ID A0A087SI81_AUXPR Unreviewed; 228 AA.
AC A0A087SI81;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 03-MAY-2023, entry version 23.
DE RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN ORFNames=F751_5976 {ECO:0000313|EMBL:KFM25435.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM25435.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM25435.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM25435.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
CC -!- FUNCTION: Essential component of the PAM complex, a complex required
CC for the translocation of transit peptide-containing proteins from the
CC inner membrane into the mitochondrial matrix in an ATP-dependent
CC manner. {ECO:0000256|RuleBase:RU000640}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU000640}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|ARBA:ARBA00009054,
CC ECO:0000256|RuleBase:RU004478}.
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DR EMBL; KL662118; KFM25435.1; -; Genomic_DNA.
DR RefSeq; XP_011398330.1; XM_011400028.1.
DR AlphaFoldDB; A0A087SI81; -.
DR STRING; 3075.A0A087SI81; -.
DR GeneID; 23617367; -.
DR KEGG; apro:F751_5976; -.
DR eggNOG; KOG3003; Eukaryota.
DR OrthoDB; 36313at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 3.90.20.20; -; 1.
DR Gene3D; 2.30.22.10; Head domain of nucleotide exchange factor GrpE; 1.
DR HAMAP; MF_01151; GrpE; 1.
DR InterPro; IPR000740; GrpE.
DR InterPro; IPR013805; GrpE_coiled_coil.
DR InterPro; IPR009012; GrpE_head.
DR PANTHER; PTHR21237:SF40; CELL CYCLE AND APOPTOSIS REGULATOR PROTEIN 2; 1.
DR PANTHER; PTHR21237; GRPE PROTEIN; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF58014; Coiled-coil domain of nucleotide exchange factor GrpE; 1.
DR SUPFAM; SSF51064; Head domain of nucleotide exchange factor GrpE; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU000640};
KW Mitochondrion {ECO:0000256|RuleBase:RU000640};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 228 AA; 23952 MW; A5F32FBA7F4122B2 CRC64;
MLGTAVPSLG DGASPSTATM DPPSATDAEG LLAEAREVAS TRQVTDAFAA TFPERLEYHL
RAASEGGPAG ADAALSALRD QHLRLAADYD NFRKRSAAER DSARTAARGD TVLELLAVVD
SFEQAAAALS PATDGERKVV AAYDAVYRQL VAAFRRLGVE AVPGEGEPFD PAVHEAIMRE
PAPAGVPDGT VVQEFRKGFR LGDKLLRAGM VKVAFAEDEP TQGGEEEA
//