HPTS_STAA8
ID HPTS_STAA8 Reviewed; 518 AA.
AC Q2G1E0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Sensor protein kinase HptS;
DE EC=2.7.13.3;
GN Name=hptS; OrderedLocusNames=SAOUHSC_00185;
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 DISRUPTION PHENOTYPE, AND FUNCTION.
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). May act as a sensor protein kinase which is
CC autophosphorylated at a histidine residue and transfers its phosphate
CC group to the conserved aspartic acid residue in the regulatory domain
CC of HptS. In turn, HptS antagonizes CcpA-dependent transcription of a
CC subset of CcpA-regulated genes involved in antibiotic susceptibility
CC (PubMed:30540769). {ECO:0000269|PubMed:25644013,
CC ECO:0000269|PubMed:30540769}.
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:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
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; ABD29363.1; -; Genomic_DNA.
DR RefSeq; WP_000127982.1; NZ_LS483365.1.
DR RefSeq; YP_498782.1; NC_007795.1.
DR PDB; 6LKG; X-ray; 1.95 A; B/D=45-215.
DR PDB; 6LKH; X-ray; 2.53 A; C/D=45-215.
DR PDB; 6LKI; X-ray; 1.78 A; B=45-215.
DR PDBsum; 6LKG; -.
DR PDBsum; 6LKH; -.
DR PDBsum; 6LKI; -.
DR AlphaFoldDB; Q2G1E0; -.
DR SMR; Q2G1E0; -.
DR STRING; 1280.SAXN108_0199; -.
DR EnsemblBacteria; ABD29363; ABD29363; SAOUHSC_00185.
DR GeneID; 3919499; -.
DR KEGG; sao:SAOUHSC_00185; -.
DR PATRIC; fig|93061.5.peg.173; -.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_525720_0_0_9; -.
DR OMA; YIWVEHR; -.
DR PRO; PR:Q2G1E0; -.
DR Proteomes; UP000008816; 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 Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR Pfam; PF06580; His_kinase; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..518
FT /note="Sensor protein kinase HptS"
FT /id="PRO_0000299126"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 297..513
FT /note="Histidine kinase"
FT MOD_RES 325
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000250"
FT HELIX 46..75
FT /evidence="ECO:0007829|PDB:6LKI"
FT HELIX 83..99
FT /evidence="ECO:0007829|PDB:6LKI"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:6LKI"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:6LKI"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6LKI"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:6LKI"
FT STRAND 138..150
FT /evidence="ECO:0007829|PDB:6LKI"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:6LKI"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:6LKI"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:6LKI"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:6LKI"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6LKI"
FT STRAND 203..213
FT /evidence="ECO:0007829|PDB:6LKI"
SQ SEQUENCE 518 AA; 61047 MW; 9F173AB7D3E1B7B4 CRC64;
MTAYKPYRHQ LRRSLFASTI FPVFLVIIIG LVSFYAIYIW IEHRTIHQHV DESQSSLHHT
EKQIQTFITQ HNNSFQELDL TNHHDVTATK RELLKLIHQQ PATLYYELSG PNQFITNNYE
HLNTKNMYLF STHQLKFKNS TYMLKIYMAN TPRLSEIKKD NRQFALIVDQ YDNILYANDD
RFTIGEKYRP QQFGFMNESV KLNHADHRLI IYKDIHENIE DGITLLIVMA VVLVLLVIFG
FISADNMAKR QTKDIETIIQ KIYYAKNRHL GTYTPLKNNS ELEEINNYIY DLFESNEQLI
HSIEHTERRL RDIQLKEIER QFQPHFLFNT MQTIQYLITL SPKLAQTVVQ QLSQMLRYSL
RTNSHTVELN EELNYIEQYV AIQNIRFDDM IKLHIESSEE ARHQTIGKMM LQPLIENAIK
HGRDTESLDI TIRLTLARQN LHVLVCDNGI GMSSSRLQYV RQSLNNDVFD TKHLGLNHLH
NKAMIQYGSH ARLHIFSKRN QGTLICYKIP LSRGNVDV
