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Database: UniProt
Entry: A0A1H7AV47_9PSED
LinkDB: A0A1H7AV47_9PSED
Original site: A0A1H7AV47_9PSED 
ID   A0A1H7AV47_9PSED        Unreviewed;       433 AA.
AC   A0A1H7AV47;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN03159495_4191 {ECO:0000313|EMBL:SEJ69168.1};
OS   Pseudomonas sp. NFR16.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1566248 {ECO:0000313|EMBL:SEJ69168.1, ECO:0000313|Proteomes:UP000199219};
RN   [1] {ECO:0000313|EMBL:SEJ69168.1, ECO:0000313|Proteomes:UP000199219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFR16 {ECO:0000313|EMBL:SEJ69168.1,
RC   ECO:0000313|Proteomes:UP000199219};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNYJ01000005; SEJ69168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7AV47; -.
DR   STRING; 1566248.SAMN03159495_4191; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000199219; 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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR013767; PAS_fold.
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; PF00989; PAS; 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; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SEJ69168.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:SEJ69168.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022592}.
FT   TRANSMEM        12..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          89..150
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          212..429
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   433 AA;  49037 MW;  BB71653D08E503A2 CRC64;
     MNHNWHGTLI RHLLLLVTAS LLAGLISGHY GWCLAIGLGL YLAWTLKQLL RLHDWLRHHK
     PDEPPPDGYG LWGDVFDSIY HLQKRDQRVR GRLQAVIDRV QESTAALRDA VIMLDSEGNL
     EWWNRAAETL LGLKTPQDSG QPVTNLVRHP RFKEYFEHAN YAEPLEIPSP VNDRLRIQML
     ITRYGNNEHL MLVRDVTRIH QLEQMRKDFV ANVSHELRTP LTVICGYLET LLDNVDDVNP
     RWVRALQQMQ QQGGRMQTLL NDLLLLAKLE ATDYPSDNQP VDVPTLLQSI KNDAQALSGS
     KNQQITLDLE SDYSLKGSEA ELRSAFSNLI FNAVKYTPAE GKVRIRWWAD ARGAHLSVQD
     SGIGIDSKHI PRLTERFYRV DSSRASNTGG TGLGLAIVKH VLLRHRATLE INSVPGKGSV
     FICNFAPIQM TKA
//
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