SAER_STAA8
ID SAER_STAA8 Reviewed; 228 AA.
AC Q2G2G2; Q840P6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Response regulator SaeR;
DE AltName: Full=Staphylococcus exoprotein expression protein R;
GN Name=saeR; OrderedLocusNames=SAOUHSC_00715;
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 transcriptional
CC regulator via a specific DNA-binding domain, recognizing motifs near
CC the promoter sequences of target genes. SaeR/SaeS activates the
CC expression of exoproteins involved in adhesion and invasion of host
CC cells, including hemolysins (Hla, Hlb), Coa, DNase, Spa and cell wall-
CC associated proteins (Emp, Eap, FnbA). Acts probably downstream of the
CC Agr system in the regulatory cascade of virulence factors.
CC {ECO:0000269|PubMed:10436918, ECO:0000269|PubMed:11442841,
CC ECO:0000269|PubMed:14523104, ECO:0000269|PubMed:14563862,
CC ECO:0000269|PubMed:15941988, ECO:0000269|PubMed:17041853,
CC ECO:0000269|PubMed:7922890, ECO:0000269|PubMed:8742355,
CC ECO:0000269|PubMed:9211714}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in the late and post-
CC exponential growth phases. {ECO:0000269|PubMed:12732971}.
CC -!- INDUCTION: Autoregulated. Transcription is affected by Agr and SarA.
CC Also, transcriptionally repressed by NaCL, pH below 6, glucose and the
CC antibiotic clindamycin. {ECO:0000269|PubMed:14523104}.
CC -!- PTM: Phosphorylated by SaeS. {ECO:0000250}.
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DR EMBL; AJ556795; CAD89114.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29848.1; -; Genomic_DNA.
DR RefSeq; WP_000149344.1; NZ_LS483365.1.
DR RefSeq; YP_499274.1; NC_007795.1.
DR PDB; 4QWQ; X-ray; 2.50 A; A/B=123-228.
DR PDBsum; 4QWQ; -.
DR AlphaFoldDB; Q2G2G2; -.
DR SMR; Q2G2G2; -.
DR STRING; 1280.SAXN108_0774; -.
DR EnsemblBacteria; ABD29848; ABD29848; SAOUHSC_00715.
DR GeneID; 3919342; -.
DR KEGG; sao:SAOUHSC_00715; -.
DR PATRIC; fig|93061.5.peg.644; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_4_9; -.
DR OMA; IMITARV; -.
DR PHI-base; PHI:4654; -.
DR PHI-base; PHI:8780; -.
DR PRO; PR:Q2G2G2; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Phosphoprotein;
KW Reference proteome; Sensory transduction; Transcription;
KW Transcription regulation; Two-component regulatory system; Virulence.
FT CHAIN 1..228
FT /note="Response regulator SaeR"
FT /id="PRO_0000295925"
FT DOMAIN 3..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 127..226
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4QWQ"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:4QWQ"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:4QWQ"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:4QWQ"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:4QWQ"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:4QWQ"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:4QWQ"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:4QWQ"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:4QWQ"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:4QWQ"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:4QWQ"
SQ SEQUENCE 228 AA; 26858 MW; 9364A49366DF1BA5 CRC64;
MTHLLIVDDE QDIVDICQTY FEYEGYKVTT TTSGKEAISL LSNDIDIMVL DIMMPEVNGY
DIVKEMKRQK LDIPFIYLTA KTQEHDTIYA LTLGADDYVK KPFSPRELVL RINNLLTRMK
KYHHQPVEQL SFDELTLINL SKVVTVNGHE VPMRIKEFEL LWYLASRENE VISKSELLEK
VWGYDYYEDA NTVNVHIHRI REKLEKESFT TYTITTVWGL GYKFERSR
