ID   PHOR_KLEPN              Reviewed;         431 AA.
AC   P45608;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Phosphate regulon sensor protein PhoR;
DE            EC=2.7.13.3;
GN   Name=phoR;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
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; M31794; AAA25123.1; -; Genomic_DNA.
DR   PIR; D44753; D44753.
DR   AlphaFoldDB; P45608; -.
DR   SMR; P45608; -.
DR   PRIDE; P45608; -.
DR   BRENDA; 2.7.13.3; 2814.
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   PROSITE; PS50109; HIS_KIN; 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_0000074848"
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          98..166
FT                   /note="PAS"
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;  49461 MW;  EA7166DD2C2D25CE CRC64;
     MLERLSWKRL ALELFLACIP ALILGAFVGH LPWFLLAAVT GLLIWHFWNL MRLSWWLWVD
     RSMTPPPGRG SWEPLLYGLH QMQMRNKKRR RELGSLIKRF RSGAESLPDA VVLTTEEGAI
     FWCNGLAQQI LNLRWPDDSG QNILNLLRYP EFANYLKQRD FSKPLNLVLN NARHLEIRVM
     PYTDKQWLMV ARDVTQMHQL EGARRNFFAN VSHELRTPLT VLQGYLEMMQ EQVLEGATRE
     KALHTMREQT QRMEGLVKQL LTLSRIEAAP ALAMNDRIDV PMMLRVVERE AQTLSQEKQT
     LIFTVDEQLK VLGNEEQLRS AISNLVYNAV NHTPPGTEIR VSWQRTPQGA LFSVEDNGPG
     IAPEHIPLLT ERFYRGDKAR SRQTGGSGLG LAIVKHAVNH HDSRLEIDST VGKGTRFSFL
     LPERLIARND A