PG29_MYCTU
ID PG29_MYCTU Reviewed; 370 AA.
AC Q79FP0; F2GET2; I6YAM6; L0T6Y1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Ubiquitin-binding protein Rv1468c {ECO:0000305};
DE AltName: Full=PE-PGRS family protein PE_PGRS29 {ECO:0000305};
GN Name=PE_PGRS29 {ECO:0000312|EMBL:CCP44227.1};
GN OrderedLocusNames=Rv1468c {ECO:0000312|EMBL:CCP44227.1};
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, INTERACTION WITH HOST UBIQUITIN, SUBCELLULAR LOCATION, INDUCTION,
RP DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 1-MET--SER-66; VAL-64 AND
RP LEU-65.
RC STRAIN=H37Rv;
RX PubMed=31036822; DOI=10.1038/s41467-019-09955-8;
RA Chai Q., Wang X., Qiang L., Zhang Y., Ge P., Lu Z., Zhong Y., Li B.,
RA Wang J., Zhang L., Zhou D., Li W., Dong W., Pang Y., Gao G.F., Liu C.H.;
RT "A Mycobacterium tuberculosis surface protein recruits ubiquitin to trigger
RT host xenophagy.";
RL Nat. Commun. 10:1973-1973(2019).
CC -!- FUNCTION: Mediates direct binding of host ubiquitin (Ub) to the
CC mycobacterial surface, which triggers host xenophagy. Interaction
CC between Rv1468c and ubiquitin recruits autophagy receptor p62 to
CC deliver mycobacteria into LC3-associated autophagosomes. It could be a
CC viable evolutionary strategy adopted by M.tuberculosis to maintain
CC long-term intracellular survival through self-controlling its
CC intracellular bacterial loads to avoid excessive host inflammatory
CC immune responses. {ECO:0000269|PubMed:31036822}.
CC -!- SUBUNIT: Interacts directly with host polyubiquitin in a UBA-dependent
CC manner. {ECO:0000269|PubMed:31036822}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:31036822}. Cell surface
CC {ECO:0000269|PubMed:31036822}.
CC -!- INDUCTION: Up-regulated after infection of macrophages.
CC {ECO:0000269|PubMed:31036822}.
CC -!- DOMAIN: Contains a eukaryotic-like ubiquitin-associated (UBA) domain
CC that mediates interaction with host ubiquitin.
CC {ECO:0000269|PubMed:31036822}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant shows enhanced viability, reduced
CC p62 aggregation and reduced colocalization with LC3 and LAMP1 in bone
CC marrow-derived murine macrophages (BMDMs).
CC {ECO:0000269|PubMed:31036822}.
CC -!- SIMILARITY: Belongs to the mycobacterial PE family. PGRS subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44227.1; -; Genomic_DNA.
DR RefSeq; WP_003407494.1; NZ_NVQJ01000004.1.
DR RefSeq; YP_177814.1; NC_000962.3.
DR AlphaFoldDB; Q79FP0; -.
DR STRING; 83332.Rv1468c; -.
DR PaxDb; Q79FP0; -.
DR DNASU; 886556; -.
DR GeneID; 886556; -.
DR KEGG; mtu:Rv1468c; -.
DR PATRIC; fig|83332.111.peg.1634; -.
DR TubercuList; Rv1468c; -.
DR eggNOG; COG3391; Bacteria.
DR OMA; WANGGNK; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR InterPro; IPR000084; PE-PGRS_N.
DR Pfam; PF00934; PE; 1.
PE 1: Evidence at protein level;
KW Cell wall; Reference proteome; Secreted; Virulence.
FT CHAIN 1..370
FT /note="Ubiquitin-binding protein Rv1468c"
FT /id="PRO_5004286516"
FT DOMAIN 1..93
FT /note="PE"
FT /evidence="ECO:0000255"
FT REGION 1..72
FT /note="UBA"
FT /evidence="ECO:0000305|PubMed:31036822"
FT SITE 64..65
FT /note="Important for interaction with host ubiquitin"
FT /evidence="ECO:0000305|PubMed:31036822"
FT MUTAGEN 1..66
FT /note="Missing: Abolishes interaction with host ubiquitin,
FT impairs host xenophagy and increases bacterial loads in
FT mice with enhanced inflammatory responses."
FT /evidence="ECO:0000269|PubMed:31036822"
FT MUTAGEN 64
FT /note="V->G: Reduces interaction with host ubiquitin."
FT /evidence="ECO:0000269|PubMed:31036822"
FT MUTAGEN 65
FT /note="L->G: Reduces interaction with host ubiquitin. Shows
FT enhanced viability, reduced p62 aggregation and reduced
FT colocalization with LC3 and LAMP1 in BMDMs."
FT /evidence="ECO:0000269|PubMed:31036822"
SQ SEQUENCE 370 AA; 32216 MW; D46B252C49CEDB03 CRC64;
MSFVVANTEF VSGAAGNLAR LGSMISAANS AAAAQTTAVA AAGADEVSAA VAALFGAHGQ
TYQVLSAQAA AFHSQFVQAL SGGAQAYAAA EATNFGPLQP LFDVINAPTL ALLNRPLIGN
GADGTAANPN GQAGGLLIGN GGNGFSPAAG PGGNGGAAGL LGHGGNGGVG ALGANGGAGG
TGGWLFGNGG AGGNSGGGGG AGGIGGSAVL FGAGGAGGIS PNGMGAGGSG GNGGLFFGNG
GAGASSFLGG GGAGGRAFLF GDGGAGGAAL SAGSAGRGGD AGFFYGNGGA GGSGAGGASS
AHGGAGGQAG LFGNGGEGGD GGALGGNGGN GGNAQLIGNG GDGGDGGGAG APGLGGRGGL
LLGLPGANGT
