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Entry: A0A0A1VIS8_9BURK
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ID   A0A0A1VIS8_9BURK        Unreviewed;       442 AA.
AC   A0A0A1VIS8;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AVS7_03243 {ECO:0000313|EMBL:GAD23483.1};
OS   Acidovorax sp. MR-S7.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD23483.1};
RN   [1] {ECO:0000313|EMBL:GAD23483.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-S7 {ECO:0000313|EMBL:GAD23483.1};
RX   DOI=10.1128/genomeA.00412-13;
RA   Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT   "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT   Acidovorax sp. Strain MR-S7.";
RL   Genome Announc. 1:e00412-13(2013).
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; DF238947; GAD23483.1; -; Genomic_DNA.
DR   RefSeq; WP_020229302.1; NZ_DF238947.1.
DR   AlphaFoldDB; A0A0A1VIS8; -.
DR   STRING; 1268622.AVS7_03243; -.
DR   eggNOG; COG5002; Bacteria.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000030646; 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   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:GAD23483.1};
KW   Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030646};
KW   Transferase {ECO:0000313|EMBL:GAD23483.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022592}.
FT   DOMAIN          212..439
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   442 AA;  48561 MW;  606CBA44A498F23F CRC64;
     MLLRFLFFFL CQAAGAALGW WQAGPWGAVA GACAAAWVWF AWDLWRGARV LAWMREGDPA
     RAPRLRGMWG EAADRARRLV RQGRLREQAS DARLQEILAA LQASPNGVTL LDAEGRIEWC
     NQMAEEHFGI HFERDALQSI GNLVRDPDFS AYYAGHDFTR DVVLQGRAST PSRPVRISMH
     LHPYGDGRKL LLSRDITALE QAEAMRRDFV ANVSHEIRTP LTVLMGFVET LQTLQLGADE
     RARYLGMMSQ QAQRMHHLVQ DLLTLSRLEG SPLPGLVDWV PVASLLRHCE DEARALSAML
     TQGAPQPHRI AFPTPDEAQA AGQVAGIAAE LQSALANLVN NAVRYTPAGG SITVAWEAGE
     GGGARFSVSD TGPGIAAEHL PRITERFYRV DRSRSRDTGG TGLGLAIVKH VVQRHGGTLH
     VRSVVGQGSV FSVDLPPMRV RR
//
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