016/j.molcel.2013.02.022;
RA Gutu A., O'Shea E.K.;
RT "Two antagonistic clock-regulated histidine kinases time the activation of
RT circadian gene expression.";
RL Mol. Cell 50:288-294(2013).
RN [11]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=26113641; DOI=10.1126/science.1260031;
RA Chang Y.G., Cohen S.E., Phong C., Myers W.K., Kim Y.I., Tseng R., Lin J.,
RA Zhang L., Boyd J.S., Lee Y., Kang S., Lee D., Li S., Britt R.D., Rust M.J.,
RA Golden S.S., LiWang A.;
RT "Circadian rhythms. A protein fold switch joins the circadian oscillator to
RT clock output in cyanobacteria.";
RL Science 349:324-328(2015).
RN [12]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=28302851; DOI=10.1126/science.aag2516;
RA Tseng R., Goularte N.F., Chavan A., Luu J., Cohen S.E., Chang Y.G.,
RA Heisler J., Li S., Michael A.K., Tripathi S., Golden S.S., LiWang A.,
RA Partch C.L.;
RT "Structural basis of the day-night transition in a bacterial circadian
RT clock.";
RL Science 355:1174-1180(2017).
RN [13]
RP CLOCK RECONSTITUTION, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP MUTAGENESIS OF HIS-28; GLN-94 AND HIS-161.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=34618577; DOI=10.1126/science.abd4453;
RA Chavan A.G., Swan J.A., Heisler J., Sancar C., Ernst D.C., Fang M.,
RA Palacios J.G., Spangler R.K., Bagshaw C.R., Tripathi S., Crosby P.,
RA Golden S.S., Partch C.L., LiWang A.;
RT "Reconstitution of an intact clock reveals mechanisms of circadian
RT timekeeping.";
RL Science 374:eabd4453-eabd4453(2021).
RN [14] {ECO:0007744|PDB:1T4Y, ECO:0007744|PDB:1T4Z}
RP STRUCTURE BY NMR OF 4-103.
RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
RX PubMed=15313603; DOI=10.1016/j.jmb.2004.07.010;
RA Vakonakis I., Klewer D.A., Williams S.B., Golden S.S., LiWang A.C.;
RT "Structure of the N-terminal domain of the circadian clock-associated
RT histidine kinase SasA.";
RL J. Mol. Biol. 342:9-17(2004).
CC -!- FUNCTION: Member of the two-component regulatory system SasA/RpaA
CC involved in genome-wide circadian gene expression (PubMed:16882723).
CC One of three clock output pathways. Participates in the KaiABC clock
CC protein complex, which constitutes the main circadian regulator in
CC cyanobacteria, via its interaction with KaiC. Required for robustness
CC of the circadian rhythm of gene expression and involved in clock output
CC (PubMed:10786837, PubMed:20133618, PubMed:34618577). KaiC enhances the
CC autophosphorylation activity of SasA, which then transfers its
CC phosphate group to RpaA to activate it. Phosphotransfer is maximal when
CC KaiC phosphorylation is active during the circadian cycle; this two-
CC component system is activated by fully phosphorylated KaiC
CC (PubMed:16882723, PubMed:16707582, PubMed:23541768, PubMed:26113641,
CC PubMed:34618577). A very robust clock is reconstituted with KaiA, KaiB,
CC KaiC, SasA, CikA and RpaA; output is measured by transcription from an
CC appropriate reporter (PubMed:34618577). In addition to its output
CC function, recruits fold-shifted KaiB (KaiB(fs)) to KaiC to
CC cooperatively form the KaiB(6):KaiC(6) complex (independent of SasA
CC kinase activity); at physiological concentrations increases their
CC association. At higher concentrations SasA and KaiB(fs) compete to bind
CC to KaiC. Mutations that decrease cooperativity nearly phenocopy a
CC deletion mutation (PubMed:34618577). {ECO:0000269|PubMed:10786837,
CC ECO:0000269|PubMed:16707582, ECO:0000269|PubMed:16882723,
CC ECO:0000269|PubMed:20133618, ECO:0000269|PubMed:23541768,
CC ECO:0000269|PubMed:26113641, ECO:0000269|PubMed:34618577}.
