ID   PHOU_EDWTA              Reviewed;         243 AA.
AC   Q83WB2;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Phosphate-specific transport system accessory protein PhoU {ECO:0000250|UniProtKB:P0A9K7};
DE            Short=Pst system accessory protein PhoU {ECO:0000250|UniProtKB:P0A9K7};
DE   AltName: Full=Repressor protein PhoU {ECO:0000312|EMBL:AAN05785.1};
GN   Name=phoU {ECO:0000312|EMBL:AAN05785.1};
OS   Edwardsiella tarda.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=636;
RN   [1] {ECO:0000312|EMBL:AAN05785.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PPD130/91 {ECO:0000312|EMBL:AAN05785.1};
RX   PubMed=12595451; DOI=10.1128/iai.71.3.1343-1351.2003;
RA   Srinivasa Rao P.S., Lim T.M., Leung K.Y.;
RT   "Functional genomics approach to the identification of virulence genes
RT   involved in Edwardsiella tarda pathogenesis.";
RL   Infect. Immun. 71:1343-1351(2003).
RN   [2] {ECO:0000305}
RP   OPERON STRUCTURE, SUBUNIT, INTERACTION WITH PHOB AND FUR, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=PPD130/91 {ECO:0000269|PubMed:21953460};
RX   PubMed=21953460; DOI=10.1074/jbc.m111.295188;
RA   Chakraborty S., Sivaraman J., Leung K.Y., Mok Y.K.;
RT   "Two-component PhoB-PhoR regulatory system and ferric uptake regulator
RT   sense phosphate and iron to control virulence genes in type III and VI
RT   secretion systems of Edwardsiella tarda.";
RL   J. Biol. Chem. 286:39417-39430(2011).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with phosphate regulon transcriptional
CC       regulatory protein PhoB and ferric uptake regulation protein Fur.
CC       {ECO:0000250|UniProtKB:O67053, ECO:0000269|PubMed:21953460}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9K7}.
CC   -!- INDUCTION: Decreased expression in high concentrations of phosphate and
CC       iron. Transcriptionally regulated by PhoB.
CC       {ECO:0000269|PubMed:21953460}.
CC   -!- DISRUPTION PHENOTYPE: Entirely abolishes the secretion of proteins from
CC       both type III and type VI secretion systems, T3SS and T6SS,
CC       respectively. Transcription of phoB is reduced by about 25% compared
CC       with wild-type. Transcription of esrC is completely abolished.
CC       Transcription of fur is increased. {ECO:0000269|PubMed:21953460}.
CC   -!- SIMILARITY: Belongs to the PhoU family. {ECO:0000255}.
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DR   EMBL; AY090560; AAN05785.1; -; Genomic_DNA.
DR   RefSeq; WP_012850335.1; NZ_LC127084.1.
DR   AlphaFoldDB; Q83WB2; -.
DR   SMR; Q83WB2; -.
DR   STRING; 667121.ET1_13_02010; -.
DR   PRIDE; Q83WB2; -.
DR   GeneID; 58257738; -.
DR   OMA; WKHGIET; -.
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:0045936; P:negative regulation of phosphate metabolic process; ISS: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   GO; GO:0019220; P:regulation of phosphate metabolic process; IEP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
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..243
FT                   /note="Phosphate-specific transport system accessory
FT                   protein PhoU"
FT                   /id="PRO_0000420873"
SQ   SEQUENCE   243 AA;  27809 MW;  89B18EE069F6D491 CRC64;
     MDNLNLNKHT SGQFNAELEY IRTQVMSMGG LVEQQLTDAI TAMHNQDADL ARRVVEGDAK
     VNMMEIAIDE ACVKIIAKRQ PTASDLRLVM AIIKTISELE RIGDVADKIC RTALEKFSQQ
     HQPLLVSLES LGQHTVQMLH DVLDAFARMD LNEAIRIYRE DKKVDQEYEG IVRQLMTYMM
     EDSRTIPSVL TALFCARSIE RIGDRCQNIC EFIFYYVKGQ DFRHIGGDDL EQLLTDHRRV
     DEA