PHOU_STRPN
ID PHOU_STRPN Reviewed; 216 AA.
AC P0A3Y7; Q9X4T4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phosphate-specific transport system accessory protein PhoU homolog;
DE Short=Pst system accessory protein PhoU homolog;
GN Name=phoU; OrderedLocusNames=SP_2088;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of the phosphate transport system regulatory protein
RT phoU from Streptococcus pneumoniae.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Plays a role in the regulation of phosphate uptake.
CC {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; AE005672; AAK76148.1; -; Genomic_DNA.
DR PIR; C95244; C95244.
DR RefSeq; WP_001245781.1; NZ_AKVY01000001.1.
DR PDB; 2I0M; X-ray; 2.40 A; A=1-216.
DR PDBsum; 2I0M; -.
DR AlphaFoldDB; P0A3Y7; -.
DR SMR; P0A3Y7; -.
DR STRING; 170187.SP_2088; -.
DR EnsemblBacteria; AAK76148; AAK76148; SP_2088.
DR GeneID; 60232703; -.
DR GeneID; 66807168; -.
DR KEGG; spn:SP_2088; -.
DR eggNOG; COG0704; Bacteria.
DR OMA; DAMYNSL; -.
DR PhylomeDB; P0A3Y7; -.
DR BioCyc; SPNE170187:G1FZB-2173-MON; -.
DR EvolutionaryTrace; P0A3Y7; -.
DR Proteomes; UP000000585; 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: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; -; 1.
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 3D-structure; Cytoplasm; Phosphate transport; Transport.
FT CHAIN 1..216
FT /note="Phosphate-specific transport system accessory
FT protein PhoU homolog"
FT /id="PRO_0000155179"
FT HELIX 5..35
FT /evidence="ECO:0007829|PDB:2I0M"
FT HELIX 39..66
FT /evidence="ECO:0007829|PDB:2I0M"
FT HELIX 74..105
FT /evidence="ECO:0007829|PDB:2I0M"
FT HELIX 117..136
FT /evidence="ECO:0007829|PDB:2I0M"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2I0M"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:2I0M"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:2I0M"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2I0M"
FT HELIX 177..209
FT /evidence="ECO:0007829|PDB:2I0M"
SQ SEQUENCE 216 AA; 24192 MW; 58E2C3ABBE653B4B CRC64;
MRNQFDLELH ELEQSFLGLG QLVLETASKA LLALASKDKE MAELIINKDH AINQGQSAIE
LTCARLLALQ QPQVSDLRFV ISIMSSCSDL ERMGDHMAGI AKAVLQLKEN QLAPDEEQLH
QMGKLSLSML ADLLVAFPLH QASKAISIAQ KDEQIDQYYY ALSKEIIGLM KDQETSIPNG
TQYLYIIGHL ERFADYIANI CERLVYLETG ELVDLN