ID   PHOR_SHIDY              Reviewed;         431 AA.
AC   P45609;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Phosphate regulon sensor protein PhoR;
DE            EC=2.7.13.3;
GN   Name=phoR;
OS   Shigella dysenteriae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2556368; DOI=10.1128/jb.171.12.6593-6599.1989;
RA   Lee T.Y., Makino K., Shinagawa H., Amemura M., Nakata A.;
RT   "Phosphate regulon in members of the family Enterobacteriaceae: comparison
RT   of the phoB-phoR operons of Escherichia coli, Shigella dysenteriae, and
RT   Klebsiella pneumoniae.";
RL   J. Bacteriol. 171:6593-6599(1989).
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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M31793; AAA26536.1; -; Genomic_DNA.
DR   PIR; B44753; B44753.
DR   AlphaFoldDB; P45609; -.
DR   SMR; P45609; -.
DR   BRENDA; 2.7.13.3; 5711.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; 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:0046777; P:protein autophosphorylation; IEA:UniProt.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.565.10; -; 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   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; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR02966; phoR_proteo; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphate transport; Phosphoprotein; Transferase;
KW   Transmembrane; Transmembrane helix; Transport;
KW   Two-component regulatory system.
FT   CHAIN           1..431
FT                   /note="Phosphate regulon sensor protein PhoR"
FT                   /id="PRO_0000074850"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..38
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..431
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          96..167
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          210..425
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         213
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   431 AA;  49703 MW;  0D0D84FC268253E0 CRC64;
     MLERLSWKRL VLELLLCCLP AFILGAFFGY LPWFLLASVT GLLIWHLWNL LRLSWWLWVD
     RSMTPPPGRG SWEPLLYGLH QMQLRNKKRR RELGNLIKRF RSGAESLPDA VVLTTEEGSI
     FWCNGLAQQI LGLRWPEDNG QNILNLLRYP EFTQYLKTRD FSRPLNLVLN TVRHLEIRVM
     PYTHKQLLMV ARDVTQMHQL EGARRNFFAN VSHELRMPLT VLQGYLEMMD EQPLEGAVRE
     KALHTMREQT QRMEGLVKQL LTLSKIEAAP TQLLNEKVDV PMMLRVVERE AQTLSQKKQT
     FTFEIDNALK VSGNEDQLRS AISNLVYNAV NHTPEGTHIT VRWQRVPHGA EFSVEDNGPG
     IAPEHIPRLT ERFYRVDKAR SRQTGGSGLG LAIVKHAVNH HESRLNIEST VGKGTRFSFV
     IPERLIAKNS N