HPTR_STAA8
ID HPTR_STAA8 Reviewed; 252 AA.
AC Q2G1E1;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Transcriptional regulatory protein HptR;
GN Name=hptR; OrderedLocusNames=SAOUHSC_00184;
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 [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 [2]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=25644013; DOI=10.1128/iai.03109-14;
RA Park J.Y., Kim J.W., Moon B.Y., Lee J., Fortin Y.J., Austin F.W.,
RA Yang S.J., Seo K.S.;
RT "Characterization of a novel two-component regulatory system, HptRS, the
RT regulator for the hexose phosphate transport system in Staphylococcus
RT aureus.";
RL Infect. Immun. 83:1620-1628(2015).
RN [3]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=26711125; DOI=10.1007/s00430-015-0446-6;
RA Yang Y., Sun H., Liu X., Wang M., Xue T., Sun B.;
RT "Regulatory mechanism of the three-component system HptRSA in glucose-6-
RT phosphate uptake in Staphylococcus aureus.";
RL Med. Microbiol. Immunol. 205:241-253(2016).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30540769; DOI=10.1371/journal.pone.0207161;
RA Reed J.M., Olson S., Brees D.F., Griffin C.E., Grove R.A., Davis P.J.,
RA Kachman S.D., Adamec J., Somerville G.A.;
RT "Coordinated regulation of transcription by CcpA and the Staphylococcus
RT aureus two-component system HptRS.";
RL PLoS ONE 13:E0207161-E0207161(2018).
CC -!- FUNCTION: Member of the two-component regulatory system HptS/HptR that
CC regulates genes involved in hexose phosphate transport system in
CC response to changes in extracellular phosphate sources
CC (PubMed:25644013). Activates uhpT expression to facilitate glucose-6-
CC phosphate/G6P utilization by directly binding to its promoter
CC (PubMed:26711125). Antagonizes CcpA-dependent transcription of a subset
CC of CcpA-regulated genes involved in antibiotic susceptibility
CC (PubMed:30540769). {ECO:0000269|PubMed:25644013,
CC ECO:0000269|PubMed:26711125, ECO:0000269|PubMed:30540769}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by HptS. {ECO:0000269|PubMed:26711125}.
CC -!- DISRUPTION PHENOTYPE: Deletion leads to impaired growth when the
CC available carbon source is limited to glucose-6-phosphate
CC (PubMed:25644013). Deletion alters also antibiotic susceptibility
CC (PubMed:30540769). {ECO:0000269|PubMed:25644013,
CC ECO:0000269|PubMed:30540769}.
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DR EMBL; CP000253; ABD29362.1; -; Genomic_DNA.
DR RefSeq; WP_000477521.1; NZ_LS483365.1.
DR RefSeq; YP_498781.1; NC_007795.1.
DR AlphaFoldDB; Q2G1E1; -.
DR SMR; Q2G1E1; -.
DR STRING; 1280.SAXN108_0198; -.
DR EnsemblBacteria; ABD29362; ABD29362; SAOUHSC_00184.
DR GeneID; 3919498; -.
DR KEGG; sao:SAOUHSC_00184; -.
DR PATRIC; fig|93061.5.peg.172; -.
DR eggNOG; COG2207; Bacteria.
DR eggNOG; COG4753; Bacteria.
DR HOGENOM; CLU_000445_5_1_9; -.
DR OMA; IMTAFEM; -.
DR PRO; PR:Q2G1E1; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..252
FT /note="Transcriptional regulatory protein HptR"
FT /id="PRO_0000299115"
FT DOMAIN 3..118
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 153..250
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 170..191
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 217..240
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 252 AA; 29599 MW; F42C8E41A0CE4082 CRC64;
MFKVVICDDE RIIREGLKQI IPWGDYHFNT IYTAKDGVEA LSLIQQHQPE LVITDIRMPR
KNGVDLLNDI AHLDCNVIIL SSYDDFEYMK AGIQHHVLDY LLKPVDHAQL EVILGRLVRT
LLEQQSQNGR SLASCHDAFQ PLLKVEYDDY YVNQIVDQIK QSYQTKVTVS DLIQHIDVSE
SYAMRTFKDH VGITIVDYLN RYRILQSLQL LDRHYKHYEI ADKVGFSEYK MFSYHFKKYL
QMSPSDYCKQ AK
