ID   SASA_PARMW              Reviewed;         383 AA.
AC   Q7U871;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Adaptive-response sensory-kinase SasA {ECO:0000255|HAMAP-Rule:MF_01837};
DE            EC=2.7.13.3;
GN   Name=sasA {ECO:0000255|HAMAP-Rule:MF_01837}; OrderedLocusNames=SYNW0753;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
CC   -!- FUNCTION: May be involved in signal transduction. Participates in the
CC       KaiABC clock protein complex, which constitutes the main circadian
CC       regulator in cyanobacteria, via its interaction with KaiC. Required for
CC       robustness of the circadian rhythm of gene expression and is involved
CC       in clock outputs. {ECO:0000255|HAMAP-Rule:MF_01837}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBUNIT: Interacts with KaiC. Participates in the KaiABC complex, whose
CC       core is composed of a KaiC homohexamer, a KaiB dimer and two KaiA
CC       dimers. {ECO:0000255|HAMAP-Rule:MF_01837}.
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DR   EMBL; BX569691; CAE07268.1; -; Genomic_DNA.
DR   RefSeq; WP_011127618.1; NC_005070.1.
DR   AlphaFoldDB; Q7U871; -.
DR   SMR; Q7U871; -.
DR   STRING; 84588.SYNW0753; -.
DR   EnsemblBacteria; CAE07268; CAE07268; SYNW0753.
DR   KEGG; syw:SYNW0753; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_723030_0_0_3; -.
DR   OMA; AHYGQIW; -.
DR   OrthoDB; 1755994at2; -.
DR   Proteomes; UP000001422; 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:0007623; P:circadian rhythm; IEA:UniProtKB-UniRule.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd02978; KaiB_like; 1.
DR   Gene3D; 3.30.565.10; -; 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   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; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Biological rhythms; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Two-component regulatory system.
FT   CHAIN           1..383
FT                   /note="Adaptive-response sensory-kinase SasA"
FT                   /id="PRO_0000074873"
FT   DOMAIN          152..365
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
FT   MOD_RES         155
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
SQ   SEQUENCE   383 AA;  43221 MW;  D34ED511BC9793E4 CRC64;
     MGEDDPKGRQ RLKLLLVAAR HHLSGPDLRS VVHYLERDDV GFQVTLQLAD PSQQPELLEL
     HRLVITPALI KLSPAPKQVF AGSNILQQLK GWVPRWQQDG VVSGLGLSLR PTELDGSRTQ
     KELQLEDQLL VLRQENETLI DRIHAQERLL RMVAHELRTP LTAAALALQS QRLGQIDMTR
     FQDVITRRLE EMEALSKDLL EVGTTRWETL FNPQRLDLAS VSAEVILELE KLWLGRNVEI
     RTDIPSDLPK VFADQRRMRQ VLLNLLENAL KYTGNGGHIT LTMLHRTSQR VEVSVCDSGP
     GIPTEEQQRI FLDRVRLPQT SDRTTGFGVG LSVCRRIVEV HGGRIWVVSE PGEGACFTFT
     VPIWQGQGQE WGQAVLTEGE LEP