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 27-MAR-2024, entry version 140.
DE RecName: Full=Sensor protein SphS;
DE EC=2.7.13.3;
GN Name=sphS; OrderedLocusNames=Synpcc7942_1011;
OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS (Anacystis nidulans R2).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC 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=ATCC 33912 / 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., Golden S., 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D13172; BAA02454.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57041.1; -; Genomic_DNA.
DR PIR; S32932; S32932.
DR RefSeq; WP_011377829.1; NZ_JACJTX010000003.1.
DR AlphaFoldDB; P39664; -.
DR SMR; P39664; -.
DR STRING; 1140.Synpcc7942_1011; -.
DR PaxDb; 1140-Synpcc7942_1011; -.
DR GeneID; 76399756; -.
DR KEGG; syf:Synpcc7942_1011; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_2_3; -.
DR OrthoDB; 9773956at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1011-MONOMER; -.
DR BRENDA; 2.7.13.3; 6187.
DR Proteomes; UP000889800; Chromosome.
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 DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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 PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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; Reference proteome; 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
//
