ID A0A0B1YIM5_9RALS Unreviewed; 442 AA.
AC A0A0B1YIM5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PI87_09950 {ECO:0000313|EMBL:KHK56703.1};
OS Ralstonia sp. A12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1217052 {ECO:0000313|EMBL:KHK56703.1, ECO:0000313|Proteomes:UP000030970};
RN [1] {ECO:0000313|EMBL:KHK56703.1, ECO:0000313|Proteomes:UP000030970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A12 {ECO:0000313|EMBL:KHK56703.1,
RC ECO:0000313|Proteomes:UP000030970};
RA Chen J.W., Yin W.F., Chan K.G.;
RT "Draft Genome of Ralstonia A12.";
RL Submitted (NOV-2014) 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:KHK56703.1}.
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DR EMBL; JSZO01000006; KHK56703.1; -; Genomic_DNA.
DR RefSeq; WP_039597541.1; NZ_JSZO01000006.1.
DR AlphaFoldDB; A0A0B1YIM5; -.
DR STRING; 1217052.PI87_09950; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000030970; 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 CDD; cd00130; PAS; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KHK56703.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:KHK56703.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022592}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..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 442 AA; 49840 MW; 1B1AC4FF83CB0073 CRC64;
MNVFWTRFVV FVALMGILTA CLYVFANHVA ALAVLSALLL AMLLYYVYQI QRLWRVLDSP
AYGEIPSALG LWGEVYYRLH RLMKGWRTQV LQVEQQHSRF IQAIQASPNG VLMLDAEDQI
EWCNAVAEEH FGLSAKRDLR QRITHLIRRP EFVRYLARGE FEEPLTMHDV GPHKQSIVSV
QVLPYGEDRK LLVSQDITKL ENTEAMRRDF VANVSHELKT PLTVLSGFLE TVRDIPLPEE
DKKRYLDMMH TQAMRMQHLV EDLLALATLE GNSEPPSVTP VPMQRMMLQL EHDIEALSAG
RHTISMTCDP TVSVCGAELE LLSAFSNLAS NAVRYTPDGG TIRLDWSVRD GHGMFSVTDT
GIGIAPEHIP RLTERFYRVD RSRSRDTGGT GLGLAIVKHV LSRHGGELQV TSEHGKGSTF
RAVFPPERTV VRSVSISDER AA
//
