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Database: UniProt
Entry: A0A238D6B0_THIDL
LinkDB: A0A238D6B0_THIDL
Original site: A0A238D6B0_THIDL 
ID   A0A238D6B0_THIDL        Unreviewed;       454 AA.
AC   A0A238D6B0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=phoR {ECO:0000313|EMBL:SBP88868.1};
GN   ORFNames=THIARS_70488 {ECO:0000313|EMBL:SBP88868.1};
OS   Thiomonas delicata (Thiomonas cuprina).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=364030 {ECO:0000313|EMBL:SBP88868.1, ECO:0000313|Proteomes:UP000214566};
RN   [1] {ECO:0000313|EMBL:SBP88868.1, ECO:0000313|Proteomes:UP000214566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16361 {ECO:0000313|EMBL:SBP88868.1,
RC   ECO:0000313|Proteomes:UP000214566};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; FLMQ01000056; SBP88868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238D6B0; -.
DR   Proteomes; UP000214566; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214566};
KW   Transferase {ECO:0000313|EMBL:SBP88868.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022592}.
FT   DOMAIN          93..151
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          213..432
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   454 AA;  50337 MW;  6CC430067AAA8317 CRC64;
     MRAVFFRLIG VVTLMLAAAG LVGWLAGPLP GVLAASVVAL SVIGQDTAAQ LRLLAWLKWP
     QLDNVPVMRG VWAEVFYRTA RQFRLWETRL AREEDKLRRF IEALQASPNG VILMDASDQI
     DWCNDTAAAH FGLDPQRDLR QHAVHLIRNP EFFGYMGAKR FDEPLLMRRN GARGSLLLSV
     QVISYGDGKK LLLSRDVTQV ERTEAMRRDF VANVSHEIKT PLTVIAGFVE SLRGLDFSAE
     ERERILGLMQ EQSDRMRHLV EDLLTLAHLE GDPHQPAEER LNMRQMVDRL VADARALSGG
     RHHIEASADG GDLRGARTEL VSAFTNLVSN AVRYTPAGGD VRIAWRVTEQ DYGDPVAEFS
     VSDSGIGIAA EHIPRLTERF YRVDRGRSRE SGGTGLGLAI VKHVLLRHQA ELRISSQPGL
     GSTFSVRFPV QRLVLPKAPA APDAPQGDRE SISA
//
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