ID   SAES_STAES              Reviewed;         352 AA.
AC   Q8CTI3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Histidine protein kinase SaeS;
DE            EC=2.7.13.3;
DE   AltName: Full=Sensor protein SaeS;
GN   Name=saeS; OrderedLocusNames=SE_0478;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Member of the two-component regulatory system SaeR/SaeS.
CC       Probably functions as a membrane-associated protein kinase that upon
CC       sensing the appropriate signal, autophosphorylates and in turn
CC       activates the cytosolic response regulator SaeR (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO04075.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE015929; AAO04075.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_764033.1; NC_004461.1.
DR   AlphaFoldDB; Q8CTI3; -.
DR   SMR; Q8CTI3; -.
DR   STRING; 176280.SE_0478; -.
DR   EnsemblBacteria; AAO04075; AAO04075; SE_0478.
DR   KEGG; sep:SE_0478; -.
DR   PATRIC; fig|176280.10.peg.450; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_3_9; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; 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   CDD; cd00082; HisKA; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..352
FT                   /note="Histidine protein kinase SaeS"
FT                   /id="PRO_0000295939"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          130..349
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         133
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   352 AA;  40285 MW;  2726104F160739FA CRC64;
     MTIFSIRSQI IIGVISSVIL TTIILVIAYK LMWFNGHMTL TLAITTMITS CLTLSICSIF
     INPLIQKIKQ FNIKTKQFIN HEKFIDDETF QSPREIKELN DSFNKMAYEI NNQMNMIKNE
     QQEKTEIIQN LAHDLKTPLA GIRSYSEGLR DGVISDPQEV HEAYEILIKQ ANRLSILFDD
     ITHVINLNTG RSYPLELIQL DQLLVNILQP YEQHIKQENR TLEVNFCTDI DAFYQYRPPI
     ERILTNLLDN ALKFSNSGSR IDIIISECKE NDVISISIKD EGIGIVPELQ SRIFERTFRV
     EDSRNTKTGG SGLGLYIANE LAQQIDASIT VQSDLDIGTT MTLTLKKFQF KK