PHOU_SHIFL
ID PHOU_SHIFL Reviewed; 241 AA.
AC P0A9K8; P07656;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Phosphate-specific transport system accessory protein PhoU;
DE Short=Pst system accessory protein PhoU;
GN Name=phoU; OrderedLocusNames=SF3731, S4041;
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).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PhoU family. {ECO:0000305}.
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DR EMBL; AE005674; AAN45177.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP19021.1; -; Genomic_DNA.
DR RefSeq; NP_709470.2; NC_004337.2.
DR RefSeq; WP_000377786.1; NZ_WPGW01000131.1.
DR AlphaFoldDB; P0A9K8; -.
DR SMR; P0A9K8; -.
DR STRING; 198214.SF3731; -.
DR EnsemblBacteria; AAN45177; AAN45177; SF3731.
DR EnsemblBacteria; AAP19021; AAP19021; S4041.
DR GeneID; 1026175; -.
DR GeneID; 66672376; -.
DR KEGG; sfl:SF3731; -.
DR KEGG; sfx:S4041; -.
DR PATRIC; fig|198214.7.peg.4404; -.
DR HOGENOM; CLU_078518_2_1_6; -.
DR OMA; WKHGIET; -.
DR OrthoDB; 1648549at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; 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 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 3: Inferred from homology;
KW Cytoplasm; Phosphate transport; Reference proteome; Transport.
FT CHAIN 1..241
FT /note="Phosphate-specific transport system accessory
FT protein PhoU"
FT /id="PRO_0000155178"
SQ SEQUENCE 241 AA; 27417 MW; 29843C1C3827FACD CRC64;
MDSLNLNKHI SGQFNAELES IRTQVMTMGG MVEQQLSDAI TAMHNQDSDL AKRVIEGDKN
VNMMEVAIDE ACVRIIAKRQ PTASDLRLVM VISKTIAELE RIGDVADKIC RTALEKFSQQ
HQPLLVSLES LGRHTIQMLH DVLDAFARMD IDEAVRIYRE DKKVDQEYEG IVRQLMTYMM
EDSRTIPSVL TALFCARSIE RIGDRCQNIC EFIFYYVKGQ DFRHVGGDEL DKLLAGKDSD
K