PHOU_SERMA
ID PHOU_SERMA Reviewed; 243 AA.
AC B6ZCF1;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Phosphate-specific transport system accessory protein PhoU {ECO:0000250|UniProtKB:P0A9K7, ECO:0000312|EMBL:CAR92143.1};
DE Short=Pst system accessory protein PhoU {ECO:0000250|UniProtKB:P0A9K7};
GN Name=phoU {ECO:0000312|EMBL:CAR92143.1};
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1] {ECO:0000312|EMBL:CAR92143.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 39006 / SC 11482 {ECO:0000269|PubMed:12519208};
RX PubMed=12519208; DOI=10.1046/j.1365-2958.2003.03295.x;
RA Slater H., Crow M., Everson L., Salmond G.P.C.;
RT "Phosphate availability regulates biosynthesis of two antibiotics,
RT prodigiosin and carbapenem, in Serratia via both quorum-sensing-dependent
RT and -independent pathways.";
RL Mol. Microbiol. 47:303-320(2003).
RN [2] {ECO:0000312|EMBL:CAR92143.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OPERON STRUCTURE.
RC STRAIN=ATCC 39006 / SC 11482 {ECO:0000269|PubMed:19476633};
RX PubMed=19476633; DOI=10.1186/1471-2180-9-112;
RA Gristwood T., Fineran P.C., Everson L., Williamson N.R., Salmond G.P.;
RT "The PhoBR two-component system regulates antibiotic biosynthesis in
RT Serratia in response to phosphate.";
RL BMC Microbiol. 9:112-112(2009).
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|UniProtKB:O67053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9K7}.
CC -!- SIMILARITY: Belongs to the PhoU family. {ECO:0000255}.
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DR EMBL; FM244836; CAR92143.1; -; Genomic_DNA.
DR STRING; 273526.SMDB11_4138; -.
DR PRIDE; B6ZCF1; -.
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 GO; GO:0019220; P:regulation of phosphate metabolic process; IGC: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 3: Inferred from homology;
KW Cytoplasm; Phosphate transport; Transport.
FT CHAIN 1..243
FT /note="Phosphate-specific transport system accessory
FT protein PhoU"
FT /id="PRO_0000420874"
SQ SEQUENCE 243 AA; 27594 MW; 77791B58400C67E0 CRC64;
MENLNLNKHI SGQFNAELEN IRTQVLSMGG LVEQQLTDAI TAMHNQDSEL ATRVIEGDSK
VNLMEVTIDE ACVRIIAKRQ PTASDLRLVM AIIKTISELE RIGDVADKIC RTALEKFSHQ
HQPLLVSLES LGRHTVQMLH DVLDAFARMD LDEAIRIYRE DKKVDKEYEG IVRQLMTHMM
EDSRTIPSVL TALFCARSIE RIGDRCQNIC EFIFYFVKGQ DVRHMGGDAL EKLLIASDXK
KAK