CC -!- FUNCTION: Autophosphorylation and phosphotransfer activities are not
CC essential for clock rhythms in continuous light, but they are essential
CC for adaptation to light/dark cycles. {ECO:0000269|PubMed:22512339}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01837,
CC ECO:0000305|PubMed:16882723, ECO:0000305|PubMed:34618577};
CC -!- SUBUNIT: Homooligomerizes (By similarity). Part of the circadian clock
CC (KaiA, KaiB, KaiC, CikA, RpaA, SasA), the composition of which varies
CC during the circadian cycle (PubMed:10786837, PubMed:15347812,
CC PubMed:26113641, PubMed:28302851, PubMed:34618577). Binds to the CI
CC domain of KaiC; KaiB(fs) and SasA compete for the binding site
CC (PubMed:10786837, PubMed:15347812, PubMed:26113641, PubMed:28302851,
CC PubMed:34618577). Binds preferentially to doubly phosphorylated KaiC
CC (PubMed:34618577). Interacts with LdpA (PubMed:15775978).
CC {ECO:0000250|UniProtKB:Q8DMT2, ECO:0000269|PubMed:10786837,
CC ECO:0000269|PubMed:15347812, ECO:0000269|PubMed:15775978,
CC ECO:0000269|PubMed:26113641, ECO:0000269|PubMed:28302851,
CC ECO:0000269|PubMed:34618577}.
CC -!- INTERACTION:
CC Q06904; Q79PF4: kaiC; NbExp=6; IntAct=EBI-626872, EBI-592287;
CC -!- INDUCTION: Transcribed in a circadian pattern, protein accumulates in
CC light (at protein level). {ECO:0000269|PubMed:10786837}.
CC -!- DOMAIN: The N-terminus interacts with KaiC, while the C-terminal
CC histidine kinase domain autophosphorylates and is probably responsible
CC for self-oligomerization. The N-terminal domain stimulates the C-
CC terminus to autophosphorylate. {ECO:0000255|HAMAP-Rule:MF_01837}.
CC -!- PTM: Autophosphorylates in vitro. {ECO:0000269|PubMed:16882723,
CC ECO:0000269|PubMed:8370532}.
CC -!- DISRUPTION PHENOTYPE: No growth phenotype in low, continuous light,
CC dysregulation of expression of many genes. In a light/dark regime cells
CC grow very slowly (PubMed:10786837, PubMed:20133618, PubMed:22512339).
CC At medium light lowers kaiA and kaiBC expression, attenuating but not
CC destroying circadian rhythms and affecting the expression of many genes
CC (clock output) (PubMed:10786837, PubMed:20133618). Chromosome
CC compaction remains rhythmic (PubMed:16707582). Loss of circadian
CC control of gene expression; KaiA protein levels are unaffected, KaiC is
CC constitutively phosphorylated (PubMed:16882723). Phospho-RpaA is barely
CC detected (PubMed:23541768). {ECO:0000269|PubMed:10786837,
CC ECO:0000269|PubMed:16707582, ECO:0000269|PubMed:16882723,
CC ECO:0000269|PubMed:20133618, ECO:0000269|PubMed:22512339,
CC ECO:0000269|PubMed:23541768}.
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DR EMBL; D14056; BAA03145.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58144.1; -; Genomic_DNA.
DR PIR; JN0793; JN0793.
DR RefSeq; WP_011378322.1; NZ_JACJTX010000001.1.
DR PDB; 1T4Y; NMR; -; A=4-103.
DR PDB; 1T4Z; NMR; -; A=4-103.
DR PDBsum; 1T4Y; -.
DR PDBsum; 1T4Z; -.
DR AlphaFoldDB; Q06904; -.
DR BMRB; Q06904; -.
DR SMR; Q06904; -.
