SAES_STAA8
ID SAES_STAA8 Reviewed; 351 AA.
AC Q2G2U1; Q840P5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 110.
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=SAOUHSC_00714;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN REGULATION OF
RP EXOPROTEINS SYNTHESIS.
RX PubMed=14563862; DOI=10.1128/jb.185.21.6278-6286.2003;
RA Steinhuber A., Goerke C., Bayer M.G., Doering G., Wolz C.;
RT "Molecular architecture of the regulatory locus sae of Staphylococcus
RT aureus and its impact on expression of virulence factors.";
RL J. Bacteriol. 185:6278-6286(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP FUNCTION IN REGULATION OF EXOPROTEINS SYNTHESIS.
RX PubMed=7922890; DOI=10.1139/m94-107;
RA Giraudo A.T., Raspanti C.G., Calzolari A., Nagel R.;
RT "Characterization of a Tn551-mutant of Staphylococcus aureus defective in
RT the production of several exoproteins.";
RL Can. J. Microbiol. 40:677-681(1994).
RN [4]
RP FUNCTION IN REGULATION OF EXOPROTEINS SYNTHESIS.
RX PubMed=8742355; DOI=10.1139/m96-019;
RA Giraudo A.T., Rampone H., Calzolari A., Nagel R.;
RT "Phenotypic characterization and virulence of a sae- agr- mutant of
RT Staphylococcus aureus.";
RL Can. J. Microbiol. 42:120-123(1996).
RN [5]
RP FUNCTION IN REGULATION OF EXOPROTEINS SYNTHESIS.
RX PubMed=9211714; DOI=10.1007/s002030050469;
RA Giraudo A.T., Cheung A.L., Nagel R.;
RT "The sae locus of Staphylococcus aureus controls exoprotein synthesis at
RT the transcriptional level.";
RL Arch. Microbiol. 168:53-58(1997).
RN [6]
RP FUNCTION IN REGULATION OF EXOPROTEINS SYNTHESIS.
RX PubMed=10436918; DOI=10.1111/j.1574-6968.1999.tb13707.x;
RA Giraudo A.T., Calzolari A., Cataldi A.A., Bogni C., Nagel R.;
RT "The sae locus of Staphylococcus aureus encodes a two-component regulatory
RT system.";
RL FEMS Microbiol. Lett. 177:15-22(1999).
RN [7]
RP FUNCTION IN REGULATION OF EXOPROTEINS SYNTHESIS.
RX PubMed=11442841; DOI=10.1046/j.1365-2958.2001.02494.x;
RA Goerke C., Fluckiger U., Steinhuber A., Zimmerli W., Wolz C.;
RT "Impact of the regulatory loci agr, sarA and sae of Staphylococcus aureus
RT on the induction of alpha-toxin during device-related infection resolved by
RT direct quantitative transcript analysis.";
RL Mol. Microbiol. 40:1439-1447(2001).
RN [8]
RP REGULATION BY AGR, AND DEVELOPMENTAL STAGE.
RX PubMed=12732971; DOI=10.1007/s00284-002-3853-z;
RA Giraudo A.T., Mansilla C., Chan A., Raspanti C.G., Nagel R.;
RT "Studies on the expression of regulatory locus sae in Staphylococcus
RT aureus.";
RL Curr. Microbiol. 46:246-250(2003).
RN [9]
RP FUNCTION IN REGULATION OF EXOPROTEINS SYNTHESIS, AND INDUCTION.
RX PubMed=14523104; DOI=10.1099/mic.0.26575-0;
RA Novick R.P., Jiang D.;
RT "The staphylococcal saeRS system coordinates environmental signals with agr
RT quorum sensing.";
RL Microbiology 149:2709-2717(2003).
RN [10]
RP VIRULENCE.
RX PubMed=15576798; DOI=10.1128/jb.186.24.8478-8489.2004;
RA Benton B.M., Zhang J.P., Bond S., Pope C., Christian T., Lee L.,
RA Winterberg K.M., Schmid M.B., Buysse J.M.;
RT "Large-scale identification of genes required for full virulence of
RT Staphylococcus aureus.";
RL J. Bacteriol. 186:8478-8489(2004).
RN [11]
RP FUNCTION IN REGULATION OF ADHESIN SYNTHESIS.
RX PubMed=15941988; DOI=10.1099/mic.0.27902-0;
RA Harraghy N., Kormanec J., Wolz C., Homerova D., Goerke C., Ohlsen K.,
RA Qazi S., Hill P., Herrmann M.;
RT "Sae is essential for expression of the staphylococcal adhesins Eap and
RT Emp.";
RL Microbiology 151:1789-1800(2005).
RN [12]
RP FUNCTION IN REGULATION OF EXOPROTEINS SYNTHESIS, AND VIRULENCE.
RX PubMed=17041853; DOI=10.1086/508210;
RA Xiong Y.Q., Willard J., Yeaman M.R., Cheung A.L., Bayer A.S.;
RT "Regulation of Staphylococcus aureus alpha-toxin gene (hla) expression by
RT agr, sarA, and sae in vitro and in experimental infective endocarditis.";
RL J. Infect. Dis. 194:1267-1275(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. SaeR/SaeS activates the expression of exoproteins
CC involved in adhesion and invasion of host cells, including hemolysins
CC (hla, hlb), coa, Dnase, spa and cell wall-associated proteins (emp,
CC eap, fnbA). Acts probably downstream of the agr system in the
CC regulatory cascade of virulence factors. {ECO:0000269|PubMed:10436918,
CC ECO:0000269|PubMed:11442841, ECO:0000269|PubMed:14523104,
CC ECO:0000269|PubMed:14563862, ECO:0000269|PubMed:15941988,
CC ECO:0000269|PubMed:17041853, ECO:0000269|PubMed:7922890,
CC ECO:0000269|PubMed:8742355, ECO:0000269|PubMed:9211714}.
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 -!- DEVELOPMENTAL STAGE: Expressed at high levels in the late and post-
CC exponential growth phases. {ECO:0000269|PubMed:12732971}.
CC -!- INDUCTION: Transcription is affected by Agr and SarA. Also,
CC transcriptionally repressed by NaCL, pH below 6, glucose and the
CC antibiotic clindamycin. {ECO:0000269|PubMed:14523104}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
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DR EMBL; AJ556795; CAD89115.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29847.1; -; Genomic_DNA.
DR RefSeq; WP_000244412.1; NZ_LS483365.1.
DR RefSeq; YP_499273.1; NC_007795.1.
DR AlphaFoldDB; Q2G2U1; -.
DR SMR; Q2G2U1; -.
DR STRING; 1280.SAXN108_0773; -.
DR BindingDB; Q2G2U1; -.
DR ChEMBL; CHEMBL4295597; -.
DR EnsemblBacteria; ABD29847; ABD29847; SAOUHSC_00714.
DR GeneID; 3919341; -.
DR KEGG; sao:SAOUHSC_00714; -.
DR PATRIC; fig|93061.5.peg.643; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_3_9; -.
DR OMA; LIRVIDH; -.
DR PHI-base; PHI:4655; -.
DR PHI-base; PHI:8781; -.
DR PRO; PR:Q2G2U1; -.
DR Proteomes; UP000008816; 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:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IBA:GO_Central.
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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system; Virulence.
FT CHAIN 1..351
FT /note="Histidine protein kinase SaeS"
FT /id="PRO_0000295937"
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
