ID   SAES_STAAC              Reviewed;         351 AA.
AC   Q5HHW5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
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;
DE   AltName: Full=Staphylococcus exoprotein expression protein S;
GN   Name=saeS; OrderedLocusNames=SACOL0765;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
RN   [2]
RP   FUNCTION IN GLOBAL REGULATION.
RX   PubMed=17079681; DOI=10.1128/jb.00555-06;
RA   Rogasch K., Ruehmling V., Pane-Farre J., Hoeper D., Weinberg C., Fuchs S.,
RA   Schmudde M., Broeker B.M., Wolz C., Hecker M., Engelmann S.;
RT   "Influence of the two-component system saeRS on global gene expression in
RT   two different Staphylococcus aureus strains.";
RL   J. Bacteriol. 188:7742-7758(2006).
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). Modulates the expression of several
CC       genes. {ECO:0000250, ECO:0000269|PubMed:17079681}.
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   ---------------------------------------------------------------------------
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; CP000046; AAW37824.1; -; Genomic_DNA.
DR   RefSeq; WP_000244412.1; NC_002951.2.
DR   AlphaFoldDB; Q5HHW5; -.
DR   SMR; Q5HHW5; -.
DR   EnsemblBacteria; AAW37824; AAW37824; SACOL0765.
DR   KEGG; sac:SACOL0765; -.
DR   HOGENOM; CLU_000445_89_3_9; -.
DR   OMA; LIRVIDH; -.
DR   Proteomes; UP000000530; 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; 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   1: Evidence at protein level;
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_0000295931"
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;  39741 MW;  08CB447C472A1B47 CRC64;
     MVLSIRSQII IGVVSSILLT STILAIAYIL MWFNGHMTLT LTLTTIITSC LTLLICSIFI
     NPLIQKIKQF NIKTKQFANG NYASNDKTFN SPKEIYELNQ SFNKMASEIT QQMNQIKSEQ
     QEKTELIQNL AHDLKTPLAS IISYSEGLRD GIITKDHEIK ESYDILIKQA NRLSTLFDDM
     THIITLNTGK TYPPELIQLD QLLVSILQPY EQRIKHENRT LEVNFCNEID AFYQYRTPLE
     RILTNLLDNA LKFSNVGSRI DINISENEDQ DTIDIAISDE GIGIIPELQE RIFERTFRVE
     NSRNTKTGGS GLGLYIANEL AQQNNAKISV SSDIDVGTTM TVTLHKLDIT S