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 27-MAR-2024, entry version 117.
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; Bacillota; 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}.
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DR EMBL; CP000046; AAW37824.1; -; Genomic_DNA.
DR RefSeq; WP_000244412.1; NC_002951.2.
DR AlphaFoldDB; Q5HHW5; -.
DR SMR; Q5HHW5; -.
DR KEGG; sac:SACOL0765; -.
DR HOGENOM; CLU_000445_89_3_9; -.
DR Proteomes; UP000000530; Chromosome.
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; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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 PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
DR Pfam; PF00672; HAMP; 1.
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; 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; 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
//
