ID   SASA_PROMM              Reviewed;         370 AA.
AC   Q7V6P7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 116.
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=PMT_1099;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(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. {ECO:0000255|HAMAP-
CC       Rule:MF_01837}.
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DR   EMBL; BX548175; CAE21274.1; -; Genomic_DNA.
DR   RefSeq; WP_011130471.1; NC_005071.1.
DR   AlphaFoldDB; Q7V6P7; -.
DR   SMR; Q7V6P7; -.
DR   STRING; 74547.PMT_1099; -.
DR   EnsemblBacteria; CAE21274; CAE21274; PMT_1099.
DR   KEGG; pmt:PMT_1099; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_723030_0_0_3; -.
DR   OMA; AHYGQIW; -.
DR   OrthoDB; 1755994at2; -.
DR   Proteomes; UP000001423; 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   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; PF07689; KaiB; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 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..370
FT                   /note="Adaptive-response sensory-kinase SasA"
FT                   /id="PRO_0000074869"
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   370 AA;  42224 MW;  91FDD04EBE988642 CRC64;
     MDGVKANQRQ QLQLLLVAAR HQLSRSDLRS MIQFLENEDC GFNVTLQMAD PSEQPELLEL
     HRLVATPALI KLSPTPKQVF AGSSIFQQLQ NWITRWQQDI VVTGLGLSLR PTELDGSRTQ
     RELQLEDQLL VLRQENETLI DRLNAQERTL RMVAHELRTP LTAAVLALQS QQLGQINIEH
     FQDVVKRRLD EIELLSKDLL EVKSTKWEDL FNPQNLDLGN IAAEAILELE KLWLDRNIEI
     RTDIPSDLPK VFADQRRMRQ VLLNLLENAL KFTEDGGEVS LTMLHRTSHW VQVSICDNGP
     GIPEDEQERI FLDRVRLPQT SVSTSGFGVG LSVCRRIVEV HGGKIWVVSE PDKGACFYLT
     VPVWQRNGQE