SAES_STAAE
ID SAES_STAAE Reviewed; 351 AA.
AC Q840P7; A6QF14; Q9S4L8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 114.
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=NWMN_0674;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN REGULATION OF
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN REGULATION OF
RP EXOPROTEINS AND TYPE 5 CAPSULAR POLYSACCHARIDE 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [4]
RP FUNCTION IN REGULATION OF EXOPROTEINS SYNTHESIS.
RC STRAIN=ATCC 13565 / 196E;
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 [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=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 [7]
RP FUNCTION IN REGULATION OF EXOPROTEINS SYNTHESIS.
RX PubMed=15908369; DOI=10.1128/iai.73.6.3415-3421.2005;
RA Goerke C., Fluckiger U., Steinhuber A., Bisanzio V., Ulrich M.,
RA Bischoff M., Patti J.M., Wolz C.;
RT "Role of Staphylococcus aureus global regulators sae and sigmaB in
RT virulence gene expression during device-related infection.";
RL Infect. Immun. 73:3415-3421(2005).
RN [8]
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 [9]
RP FUNCTION IN REGULATION OF EXOPROTEINS SYNTHESIS.
RC STRAIN=Smith;
RX PubMed=16734776; DOI=10.1111/j.1574-6968.2006.00236.x;
RA Yamazaki K., Kato F., Kamio Y., Kaneko J.;
RT "Expression of gamma-hemolysin regulated by sae in Staphylococcus aureus
RT strain Smith 5R.";
RL FEMS Microbiol. Lett. 259:174-180(2006).
RN [10]
RP FUNCTION IN REGULATION OF EXOPROTEINS SYNTHESIS, AND VIRULENCE.
RC STRAIN=WCUH29 / NCIMB 40771;
RX PubMed=16861653; DOI=10.1128/iai.00322-06;
RA Liang X., Yu C., Sun J., Liu H., Landwehr C., Holmes D., Ji Y.;
RT "Inactivation of a two-component signal transduction system, saeRS,
RT eliminates adherence and attenuates virulence of Staphylococcus aureus.";
RL Infect. Immun. 74:4655-4665(2006).
RN [11]
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. SaeR/SaeS activates the expression of exoproteins
CC involved in adhesion and invasion of host cells, including hemolysins
CC (hla, hlb, hlgC), coa, DNase, spa and cell wall-associated proteins
CC (emp, eap, fnbA, fnbB, efb). Represses the expression of type 5
CC capsular polysaccharide (cap operon). Also modulates the expression of
CC several other genes. {ECO:0000269|PubMed:10436918,
CC ECO:0000269|PubMed:11442841, ECO:0000269|PubMed:14563862,
CC ECO:0000269|PubMed:15908369, ECO:0000269|PubMed:15941988,
CC ECO:0000269|PubMed:16734776, ECO:0000269|PubMed:16861653,
CC ECO:0000269|PubMed:17079681, ECO:0000269|PubMed:7922890,
CC 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 -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD48403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF129010; AAD48403.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ556794; CAD89111.1; -; Genomic_DNA.
DR EMBL; AP009351; BAF66946.1; -; Genomic_DNA.
DR RefSeq; WP_000244421.1; NZ_CP023390.1.
DR AlphaFoldDB; Q840P7; -.
DR SMR; Q840P7; -.
DR EnsemblBacteria; BAF66946; BAF66946; NWMN_0674.
DR KEGG; sae:NWMN_0674; -.
DR HOGENOM; CLU_000445_89_3_9; -.
DR OMA; LIRVIDH; -.
DR BRENDA; 2.7.13.3; 3352.
DR Proteomes; UP000006386; 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_0000295929"
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"
FT CONFLICT 76
FT /note="Q -> P (in Ref. 1; AAD48403)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..219
FT /note="QPYEQRIKHENR -> PTIGATYPNMKTA (in Ref. 1; AAD48403)"
FT /evidence="ECO:0000305"
FT CONFLICT 227..238
FT /note="NEIDAFYQYRTP -> KRNSCILSISKRQ (in Ref. 1; AAD48403)"
FT /evidence="ECO:0000305"
FT CONFLICT 244..248
FT /note="TNLLD -> NKTYLM (in Ref. 1; AAD48403)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="E -> G (in Ref. 1; AAD48403)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="S -> R (in Ref. 1; AAD48403)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="M -> V (in Ref. 1; AAD48403)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39725 MW; A9C39D3492E5ECAA CRC64;
MVLSIRSQII IGVVSSIPLT 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
