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Database: UniProt
Entry: A0A087SI81_AUXPR
LinkDB: A0A087SI81_AUXPR
Original site: A0A087SI81_AUXPR 
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
//
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