ID   SPHS_SYNE7              Reviewed;         413 AA.
AC   P39664; Q31PH8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Sensor protein SphS;
DE            EC=2.7.13.3;
GN   Name=sphS; OrderedLocusNames=Synpcc7942_1011;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF N-TERMINUS.
RX   PubMed=8497200; DOI=10.1111/j.1365-2958.1993.tb01205.x;
RA   Aiba H., Nagaya M., Mizuno T.;
RT   "Sensor and regulator proteins from the cyanobacterium Synechococcus
RT   species PCC7942 that belong to the bacterial signal-transduction protein
RT   families: implication in the adaptive response to phosphate limitation.";
RL   Mol. Microbiol. 8:81-91(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Member of the two-component regulatory system SphR/SphS.
CC       Sensory kinase. Is involved in inducible production of alkaline
CC       phosphatase in response to phosphate limitation as it is directly
CC       involved in the regulation of phoA transcription in response to
CC       phosphate limitation. SphS functions as a protein kinase that
CC       phosphorylates SphR.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR   EMBL; D13172; BAA02454.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57041.1; -; Genomic_DNA.
DR   PIR; S32932; S32932.
DR   RefSeq; WP_011377829.1; NC_007604.1.
DR   AlphaFoldDB; P39664; -.
DR   SMR; P39664; -.
DR   STRING; 1140.Synpcc7942_1011; -.
DR   PRIDE; P39664; -.
DR   EnsemblBacteria; ABB57041; ABB57041; Synpcc7942_1011.
DR   KEGG; syf:Synpcc7942_1011; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_2_3; -.
DR   OMA; ENQLLWC; -.
DR   OrthoDB; 1827824at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1011-MON; -.
DR   BRENDA; 2.7.13.3; 6187.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.565.10; -; 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; IPR000014; PAS.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Transferase;
KW   Two-component regulatory system.
FT   CHAIN           1..413
FT                   /note="Sensor protein SphS"
FT                   /id="PRO_0000074880"
FT   DOMAIN          176..398
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         179
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   CONFLICT        384..413
FT                   /note="VTGGAWLRVQLPQEPSLTPALKIGTGRRSG -> SPAGLGCGYNCPKNHPSP
FT                   LRLRSELDVAAA (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   413 AA;  46216 MW;  FA93EC0909A8DB87 CRC64;
     MAAWEFALGL LTASLWRWAR KWRSPVKVKP MLAAVSSLEP QLEQITTDLR DRDRLLEDLP
     VSFLLLDADN LVLEANRSAR VLLALPPEDY CRPLLEVVRS YELDRLVARC RAANAPQTDR
     WTLTPVNPDP LQVVPQTPRP VQGQAIPLSN GQIGVLIEDR QELVDLAQQR NRWVSDVAHE
     LKTPLTSIRL LAEALRDRLQ DEPQVWVDRL LGETQRLGQL VQDLLELSRL EQGPSGLQKL
     EAVDLVALLT SVRNSLEPLA EPLRLGWAYQ GPEQGFVRGD RQRLFRLWLN LVDNAIRHSP
     SGGCLYVELR QRGDTWICDL YDDGPGFADA DLPYLFERFY RGDPSRVRPA AASSSSPGSG
     LGLAIARQVV EAHQGRISAR NHPVTGGAWL RVQLPQEPSL TPALKIGTGR RSG