PPE15_MYCTU
ID PPE15_MYCTU Reviewed; 391 AA.
AC P9WI31; L0T5J3; Q79FT5; Q7D8Y7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=PPE family protein PPE15 {ECO:0000305};
DE AltName: Full=Mycobacterial perilipin-1 {ECO:0000303|PubMed:27325376};
DE Short=MPER1 {ECO:0000303|PubMed:27325376};
GN Name=PPE15; Synonyms=mper1 {ECO:0000303|PubMed:27325376};
GN OrderedLocusNames=Rv1039c;
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, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27325376; DOI=10.1111/mmi.13422;
RA Daniel J., Kapoor N., Sirakova T., Sinha R., Kolattukudy P.;
RT "The perilipin-like PPE15 protein in Mycobacterium tuberculosis is required
RT for triacylglycerol accumulation under dormancy-inducing conditions.";
RL Mol. Microbiol. 101:784-794(2016).
CC -!- FUNCTION: May play a critical role in the homeostasis of
CC triacylglycerol-containing lipid droplets in M.tuberculosis and
CC influence the entry of the pathogen into a dormant state.
CC {ECO:0000269|PubMed:27325376}.
CC -!- INDUCTION: Up-regulated in tuberculosis dormancy.
CC {ECO:0000305|PubMed:27325376}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant shows a significant decrease in
CC the biosynthesis and accumulation of lipid droplets containing
CC triacylglycerol and in its tolerance to rifampicin.
CC {ECO:0000269|PubMed:27325376}.
CC -!- SIMILARITY: Belongs to the mycobacterial PPE family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43790.1; -; Genomic_DNA.
DR PIR; B70625; B70625.
DR RefSeq; WP_003405368.1; NZ_NVQJ01000098.1.
DR RefSeq; YP_177778.1; NC_000962.3.
DR PDB; 5XFS; X-ray; 2.90 A; B=1-194.
DR PDBsum; 5XFS; -.
DR AlphaFoldDB; P9WI31; -.
DR SMR; P9WI31; -.
DR STRING; 83332.Rv1039c; -.
DR PaxDb; P9WI31; -.
DR DNASU; 888477; -.
DR GeneID; 888477; -.
DR KEGG; mtu:Rv1039c; -.
DR TubercuList; Rv1039c; -.
DR eggNOG; COG5651; Bacteria.
DR OMA; MDIRAGL; -.
DR PhylomeDB; P9WI31; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0052572; P:response to host immune response; IBA:GO_Central.
DR Gene3D; 1.20.1260.20; -; 1.
DR InterPro; IPR022171; PPE_C.
DR InterPro; IPR000030; PPE_family.
DR InterPro; IPR038332; PPE_sf.
DR Pfam; PF00823; PPE; 1.
DR Pfam; PF12484; PPE-SVP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..391
FT /note="PPE family protein PPE15"
FT /id="PRO_0000378477"
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:5XFS"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:5XFS"
FT HELIX 22..55
FT /evidence="ECO:0007829|PDB:5XFS"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:5XFS"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5XFS"
FT HELIX 62..103
FT /evidence="ECO:0007829|PDB:5XFS"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:5XFS"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:5XFS"
FT HELIX 130..161
FT /evidence="ECO:0007829|PDB:5XFS"
SQ SEQUENCE 391 AA; 38081 MW; AFDF3EA4FB195C4F CRC64;
MDFGALPPEI NSARMYAGAG AGPMMAAGAA WNGLAAELGT TAASYESVIT RLTTESWMGP
ASMAMVAAAQ PYLAWLTYTA EAAAHAGSQA MASAAAYEAA YAMTVPPEVV AANRALLAAL
VATNVLGINT PAIMATEALY AEMWAQDALA MYGYAAASGA AGMLQPLSPP SQTTNPGGLA
AQSAAVGSAA ATAAVNQVSV ADLISSLPNA VSGLASPVTS VLDSTGLSGI IADIDALLAT
PFVANIINSA VNTAAWYVNA AIPTAIFLAN ALNSGAPVAI AEGAIEAAEG AASAAAAGLA
DSVTPAGLGA SLGEATLVGR LSVPAAWSTA APATTAGATA LEGSGWTVAA EEAGPVTGMM
PGMASAAKGT GAYAGPRYGF KPTVMPKQVV V