ID A0A1D9H0Q4_9BURK Unreviewed; 446 AA.
AC A0A1D9H0Q4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BKK79_17930 {ECO:0000313|EMBL:AOY93467.1};
OS Cupriavidus sp. USMAA2-4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=876364 {ECO:0000313|EMBL:AOY93467.1, ECO:0000313|Proteomes:UP000178101};
RN [1] {ECO:0000313|EMBL:AOY93467.1, ECO:0000313|Proteomes:UP000178101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USMAA2-4 {ECO:0000313|EMBL:AOY93467.1,
RC ECO:0000313|Proteomes:UP000178101};
RA Abdullah A.A.-A., Shafie N.A.H., Lau N.S.;
RT "Complete genome sequences of three Cupriavidus strains isolated from
RT various Malaysian environments.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Member of the two-component regulatory system PhoR/PhoB
CC involved in the phosphate regulon genes expression. PhoR may function
CC as a membrane-associated protein kinase that phosphorylates PhoB in
CC response to environmental signals. {ECO:0000256|ARBA:ARBA00025207}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; CP017748; AOY93467.1; -; Genomic_DNA.
DR RefSeq; WP_071014073.1; NZ_CP017748.1.
DR AlphaFoldDB; A0A1D9H0Q4; -.
DR STRING; 876364.BKK79_17930; -.
DR KEGG; cuu:BKK79_17930; -.
DR Proteomes; UP000178101; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR021766; PhoR.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR014310; Sig_transdc_His_kinase_PhoR.
DR NCBIfam; TIGR02966; phoR_proteo; 1.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF11808; PhoR; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AOY93467.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000178101};
KW Transferase {ECO:0000313|EMBL:AOY93467.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022592}.
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..428
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 446 AA; 50189 MW; E6E5738D15F5E689 CRC64;
MNVIWARSAA ILISVAVASA GLYLWRGPVW ALSLGCLALL GQLGYYLYQI NRLWKVLDAP
AYGEIPSALG LWGEVYYRLH RLVKRWRLQV LQVEQQHLRF IQAIQASPNG VLMLDDADQI
EWCNDVAEHH LGLNARRDVR QRITHLIRRP EFVQYLMRQR FDDPLVMRDM GSHKHGVIAV
QILPYGENRK LVLTQDITKL ENTEAMRRDF VANVSHELKT PLTVLTGFLE TVRDLPVSEE
DRRRYVDLML VQSMRMQHIV EDLLALAKLE SDAQAPGYEP IPVNGMIAHL LHDAEALSQG
RHRITSDVDA GVILRGSETE LFSALANLVS NAVRYTPDGG QIGIRLAMDE GHAVFSVSDT
GLGIAPEHIP RLTERFYRVD RSRSRDTGGT GLGLAIVKHV LSRHHADLRI SSEVGRGSVF
RVVFPLDRSG HEAQQVRGGD MPQRAA
//
