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 08-NOV-2023, entry version 121.
DE RecName: Full=Phosphate regulon sensor protein PhoR;
DE EC=2.7.13.3;
GN Name=phoR;
OS Shigella dysenteriae.
OC Bacteria; Pseudomonadota; 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.
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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: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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16952; HATPase_EcPhoR-like; 1.
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 NCBIfam; TIGR00229; sensory_box; 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 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
//
