ID   SAES_STAAB              Reviewed;         351 AA.
AC   Q2YSM6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Histidine protein kinase SaeS;
DE            EC=2.7.13.3;
DE   AltName: Full=Sensor protein SaeS;
DE   AltName: Full=Staphylococcus exoprotein expression protein S;
GN   Name=saeS; OrderedLocusNames=SAB0654c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- FUNCTION: Member of the two-component regulatory system SaeR/SaeS
CC       involved in the regulation of staphylococcal virulence factors in a
CC       strain-dependent fashion. Probably functions as a membrane-associated
CC       protein kinase that upon sensing the appropriate signal,
CC       autophosphorylates and in turn activates the cytosolic response
CC       regulator SaeR (By similarity). {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}.
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DR   EMBL; AJ938182; CAI80342.1; -; Genomic_DNA.
DR   RefSeq; WP_000244415.1; NC_007622.1.
DR   AlphaFoldDB; Q2YSM6; -.
DR   SMR; Q2YSM6; -.
DR   KEGG; sab:SAB0654c; -.
DR   HOGENOM; CLU_000445_89_3_9; -.
DR   OMA; LIRVIDH; -.
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; IPR003660; HAMP_dom.
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; PS50885; HAMP; 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; Virulence.
FT   CHAIN           1..351
FT                   /note="Histidine protein kinase SaeS"
FT                   /id="PRO_0000295930"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          61..114
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          129..348
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         132
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   351 AA;  39714 MW;  E6255586417AAC4D CRC64;
     MVLSIRSQII IGVVSSILLT STILAIAYIL MWFNGHMTLT LTLTTIITSC LTLLICSIFI
     NPLIQKIKQF NIKTKQFANG NYASNDKTFN SPKEIYELNQ SFNKMASEIT QQMNQIKSEQ
     QEKTELIQNL AHDLKTPLAS IISYSEGLRD GIITKDHEIK ESYDILIKQA NRLSTLFDDM
     THIITLNTGK TYPPELIQLD QLLVSILQPY EQRIKHENRT LEVNFCSEID AFYQYRTPLE
     RILTNLLDNA LKFSNVGSRI DINISENKDQ DTIDIAISDE GIGIIPELQE RIFERTFRVE
     NSRNTKTGGS GLGLYIANEL AQQNNAKISV SSDIDVGTTM TVTLHKLDIT S