PHOQ_SHIFL
ID PHOQ_SHIFL Reviewed; 486 AA.
AC Q83RR1; Q7C203;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Virulence 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=SF1148, S1231;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
RN [3]
RP FUNCTION.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=11207599; DOI=10.1046/j.1462-5822.2000.00065.x;
RA Moss J.E., Fisher P.E., Vick B., Groisman E.A., Zychlinsky A.;
RT "The regulatory protein PhoP controls susceptibility to the host
RT inflammatory response in Shigella flexneri.";
RL Cell. Microbiol. 2:443-452(2000).
CC -!- FUNCTION: Member of the two-component regulatory system PhoP/PhoQ
CC involved in virulence and adaptation to low Mg(2+) environments. In low
CC periplasmic Mg(2+), PhoQ functions as a membrane-associated protein
CC kinase that undergoes autophosphorylation and subsequently transfers
CC the phosphate to PhoP, which results in the expression of PhoP-
CC activated genes (PAG) and repression of PhoP-repressed genes (PRG). In
CC high periplasmic Mg(2+), acts as a protein phosphatase that
CC dephosphorylates phospho-PhoP, which results in the repression of PAG
CC and may lead to expression of some PRG (By similarity). Necessary for
CC resistance to killing by polymorphonuclear leukocytes (PMNs) and
CC cationic antimicrobial peptides (CAMP) they produce. {ECO:0000250,
CC ECO:0000269|PubMed:11207599}.
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}.
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DR EMBL; AE005674; AAN42765.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16654.1; -; Genomic_DNA.
DR RefSeq; NP_707058.1; NC_004337.2.
DR RefSeq; WP_000735425.1; NZ_WPGW01000001.1.
DR AlphaFoldDB; Q83RR1; -.
DR SMR; Q83RR1; -.
DR STRING; 198214.SF1148; -.
DR EnsemblBacteria; AAN42765; AAN42765; SF1148.
DR EnsemblBacteria; AAP16654; AAP16654; S1231.
DR GeneID; 1024096; -.
DR GeneID; 58390821; -.
DR KEGG; sfl:SF1148; -.
DR KEGG; sfx:S1231; -.
DR PATRIC; fig|198214.7.peg.1349; -.
DR HOGENOM; CLU_000445_42_0_6; -.
DR OMA; TLVFIYD; -.
DR OrthoDB; 692375at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Virulence.
FT CHAIN 1..486
FT /note="Virulence sensor protein PhoQ"
FT /id="PRO_0000074844"
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; 55300 MW; 926D7912A49F4B20 CRC64;
MKKLLRLFFP LSLRVRFLLA TAAVVLVLSL AYGMVALIGY SVSFDKTTFR LLRGESNLFY
TLAQWENNKL 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 YLHRASMRGG TLLSRELHPV APLLDNLTSA LNKVYQRKGV
NISLDISPEI SFVGEQNDFV EVMGNVLDNA CKYCLEFVEI SARQTDEHLY IVVEDDGPGI
PLSKREVIFD RGQRVDTLRP GQGVGLAVAR EITEQYEGKI VAGESMLGGA RMEVIFGRQH
SAPKDE
