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Database: UniProt
Entry: A0A257DCM2_9BURK
LinkDB: A0A257DCM2_9BURK
Original site: A0A257DCM2_9BURK 
ID   A0A257DCM2_9BURK        Unreviewed;       464 AA.
AC   A0A257DCM2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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:OYT99422.1};
GN   ORFNames=CFE40_06105 {ECO:0000313|EMBL:OYT99422.1};
OS   Burkholderiales bacterium PBB1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=2015563 {ECO:0000313|EMBL:OYT99422.1, ECO:0000313|Proteomes:UP000216950};
RN   [1] {ECO:0000313|EMBL:OYT99422.1, ECO:0000313|Proteomes:UP000216950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBB1 {ECO:0000313|EMBL:OYT99422.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-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:OYT99422.1}.
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DR   EMBL; NKIN01000002; OYT99422.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257DCM2; -.
DR   Proteomes; UP000216950; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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; 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   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.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:OYT99422.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216950};
KW   Transferase {ECO:0000313|EMBL:OYT99422.1};
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..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          216..437
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   464 AA;  50157 MW;  2ABF85D74CD53B13 CRC64;
     MGWLFPRLLA ASTSVLVTGL LGWLVGRASH VPVLGALLGA SLGALGYASL DALRGQRFLK
     WLQSWNGASA PRDSGFWGEV GYRVERSTRS LEQQIEREKV RLEQFLSAIE ASPNGVMLLD
     VNDQIEWCNS VAADHFGLDP QRDRLQPITN LIRAPIFVAY LQAGQFDEAV SFPGPGSRGT
     VSVLIKPYGE SMKLVLSQDI TERERNDSMR RGFVANVSHE IRTPLTVLSG FIETMSSLQL
     TDVERRRVIE LMAQQAQRMQ LLVGDLLTLA QLEGSPRPPA DRWVPVQQLL TQVRAAAEAL
     SAGRHTLVCG SAAMPEGGGD LIAGAEQELH SAIANLVNNA IRYTPSGGAV HVSWVVRADG
     VGELEVRDTG IGIEKEHLPR LTERFYRVDG SRSRDTGGTG LGLSIVKHVV QRHGGELEIR
     SELGKGSSFK LVFPAARVRV ASAASEPEAT VAQPGTEAAL GIAD
//
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