PHOR_ECOLI
ID PHOR_ECOLI Reviewed; 431 AA.
AC P08400; Q2MC26;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Phosphate regulon sensor protein PhoR;
DE EC=2.7.13.3;
GN Name=phoR; Synonyms=nmpB; OrderedLocusNames=b0400, JW0390;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3550103; DOI=10.1016/0022-2836(86)90275-5;
RA Makino K., Shinagawa H., Amemura M., Nakata A.;
RT "Nucleotide sequence of the phoR gene, a regulatory gene for the phosphate
RT regulon of Escherichia coli.";
RL J. Mol. Biol. 192:549-556(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=2187152; DOI=10.1007/bf00391740;
RA Yamada M., Makino K., Shinagawa H., Nakata A.;
RT "Regulation of the phosphate regulon of Escherichia coli: properties of
RT phoR deletion mutants and subcellular localization of PhoR protein.";
RL Mol. Gen. Genet. 220:366-372(1990).
RN [6]
RP TOPOLOGY.
RX PubMed=8391104; DOI=10.1111/j.1365-2958.1993.tb01571.x;
RA Scholten M., Tomassen J.;
RT "Topology of the PhoR protein of Escherichia coli and functional analysis
RT of internal deletion mutants.";
RL Mol. Microbiol. 8:269-275(1993).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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 {ECO:0000269|PubMed:2187152};
CC Multi-pass membrane protein {ECO:0000269|PubMed:2187152}.
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DR EMBL; X04704; CAA28409.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18124.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73503.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76180.1; -; Genomic_DNA.
DR PIR; A25557; RGECFR.
DR RefSeq; NP_414934.1; NC_000913.3.
DR RefSeq; WP_000893623.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P08400; -.
DR SMR; P08400; -.
DR BioGRID; 4262091; 109.
DR DIP; DIP-10502N; -.
DR IntAct; P08400; 5.
DR STRING; 511145.b0400; -.
DR BindingDB; P08400; -.
DR ChEMBL; CHEMBL4295567; -.
DR jPOST; P08400; -.
DR PaxDb; P08400; -.
DR PRIDE; P08400; -.
DR EnsemblBacteria; AAC73503; AAC73503; b0400.
DR EnsemblBacteria; BAE76180; BAE76180; BAE76180.
DR GeneID; 945044; -.
DR KEGG; ecj:JW0390; -.
DR KEGG; eco:b0400; -.
DR PATRIC; fig|1411691.4.peg.1878; -.
DR EchoBASE; EB0726; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_2_6; -.
DR InParanoid; P08400; -.
DR OMA; TRFWRGS; -.
DR PhylomeDB; P08400; -.
DR BioCyc; EcoCyc:PHOR-MON; -.
DR BioCyc; MetaCyc:PHOR-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:P08400; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IMP:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:EcoCyc.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IDA:EcoCyc.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
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.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphate transport; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Transport; Two-component regulatory system.
FT CHAIN 1..431
FT /note="Phosphate regulon sensor protein PhoR"
FT /id="PRO_0000074846"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..28
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 29..32
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 33..51
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 52..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 96..172
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; 49629 MW; 33883582AF4B883C CRC64;
MLERLSWKRL VLELLLCCLP AFILGAFFGY LPWFLLASVT GLLIWHFWNL LRLSWWLWVD
RSMTPPPGRG SWEPLLYGLH QMQLRNKKRR RELGNLIKRF RSGAESLPDA VVLTTEEGGI
FWCNGLAQQI LGLRWPEDNG QNILNLLRYP EFTQYLKTRD FSRPLNLVLN TGRHLEIRVM
PYTHKQLLMV ARDVTQMHQL EGARRNFFAN VSHELRTPLT VLQGYLEMMN EQPLEGAVRE
KALHTMREQT QRMEGLVKQL LTLSKIEAAP THLLNEKVDV PMMLRVVERE AQTLSQKKQT
FTFEIDNGLK VSGNEDQLRS AISNLVYNAV NHTPEGTHIT VRWQRVPHGA EFSVEDNGPG
IAPEHIPRLT ERFYRVDKAR SRQTGGSGLG LAIVKHAVNH HESRLNIEST VGKGTRFSFV
IPERLIAKNS D
