ATG5_BEAB2
ID ATG5_BEAB2 Reviewed; 269 AA.
AC J5JH39; G9JKB6;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Autophagy-related protein 5 {ECO:0000303|PubMed:23197175};
GN Name=ATG5 {ECO:0000303|PubMed:23197175}; ORFNames=BBA_08188;
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ARSEF 2860;
RX PubMed=23197175; DOI=10.1099/mic.0.062646-0;
RA Zhang L., Wang J., Xie X.Q., Keyhani N.O., Feng M.G., Ying S.H.;
RT "The autophagy gene BbATG5, involved in the formation of the autophagosome,
RT contributes to cell differentiation and growth but is dispensable for
RT pathogenesis in the entomopathogenic fungus Beauveria bassiana.";
RL Microbiology 159:243-252(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860;
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y.,
RA St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
RN [3]
RP INDUCTION.
RX PubMed=28557308; DOI=10.1111/1462-2920.13803;
RA Chu Z.J., Sun H.H., Zhu X.G., Ying S.H., Feng M.G.;
RT "Discovery of a new intravacuolar protein required for the autophagy,
RT development and virulence of Beauveria bassiana.";
RL Environ. Microbiol. 19:2806-2818(2017).
CC -!- FUNCTION: Involved in cytoplasm to vacuole transport (Cvt) and
CC autophagic vesicle formation (By similarity). Autophagy is essential
CC for maintenance of amino acid levels and protein synthesis under
CC nitrogen starvation (By similarity). Required for selective autophagic
CC degradation of the nucleus (nucleophagy) (By similarity). Also required
CC for mitophagy, which eliminates defective or superfluous mitochondria
CC in order to fulfill cellular energy requirements and prevent excess ROS
CC production (By similarity). Conjugation with ATG12, through a
CC ubiquitin-like conjugating system involving ATG7 as an E1-like
CC activating enzyme and ATG10 as an E2-like conjugating enzyme, is
CC essential for its function (By similarity). The ATG12-ATG5 conjugate
CC acts as an E3-like enzyme which is required for lipidation of ATG8 and
CC ATG8 association to the vesicle membranes (By similarity). ATG12-ATG5
CC rearranges the ATG3 catalytic center and enhances its E2 activity (By
CC similarity). Required for proper vegetative growth, asexual/sexual
CC reproduction, but, unlike several plant and animal pathogenic fungi,
CC where ATG5 is required for infection, in B.bassiana it is dispensable
CC for pathogenesis (PubMed:23197175). {ECO:0000250|UniProtKB:Q12380,
CC ECO:0000269|PubMed:23197175}.
CC -!- SUBUNIT: Conjugated with ATG12 (By similarity). The ATG5-ATG12
CC conjugate forms a complex with several units of ATG16 (By similarity).
CC The ATG12-ATG5 conjugate associates also with ATG3 (By similarity).
CC {ECO:0000250|UniProtKB:Q12380}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q12380}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q12380}. Note=Localizes to the isolation
CC membrane (IM), a membrane sac which is generated from the pre-
CC autophagosomal structure (PAS) (By similarity). Ultimately, the IM
CC expands to become a mature autophagosome (By similarity). Localizes
CC also to a dot at the junction between the IM and the vacuolar membrane,
CC termed the vacuole-IM contact site (VICS) (By similarity). Correct
CC localization to the PAS requires ATG21 (By similarity).
CC {ECO:0000250|UniProtKB:Q12380}.
CC -!- INDUCTION: Expression is reduced when the vacuolar protein VLP4 is
CC absent (PubMed:28557308). {ECO:0000269|PubMed:28557308}.
CC -!- PTM: Conjugated to ATG12; which is essential for autophagy (By
CC similarity). Conjugation with ATG12 involves ATG7 as an E1-like
CC activating enzyme and ATG10 as an E2-like conjugating enzyme (By
CC similarity). {ECO:0000250|UniProtKB:Q12380}.
CC -!- DISRUPTION PHENOTYPE: Blocks autophagy and displays increased
CC sensitivity to nutrient limitation, with decreased conidial
CC germination, growth and sporulation (PubMed:23197175). Leads only to a
CC modest decrease in virulence (PubMed:23197175).
CC {ECO:0000269|PubMed:23197175}.
CC -!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
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DR EMBL; JN837483; AET98917.1; -; mRNA.
DR EMBL; JX392329; AFS59909.1; -; Genomic_DNA.
DR EMBL; JH725181; EJP62801.1; -; Genomic_DNA.
DR RefSeq; XP_008601507.1; XM_008603285.1.
DR AlphaFoldDB; J5JH39; -.
DR SMR; J5JH39; -.
DR STRING; 655819.J5JH39; -.
DR EnsemblFungi; EJP62801; EJP62801; BBA_08188.
DR GeneID; 19891200; -.
DR HOGENOM; CLU_051894_2_0_1; -.
DR InParanoid; J5JH39; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.246.190; -; 1.
DR Gene3D; 3.10.20.620; -; 1.
DR InterPro; IPR007239; Atg5.
DR InterPro; IPR042526; Atg5_HR.
DR InterPro; IPR042527; Atg5_UblA_dom.
DR PANTHER; PTHR13040; PTHR13040; 1.
DR Pfam; PF04106; APG5; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Isopeptide bond; Membrane; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..269
FT /note="Autophagy-related protein 5"
FT /id="PRO_0000443877"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ATG12)"
FT /evidence="ECO:0000250|UniProtKB:Q12380"
SQ SEQUENCE 269 AA; 29457 MW; 6711445C77108388 CRC64;
MSAPISQALW DARIPLLITH PLAPTTPFIT SIPRFSYLAL LLPRLSAFFN TPCSSFHFED
VVLRNLPVGL LVDLYQPSLP WRLIVNDGVS WDISDTFLNA AKEADFIRNG NANQIMKLSK
DDTRQLWHAV IDNDLAAFSR INNRLLNAPT ALKHVPMRIY LPLAPGGSAG GDVGEPTVDQ
QQGGGDASAA GAFKIIQSLV QPLGADRRPR LLGQVLRETM PKLFPSSRDP VMANVLLHGV
AVPFNAPLAD LMREAAYFDG WLSFVVVVL
