PHOU_ECOL6
ID PHOU_ECOL6 Reviewed; 247 AA.
AC Q8FBT8;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Phosphate-specific transport system accessory protein PhoU {ECO:0000250|UniProtKB:P0A9K7, ECO:0000312|EMBL:AAN83080.1};
DE Short=Pst system accessory protein PhoU {ECO:0000250|UniProtKB:P0A9K7};
DE AltName: Full=Negative regulator of Pho regulon;
GN Name=phoU {ECO:0000312|EMBL:AAN83080.1}; OrderedLocusNames=c4648;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1] {ECO:0000312|EMBL:AAN83080.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2] {ECO:0000305}
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=CFT073 / ATCC 700928 / UPEC {ECO:0000269|PubMed:16385125};
RX PubMed=16385125; DOI=10.1099/mic.0.28281-0;
RA Buckles E.L., Wang X., Lockatell C.V., Johnson D.E., Donnenberg M.S.;
RT "PhoU enhances the ability of extraintestinal pathogenic Escherichia coli
RT strain CFT073 to colonize the murine urinary tract.";
RL Microbiology 152:153-160(2006).
CC -!- FUNCTION: Part of the phosphate (Pho) regulon, which plays a key role
CC in phosphate homeostasis. Encoded together with proteins of the
CC phosphate-specific transport (Pst) system in the polycistronic pstSCAB-
CC phoU operon. PhoU is essential for the repression of the Pho regulon at
CC high phosphate conditions. In this role, it may bind, possibly as a
CC chaperone, to PhoR, PhoB or a PhoR-PhoB complex to promote
CC dephosphorylation of phospho-PhoB, or inhibit formation of the PhoR-
CC PhoB transitory complex. Is also part of complex networks important for
CC bacterial virulence, tolerance to antibiotics and stress response (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:16385125}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O67053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9K7}.
CC -!- DISRUPTION PHENOTYPE: Has derepressed alkaline phosphate activity,
CC especially under high-phosphate conditions. In single-challenge murine
CC ascending urinary tract infection (UTI) experiments, quantitative
CC cultures of urine, bladder and kidney reveal no significant
CC differences, however in competitive colonization experiments, the
CC mutant is significantly out-competed by the wild-type in kidneys and
CC urine and recovers in lower amount in bladder. In human urine, mutant
CC and wild-type grow comparably when inoculated independently, however,
CC as observed in vivo, wild-type out-competes the mutant in competition
CC growth experiments. {ECO:0000269|PubMed:16385125}.
CC -!- SIMILARITY: Belongs to the PhoU family. {ECO:0000255}.
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DR EMBL; AE014075; AAN83080.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8FBT8; -.
DR SMR; Q8FBT8; -.
DR STRING; 199310.c4648; -.
DR EnsemblBacteria; AAN83080; AAN83080; c4648.
DR KEGG; ecc:c4648; -.
DR eggNOG; COG0704; Bacteria.
DR HOGENOM; CLU_078518_2_1_6; -.
DR OMA; WKHGIET; -.
DR BioCyc; ECOL199310:C4648-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IEA:InterPro.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045936; P:negative regulation of phosphate metabolic process; IMP:UniProtKB.
DR GO; GO:2000186; P:negative regulation of phosphate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.220; -; 2.
DR InterPro; IPR028366; P_transport_PhoU.
DR InterPro; IPR038078; PhoU-like_sf.
DR InterPro; IPR026022; PhoU_dom.
DR PANTHER; PTHR42930; PTHR42930; 1.
DR Pfam; PF01895; PhoU; 2.
DR PIRSF; PIRSF003107; PhoU; 1.
DR TIGRFAMs; TIGR02135; phoU_full; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphate transport; Transport.
FT CHAIN 1..247
FT /note="Phosphate-specific transport system accessory
FT protein PhoU"
FT /id="PRO_0000420872"
SQ SEQUENCE 247 AA; 28193 MW; FE06BE3C3F7285A5 CRC64;
MIQECVMDSL NLNKHISGQF NAELESIRTQ VMTMGGMVEQ QLSDAITAMH NQDSDLAKRV
IEGDKNVNMM EVAIDEACVR IIAKRQPTAS DLRLVMVISK TIAELERIGD VADKICRTAL
EKFSQQHQPL LVSLESLGRH TIQMLHDVLD AFARMDIDEA VRIYREDKKV DQEYEGIVRQ
LMTYMMEDSR TIPSVLTALF CARSIERIGD RCQNICEFIF YYVKGQDFRH VGGDELDKLL
AEKDSDK