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   25-MAY-2022, entry version 134.
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}; Synonyms=sarA;
GN   OrderedLocusNames=sll0750;
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=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).
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; BA000022; BAA10143.1; -; Genomic_DNA.
DR   PIR; S76291; S76291.
DR   AlphaFoldDB; Q55630; -.
DR   SMR; Q55630; -.
DR   IntAct; Q55630; 9.
DR   STRING; 1148.1001516; -.
DR   PaxDb; Q55630; -.
DR   EnsemblBacteria; BAA10143; BAA10143; BAA10143.
DR   KEGG; syn:sll0750; -.
DR   eggNOG; COG2205; Bacteria.
DR   InParanoid; Q55630; -.
DR   OMA; AHYGQIW; -.
DR   PhylomeDB; Q55630; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR   GO; GO:0007623; P:circadian rhythm; IEA:UniProtKB-UniRule.
DR   GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
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; 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