ID   SASA_SYNY3              Reviewed;         383 AA.
AC   Q55630;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Adaptive-response sensory kinase SasA {ECO:0000255|HAMAP-Rule:MF_01837};
DE            EC=2.7.13.3 {ECO:0000255|HAMAP-Rule:MF_01837};
DE   AltName: Full=Sensor histidine kinase Hik8 {ECO:0000303|PubMed:15774880};
DE   AltName: Full=Sensor histidine kinase SasA {ECO:0000255|HAMAP-Rule:MF_01837, ECO:0000303|PubMed:30216574};
GN   Name=sasA {ECO:0000255|HAMAP-Rule:MF_01837};
GN   Synonyms=hik8 {ECO:0000303|PubMed:15774880}, sarA
GN   {ECO:0000303|PubMed:8590279}; OrderedLocusNames=sll0750;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1] {ECO:0000312|EMBL:BAA10143.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
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   [3]
RP   FUNCTION, REGULON, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=15774880; DOI=10.1128/jb.187.7.2368-2376.2005;
RA   Singh A.K., Sherman L.A.;
RT   "Pleiotropic effect of a histidine kinase on carbohydrate metabolism in
RT   Synechocystis sp. strain PCC 6803 and its requirement for heterotrophic
RT   growth.";
RL   J. Bacteriol. 187:2368-2376(2005).
RN   [4]
RP   OVEREXPRESSION, FUNCTION, INTERACTION WITH KAIC1, AND INDUCTION.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=25403325; DOI=10.1111/1462-2920.12715;
RA   Osanai T., Shirai T., Iijima H., Kuwahara A., Suzuki I., Kondo A.,
RA   Hirai M.Y.;
RT   "Alteration of cyanobacterial sugar and amino acid metabolism by
RT   overexpression hik8, encoding a KaiC-associated histidine kinase.";
RL   Environ. Microbiol. 17:2430-2440(2015).
RN   [5]
RP   INTERACTION WITH KAIC1 AND RPAA.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=30216574; DOI=10.1111/mmi.14129;
RA   Koebler C., Schultz S.J., Kopp D., Voigt K., Wilde A.;
RT   "The role of the Synechocystis sp. PCC 6803 homolog of the circadian clock
RT   output regulator RpaA in day-night transitions.";
RL   Mol. Microbiol. 110:847-861(2018).
CC   -!- FUNCTION: Member of the two-component regulatory system SasA/RpaA
CC       involved in genome-wide circadian gene expression. One of several clock
CC       output pathways. Participates in the Kai clock protein complex, the
CC       main circadian regulator in cyanobacteria, via its interaction with
CC       KaiC. KaiC enhances the autophosphorylation activity of SasA, which
CC       then transfers its phosphate group to RpaA to activate it. In addition
CC       to its output function, recruits fold-shifted KaiB (KaiB(fs)) to KaiC
CC       to cooperatively form the KaiB(6):KaiC(6) complex (independent of SasA
CC       kinase activity). Required for robustness of the circadian rhythm of
CC       gene expression and is involved in clock output, also required for
CC       adaptation to light/dark cycles. {ECO:0000255|HAMAP-Rule:MF_01837}.
CC   -!- FUNCTION: Plays an important role in glucose metabolism, important for
CC       expression of genes involved in glycolysis, gluconeogenesis, the
CC       oxidative pentose phosphate pathway, and glycogen metabolism. Required
CC       for heterotrophic growth (PubMed:15774880). Overexpression from the
CC       psbAII promoter leads to altered levels of genes involved in carbon
CC       metabolism, increased levels of transcripts for clock oscillator genes
CC       in the light and the dark, complete loss of glycogen accumulation,
CC       decreased levels of metabolites of sugar catabolism and increased
CC       levels of amino acids in the light and increased levels of SigE protein
CC       (PubMed:25403325). {ECO:0000269|PubMed:15774880,
CC       ECO:0000269|PubMed:25403325}.
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   -!- SUBUNIT: Homooligomerizes (By similarity). Interacts with KaiC1
CC       (PubMed:25403325, PubMed:30216574). Interacts with KaiC1 and RpaA
CC       (PubMed:30216574). Binds to the B-loop in the CI domain of KaiC; SasA
CC       and KaiB compete to bind to the CI domain (By similarity).
CC       {ECO:0000250|UniProtKB:Q8DMT2, ECO:0000269|PubMed:25403325,
CC       ECO:0000269|PubMed:30216574}.
CC   -!- INDUCTION: Expressed at the same levels in light and dark (at protein
CC       level). {ECO:0000269|PubMed:25403325}.
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   -!- DISRUPTION PHENOTYPE: Deficiency in glucose utilization and/or glucose
CC       intolerance in the absence of light; no longer grows if less than 6/24
CC       hours of light is furnished during mixotrophic (MT) growth on glucose,
CC       no heterotrophic growth (in complete darkness). Accumulates glycogen
CC       under MT growth, but seems unable to utilize it. No expression of
CC       phytochrome or its response regulator (cph1 and rcp1).
CC       {ECO:0000269|PubMed:15774880}.
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DR   EMBL; BA000022; BAA10143.1; -; Genomic_DNA.
DR   PIR; S76291; S76291.
DR   AlphaFoldDB; Q55630; -.
DR   SMR; Q55630; -.
DR   IntAct; Q55630; 9.
DR   STRING; 1148.gene:10499636; -.
DR   PaxDb; 1148-1001516; -.
DR   EnsemblBacteria; BAA10143; BAA10143; BAA10143.
DR   KEGG; syn:sll0750; -.
DR   eggNOG; COG2205; Bacteria.
DR   InParanoid; Q55630; -.
DR   PhylomeDB; Q55630; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0097167; P:circadian regulation of translation; IMP:UniProtKB.
DR   GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
DR   CDD; cd00075; HATPase; 1.
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   ATP-binding; Biological rhythms; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase;
KW   Two-component regulatory system.
FT   CHAIN           1..383
FT                   /note="Adaptive-response sensory kinase SasA"
FT                   /id="PRO_0000074874"
FT   DOMAIN          161..383
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
FT   MOD_RES         164
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
SQ   SEQUENCE   383 AA;  43436 MW;  395621F5C4BF42F1 CRC64;
     MSSSSELGNA SSVPLQFLLF IDDRPNSQDS VQEIGQCLTN LLDGHSHDLQ ILQISKHPHL
     VEHFRLVATP SLIKLQPEPR QVLAGSNIIQ QLQKWWPRWQ QELAMDPNPE DTGQSPSCPR
     EISSVGYSGE LMKMSDELFL LKKDKEELLQ QIQFKDQILA MLAHDLRSPL TAASIAVDTL
     ELLQHKPIEE QKPALRSQLL YQARKQFKIM DRLIEDILQA SKNLNSQFQV HGRPLAIADL
     CQEVLELYQA KFSKKNLTIT YDIPKDLPNV FADEELIRQV IANLLDNAIK YTPAHGSITV
     GALHRTTQKV QVSITDNGPG IPNSKQETIF EGHFRLQRDE QTDGYGLGLS LCRKIIQAHY
     GQIWVDSRPK QGSSFHFTLP VYR
//