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Database: UniProt
Entry: A0A0P0MA22_9BURK
LinkDB: A0A0P0MA22_9BURK
Original site: A0A0P0MA22_9BURK 
ID   A0A0P0MA22_9BURK        Unreviewed;       444 AA.
AC   A0A0P0MA22;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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:ALK89301.1};
GN   ORFNames=L63ED372_02098 {ECO:0000313|EMBL:ALK89301.1};
OS   Limnohabitans sp. 63ED37-2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Limnohabitans.
OX   NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK89301.1, ECO:0000313|Proteomes:UP000059510};
RN   [1] {ECO:0000313|EMBL:ALK89301.1, ECO:0000313|Proteomes:UP000059510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK89301.1,
RC   ECO:0000313|Proteomes:UP000059510};
RA   Ahn J.-H., Kim S.B.;
RT   "Limnohabitans sp. 2 strains.";
RL   Submitted (JUN-2015) 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; CP011774; ALK89301.1; -; Genomic_DNA.
DR   RefSeq; WP_062405897.1; NZ_CP011774.1.
DR   AlphaFoldDB; A0A0P0MA22; -.
DR   STRING; 1678128.L63ED372_02098; -.
DR   KEGG; lih:L63ED372_02098; -.
DR   PATRIC; fig|1678128.3.peg.2087; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000059510; Chromosome.
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.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059510};
KW   Transferase {ECO:0000313|EMBL:ALK89301.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022592}.
FT   TRANSMEM        20..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          212..435
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   444 AA;  49337 MW;  4BDA2F3BB665CAF9 CRC64;
     MFFWLLEMLF WVGLAGTPGW FLGGPFGAVL GALIAVFIYA ATLLWKLDRL ERWLSAPVLR
     QDPPWHGVWR EISVRVQRML RQQEKLAAVH QKQLQDFLQA IQASPNGVIL LDEQARIEWC
     NDTAAAHLGL DAQRDRLQHV VHLVRDPVFA RYFAQDEHTS EAVIEGRASS VVNRQKLSVQ
     LHAYGEGRSL LLTRDITALA QADAMRRDFV ANVSHEIRTP LTVLSGFVET LQSIPLGAEE
     TQQYLHLMSA QSDRMQSLVA DLLMLSQLEG SQLPSTQEKV SLAALMLQVT TEAQAFSDWM
     ANKGQGPVHQ LEFAPVPDVY VMGTRSELLS AVSNLVSNAI RYTPLGGRIQ IHWSSSPEGL
     MFIVKDSGPG IAAEHLPRLA ERFYRVDRSR SRETGGTGLG LAITKHVMQR HGGELRIESV
     VGQGSTFRLV FPQSRVVGES TPAA
//
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