PHOQ_ECO57
ID PHOQ_ECO57 Reviewed; 486 AA.
AC Q8X739; Q7AF16;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Sensor protein PhoQ;
DE EC=2.7.13.3;
DE EC=3.1.3.-;
DE AltName: Full=Sensor histidine protein kinase/phosphatase PhoQ;
GN Name=phoQ; OrderedLocusNames=Z1858, ECs1601;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Member of the two-component regulatory system PhoP/PhoQ
CC involved in virulence, adaptation to low Mg(2+) environments and the
CC control of acid resistance genes. In low periplasmic Mg(2+), PhoQ
CC functions as a membrane-associated protein kinase that undergoes
CC autophosphorylation and subsequently transfers the phosphate to PhoP,
CC resulting in the expression of PhoP-activated genes (PAG) and
CC repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+),
CC acts as a protein phosphatase that dephosphorylates phospho-PhoP, which
CC results in the repression of PG and may lead to expression of some PRG
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG55955.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG55955.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB35024.1; -; Genomic_DNA.
DR PIR; A99829; A99829.
DR PIR; G85686; G85686.
DR RefSeq; NP_309628.1; NC_002695.1.
DR AlphaFoldDB; Q8X739; -.
DR SMR; Q8X739; -.
DR STRING; 155864.EDL933_1798; -.
DR EnsemblBacteria; AAG55955; AAG55955; Z1858.
DR EnsemblBacteria; BAB35024; BAB35024; ECs_1601.
DR GeneID; 913290; -.
DR KEGG; ece:Z1858; -.
DR KEGG; ecs:ECs_1601; -.
DR PATRIC; fig|386585.9.peg.1701; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_42_0_6; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR Gene3D; 3.30.450.140; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR015014; PhoQ_Sensor.
DR InterPro; IPR038429; PhoQ_Sensor_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08918; PhoQ_Sensor; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Kinase;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..486
FT /note="Sensor protein PhoQ"
FT /id="PRO_0000074838"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..194
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 215..266
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 274..480
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 385..393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 415..420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 434..446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 202
FT /note="Plays a critical role in the switching between
FT kinase and phosphatase states"
FT /evidence="ECO:0000250"
FT MOD_RES 277
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 486 AA; 55291 MW; E2F3BDBACEF1CC0D CRC64;
MKKLLHLFFP LSLRVRFLLA TAAVVLVLSL AYGMVALIGY SVSFDKTTFR LLRGESNLFY
TLAKWENNKL HVELPENIDK QSPTMTLIYD ENGQLLWAQR DVPWLMKMIQ PDWLKSNGFH
EIEADVNDTS LLLSGDHSIQ QQLQEVREDD DDAEMTHSVA VNVYPATSRM PKLTIVVVDT
IPVELKSSYM VWSWFIYVLS ANLLLVIPLL WVAAWWSLRP IEALAKEVRE LEEHNRELLN
PATTRELTSL VRNLNRLLKS ERERYDKYRT TLTDLTHSLK TPLAVLQSTL RSLRSEKMSV
SDAEPVMLEQ ISRISQQIGY YLHRASMHGG TLLSRELHPV APLLDNLTSA LNKVYQRKGV
NISLDISPEI SFVGEQNDFV EVMGNVLDNA CKYCLEFVEI SARQTDEHLY IVVEDDGPGI
PLSKREVIFD RGQRVDTLRP GQGVGLAVAR EITKQYEGKI VAGESMLGGA RMEVIFGRQH
STPKDE