DR IntAct; Q06904; 3.
DR STRING; 1140.Synpcc7942_2114; -.
DR PaxDb; 1140-Synpcc7942_2114; -.
DR GeneID; 76400842; -.
DR KEGG; syf:Synpcc7942_2114; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_723030_0_0_3; -.
DR OrthoDB; 9773956at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2114-MONOMER; -.
DR EvolutionaryTrace; Q06904; -.
DR Proteomes; UP000889800; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IMP:CACAO.
DR GO; GO:0097167; P:circadian regulation of translation; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd02978; KaiB_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_01837; Kinase_SasA; 1.
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; IPR011649; KaiB_domain.
DR InterPro; IPR023527; Kinase_SasA.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF07689; KaiB; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM01248; KaiB; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biological rhythms; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..387
FT /note="Adaptive-response sensory kinase SasA"
FT /id="PRO_0000074872"
FT DOMAIN 158..382
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
FT REGION 1..97
FT /note="Interacts with KaiC"
FT /evidence="ECO:0000269|PubMed:10786837"
FT MOD_RES 161
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
FT MUTAGEN 28
FT /note="H->A: Decreases KaiB-KaiC complex cooperativity.
FT More severe decrease; when associated with A-94, double
FT mutant binds KaiC and phosphorylates RpaA."
FT /evidence="ECO:0000269|PubMed:34618577"
FT MUTAGEN 94
FT /note="Q->A: Decreases KaiB-KaiC complex cooperativity.
FT More severe decrease; when associated with A-28, double
FT mutant binds KaiC and phosphorylates RpaA."
FT /evidence="ECO:0000269|PubMed:34618577"
FT MUTAGEN 161
FT /note="H->A: No change in stimulation of KaiB-KaiC complex
FT cooperativity, probably catalytically inactive. Period
FT length increases by 2 hours, impaired growth in light/dark
FT cycle at 30 and 42 umol/m(2)/sec photons."
FT /evidence="ECO:0000269|PubMed:22512339,
FT ECO:0000269|PubMed:34618577"
FT MUTAGEN 161
FT /note="H->D,E: Period length increases by 2 hours, impaired
FT growth in light/dark cycle at 30 and 42 umol/m(2)/sec
FT photons."
FT /evidence="ECO:0000269|PubMed:22512339"
FT MUTAGEN 161
FT /note="H->Q: Lowers the amplitude of circadian rhythm,
FT similar to disruption."
FT /evidence="ECO:0000269|PubMed:10786837"
FT CONFLICT 135
FT /note="F -> L (in Ref. 1; BAA03145)"
FT /evidence="ECO:0000305"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1T4Y"
FT HELIX 24..40
FT /evidence="ECO:0007829|PDB:1T4Y"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1T4Y"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1T4Y"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:1T4Y"
FT STRAND 67..78
FT /evidence="ECO:0007829|PDB:1T4Y"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1T4Y"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:1T4Y"
SQ SEQUENCE 387 AA; 43315 MW; 04A0A097C3EE0438 CRC64;
MGESLSPQAL AQPLLLQLFV DTRPLSQHIV QRVKNILAAV EATVPISLQV INVADQPQLV
EYYRLVVTPA LVKIGPGSRQ VLSGIDLTDQ LANQLPQWLV QQEAFFADRE PPEVNIPFTE
LGQPETPALQ QADAFFQLQQ QYADLSERTK FLEQVIALVA HDLRNPLTAA LLAVDTIQIR
SQSFSVATAK EMQGLCSLFD QARSQLREIE RMIAEILEAT RHSGESLRIN PREVVFEPLL
QQVLEQLHER WRSKQQQLIT DVPGDLPTLY ADPDRLRQVL VNLLDNAIKY TPPGGTITIA
ALHRTSQKVQ ISISDTGSGI PRDQLSVIFK NLVRLSRDSS QEGYGIGLSV CQRIVQAHFG
RIWVASELGQ GSTFHFTMPV YRYTMPC
//