ID   PHOU_AQUAE              Reviewed;         221 AA.
AC   O67053;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Phosphate-specific transport system accessory protein PhoU homolog;
DE            Short=Pst system accessory protein PhoU homolog;
DE   AltName: Full=PhoU-like phosphate uptake regulator;
GN   Name=phoU; OrderedLocusNames=aq_906;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), IDENTIFICATION BY MASS
RP   SPECTROMETRY, SUGGESTION OF FUNCTION AS CHAPERONE, SUBCELLULAR LOCATION,
RP   AND SUBUNIT.
RX   PubMed=15937186; DOI=10.1128/jb.187.12.4238-4244.2005;
RA   Oganesyan V., Oganesyan N., Adams P.D., Jancarik J., Yokota H.A., Kim R.,
RA   Kim S.H.;
RT   "Crystal structure of the 'PhoU-like' phosphate uptake regulator from
RT   Aquifex aeolicus.";
RL   J. Bacteriol. 187:4238-4244(2005).
CC   -!- FUNCTION: Plays a role in the regulation of phosphate uptake. In this
CC       role, it may bind, possibly as a chaperone, to PhoR, PhoB or a PhoR-
CC       PhoB complex to promote dephosphorylation of phospho-PhoB, or inhibit
CC       formation of the PhoR-PhoB transitory complex (Probable).
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15937186}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15937186}.
CC   -!- SIMILARITY: Belongs to the PhoU family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07012.1; -; Genomic_DNA.
DR   PIR; B70378; B70378.
DR   RefSeq; NP_213615.1; NC_000918.1.
DR   RefSeq; WP_010880553.1; NC_000918.1.
DR   PDB; 1T72; X-ray; 2.90 A; A/B/D/E/F/G=1-221.
DR   PDB; 1T8B; X-ray; 3.23 A; A/B=1-221.
DR   PDBsum; 1T72; -.
DR   PDBsum; 1T8B; -.
DR   AlphaFoldDB; O67053; -.
DR   SMR; O67053; -.
DR   STRING; 224324.aq_906; -.
DR   EnsemblBacteria; AAC07012; AAC07012; aq_906.
DR   KEGG; aae:aq_906; -.
DR   PATRIC; fig|224324.8.peg.707; -.
DR   eggNOG; COG0704; Bacteria.
DR   HOGENOM; CLU_078518_3_0_0; -.
DR   InParanoid; O67053; -.
DR   OMA; WKHGIET; -.
DR   OrthoDB; 1648549at2; -.
DR   EvolutionaryTrace; O67053; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0030643; P:cellular phosphate ion homeostasis; IEA:InterPro.
DR   GO; GO:0010629; P:negative regulation of gene expression; NAS: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; NAS: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   3D-structure; Cytoplasm; Phosphate transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..221
FT                   /note="Phosphate-specific transport system accessory
FT                   protein PhoU homolog"
FT                   /id="PRO_0000155163"
FT   HELIX           1..33
FT                   /evidence="ECO:0007829|PDB:1T72"
FT   HELIX           37..45
FT                   /evidence="ECO:0007829|PDB:1T72"
FT   HELIX           47..68
FT                   /evidence="ECO:0007829|PDB:1T72"
FT   HELIX           72..106
FT                   /evidence="ECO:0007829|PDB:1T72"
FT   HELIX           115..136
FT                   /evidence="ECO:0007829|PDB:1T72"
FT   HELIX           140..170
FT                   /evidence="ECO:0007829|PDB:1T72"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:1T72"
FT   HELIX           175..208
FT                   /evidence="ECO:0007829|PDB:1T72"
SQ   SEQUENCE   221 AA;  25567 MW;  42C83425B0EB5D84 CRC64;
     MKLFKELEET KEQVIKMAKL VQEAIDKATE ALNKQNVELA EEVIKGDDTI DLLEVDIERR
     CIRMIALYQP EAGDLRMIMG IYKIVSDLER MGDEAENIAE RAILLAEEPP LKPYVNINFM
     SEIVKEMVND SVISFIQQDT LLAKKVIEKD DTVDELYHQL ERELMTYVLE DPRNIKRAMH
     LSFVARHYER IADHAENVAE AAIYLSEGEI VKHQHIKEKG E