PHOU2_MYCTU
ID PHOU2_MYCTU Reviewed; 213 AA.
AC P9WI95; L0T6J6; O53833; P65720;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Phosphate-specific transport system accessory protein PhoU homolog 2;
DE Short=Pst system accessory protein PhoU homolog 2;
GN Name=phoU2; Synonyms=phoY2; OrderedLocusNames=Rv0821c; ORFNames=MTV043.13c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION IN TOLERANCE TO ANTIBIOTICS, DISRUPTION PHENOTYPE, AND POTENTIAL
RP DRUG TARGET.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20360062; DOI=10.1093/jac/dkq103;
RA Shi W., Zhang Y.;
RT "PhoY2 but not PhoY1 is the PhoU homologue involved in persisters in
RT Mycobacterium tuberculosis.";
RL J. Antimicrob. Chemother. 65:1237-1242(2010).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Plays a role in the regulation of phosphate uptake. In this
CC role, it may bind, possibly as a chaperone, to PhoR, PhoP or a PhoR-
CC PhoP complex to promote dephosphorylation of phospho-PhoP, or inhibit
CC formation of the PhoR-PhoP transitory complex (By similarity).
CC Important for tolerance to antibiotics. {ECO:0000250,
CC ECO:0000269|PubMed:20360062}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Defective in persistence phenotype shown by
CC increased susceptibility to tuberculosis (TB) drugs rifampicin and
CC pyrazinamide in both minimum inhibitory concentration (MIC) testing and
CC drug exposure assays. The MICs of rifampicin and pyrazinamide decreased
CC 4-fold and 2-fold, respectively. Reduced persistence in the mouse model
CC of TB infection. Mutant was less able to survive and persist in the
CC mouse lungs and spleens as shown by an about 10- to 30-fold decrease in
CC colony forming unit (cfu) counts compared with the virulent strain.
CC {ECO:0000269|PubMed:20360062}.
CC -!- PHARMACEUTICAL: May be a drug target for designing new drugs that kill
CC persister bacteria for more effective control of bacterial infections.
CC -!- SIMILARITY: Belongs to the PhoU family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43569.1; -; Genomic_DNA.
DR PIR; E70810; E70810.
DR RefSeq; NP_215336.1; NC_000962.3.
DR RefSeq; WP_003404314.1; NZ_NVQJ01000066.1.
DR AlphaFoldDB; P9WI95; -.
DR SMR; P9WI95; -.
DR STRING; 83332.Rv0821c; -.
DR PaxDb; P9WI95; -.
DR DNASU; 885270; -.
DR GeneID; 45424784; -.
DR GeneID; 885270; -.
DR KEGG; mtu:Rv0821c; -.
DR TubercuList; Rv0821c; -.
DR eggNOG; COG0704; Bacteria.
DR OMA; WKHGIET; -.
DR PhylomeDB; P9WI95; -.
DR Proteomes; UP000001584; 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:0022611; P:dormancy process; IDA:MTBBASE.
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:0046677; P:response to antibiotic; IMP:UniProtKB.
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 Cytoplasm; Pharmaceutical; Phosphate transport; Reference proteome;
KW Transport.
FT CHAIN 1..213
FT /note="Phosphate-specific transport system accessory
FT protein PhoU homolog 2"
FT /id="PRO_0000155173"
SQ SEQUENCE 213 AA; 23514 MW; D2EDD9A9968AEA19 CRC64;
MRTAYHEQLS ELSERLGEMC GLAGIAMERA TQALLQADLV LAEQVISDHE KIATLSARAE
ESAFVLLALQ APVAGDLRAI VSAIQMVADI DRMGALALHV AKIARRRHPQ HALPEEVNGY
FAEMGRVAVE LGNSAQEVVL SHDPEKAAQI REEDDAMDDL HRHLFTVLMD REWKHGVAAA
VDVTLLSRFY ERFADHAVEV ARRVIFQATG AFP
