ID   SASA_PROMP              Reviewed;         372 AA.
AC   Q7V113;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=PMM1077;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
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; BX548174; CAE19536.1; -; Genomic_DNA.
DR   RefSeq; WP_011132710.1; NC_005072.1.
DR   AlphaFoldDB; Q7V113; -.
DR   SMR; Q7V113; -.
DR   STRING; 59919.PMM1077; -.
DR   EnsemblBacteria; CAE19536; CAE19536; PMM1077.
DR   KEGG; pmm:PMM1077; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_723030_0_0_3; -.
DR   OMA; AHYGQIW; -.
DR   OrthoDB; 1755994at2; -.
DR   Proteomes; UP000001026; 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; 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..372
FT                   /note="Adaptive-response sensory-kinase SasA"
FT                   /id="PRO_0000074870"
FT   DOMAIN          147..360
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
FT   MOD_RES         150
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01837"
SQ   SEQUENCE   372 AA;  42571 MW;  ABBFCE7AF705B0DD CRC64;
     MNEKKELKLI LVAARNHLSR GDLKLLLSYL ESDDCEFEIS LQISEPTEQP ELLELHRLVA
     IPALIKVSPA PKQIFAGSNI FVQLQTWLPR WKQEGVTKDL GINLQPSKID SIRTQKEFLL
     EEELLVLRQE NETLTKRIES QERLLRMVAH ELRTPLTAAT LAIQSQKLGQ IDIKKLQDVI
     KRRLEEIELL SQDLLEVGTT KWEALFNPQK IDLGNISAEA ILELEKFWRL RKIEIDTDIP
     SDLPSVYADQ RRMRQVFLNL IENALKFSEN SGRIKITLIH KTNQWVEITI CDKGAGIPVS
     EQKRIFLDRV RLPQTSEGTS GFGIGLSVCR RIVEVHGGRI WVVSEVGEGS CFHFTVPVWQ
     GQNKDQQHLT KG