HPTR_STAAS
ID HPTR_STAAS Reviewed; 252 AA.
AC Q6GCQ3;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Transcriptional regulatory protein HptR;
GN Name=hptR; OrderedLocusNames=SAS0198;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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. Activates uhpT
CC expression to facilitate glucose-6-phosphate/G6P utilization by
CC directly binding to its promoter. Antagonizes CcpA-dependent
CC transcription of a subset of CcpA-regulated genes involved in
CC antibiotic susceptibility. {ECO:0000250|UniProtKB:Q2G1E1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by HptS. {ECO:0000250|UniProtKB:Q2G1E1}.
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DR EMBL; BX571857; CAG41966.1; -; Genomic_DNA.
DR RefSeq; WP_000477521.1; NC_002953.3.
DR AlphaFoldDB; Q6GCQ3; -.
DR SMR; Q6GCQ3; -.
DR KEGG; sas:SAS0198; -.
DR HOGENOM; CLU_000445_5_1_9; -.
DR OMA; IMTAFEM; -.
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 3: Inferred from homology;
KW Cytoplasm; DNA-binding; Phosphoprotein; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..252
FT /note="Transcriptional regulatory protein HptR"
FT /id="PRO_0000299111"
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