SAER_STAAE
ID SAER_STAAE Reviewed; 228 AA.
AC Q840P8; A6QF15; Q9S4L9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Response regulator SaeR;
DE AltName: Full=Staphylococcus exoprotein expression protein R;
GN Name=saeR; OrderedLocusNames=NWMN_0675;
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 SEQUENCE REVISION TO 189.
RA Wolz C.;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [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 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 [9]
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 [10]
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 [11]
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 [12]
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 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, HlgC), Coa, DNase, Spa and cell
CC wall-associated proteins (Emp, Eap, FnbA, FnbB, Efb). Represses the
CC expression of type 5 capsular polysaccharide (cap operon). Also
CC modulates the expression of several other genes.
CC {ECO:0000269|PubMed:10436918, ECO:0000269|PubMed:11442841,
CC ECO:0000269|PubMed:14563862, ECO:0000269|PubMed:15908369,
CC ECO:0000269|PubMed:15941988, ECO:0000269|PubMed:16734776,
CC ECO:0000269|PubMed:16861653, ECO:0000269|PubMed:17079681,
CC ECO:0000269|PubMed:7922890, ECO:0000269|PubMed:9211714}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated by SaeS. {ECO:0000250}.
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DR EMBL; AF129010; AAD48402.1; -; Genomic_DNA.
DR EMBL; AJ556794; CAD89110.2; -; Genomic_DNA.
DR EMBL; AP009351; BAF66947.1; -; Genomic_DNA.
DR RefSeq; WP_000149344.1; NZ_CP023390.1.
DR AlphaFoldDB; Q840P8; -.
DR SMR; Q840P8; -.
DR EnsemblBacteria; BAF66947; BAF66947; NWMN_0675.
DR KEGG; sae:NWMN_0675; -.
DR HOGENOM; CLU_000445_30_4_9; -.
DR OMA; IMITARV; -.
DR Proteomes; UP000006386; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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 Activator; Cytoplasm; DNA-binding; Phosphoprotein; Repressor;
KW Sensory transduction; Transcription; Transcription regulation;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..228
FT /note="Response regulator SaeR"
FT /id="PRO_0000295917"
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 CONFLICT 112
FT /note="I -> F (in Ref. 1; AAD48402)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="K -> Y (in Ref. 1; AAD48402)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..157
FT /note="IKE -> FKQ (in Ref. 1; AAD48402)"
FT /evidence="ECO:0000305"
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
