ID A0A2I1DK26_9PROT Unreviewed; 446 AA.
AC A0A2I1DK26;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B1757_10965 {ECO:0000313|EMBL:PKY10230.1};
OS Acidithiobacillus marinus.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=187490 {ECO:0000313|EMBL:PKY10230.1, ECO:0000313|Proteomes:UP000234329};
RN [1] {ECO:0000313|EMBL:PKY10230.1, ECO:0000313|Proteomes:UP000234329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH {ECO:0000313|EMBL:PKY10230.1,
RC ECO:0000313|Proteomes:UP000234329};
RA Sharmin S., Tokuhisa M., Kanao T., Kamimura K.;
RT "Draft genime sequence of the acidophilic sulfur-oxidizing bacterium
RT Acidithiobacillus sp. SH, isolated from seawater.";
RL Submitted (MAR-2017) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKY10230.1}.
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DR EMBL; MXAV01000040; PKY10230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1DK26; -.
DR InParanoid; A0A2I1DK26; -.
DR OrthoDB; 5288098at2; -.
DR Proteomes; UP000234329; Unassembled WGS sequence.
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 SMART; SM00091; PAS; 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.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PKY10230.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000234329};
KW Transferase {ECO:0000313|EMBL:PKY10230.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022592}.
FT TRANSMEM 32..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..153
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 213..431
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 446 AA; 50332 MW; AB4D9987A1C8C957 CRC64;
MKIFRAWVFP LAVWALIPLF LAADKLRAWS YIPPVIIALV LAAWVAWHRQ QSQSFSAWFR
NPDTQLPPLA GGLWEETFAD GYHWRRDQEA RQRQLSAQIL QLRDALQAMP DVVVLMDERG
QLVWVNPSGI RLLQLQWPDD VGKPLAFWLR TPDLRAFLSG DGPSSMQLSA PADNQIQLEG
VRYPLADAGA LVIFRDVTRI RQLEQVRQDF VANVSHELRS PLTVVRGFLE NLLDGPLADD
EEVGSQLYLM EQQTLRMQSL VEDLLSLARM EAAEAEPERC DTVLISALVM SLLDTLKLSI
TEKNLQVYTE LDNSLGIFAE QVDLTSILRN LLENAIKYTP AGRSITVRWT QEPDGLRLLV
QDTGDGIAAE HLQRITERFY RVDKGRSRRM GGTGLGLAIV RHAVERYHGH LDVRSKIGEG
STFIAQFPPS LARKATESAD IVIKRS
//
