ID   GRPE2_PONAB             Reviewed;         225 AA.
AC   Q5R435;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=GrpE protein homolog 2, mitochondrial;
DE   AltName: Full=Mt-GrpE#2;
DE   Flags: Precursor;
GN   Name=GRPEL2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Seems to control the nucleotide-dependent binding of
CC       mitochondrial HSP70 to substrate proteins. Stimulates ATPase activity
CC       of mt-HSP70. May also serve to modulate the interconversion of
CC       oligomeric (inactive) and monomeric (active) forms of mt-HSP70 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Probable component of the PAM complex at least composed of a
CC       mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and
CC       TIMM14/DNAJC19. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
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DR   EMBL; CR861425; CAH93481.1; -; mRNA.
DR   RefSeq; NP_001127040.1; NM_001133568.1.
DR   AlphaFoldDB; Q5R435; -.
DR   SMR; Q5R435; -.
DR   STRING; 9601.ENSPPYP00000017827; -.
DR   GeneID; 100174067; -.
DR   KEGG; pon:100174067; -.
DR   CTD; 134266; -.
DR   eggNOG; KOG3003; Eukaryota.
DR   InParanoid; Q5R435; -.
DR   OrthoDB; 1525208at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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:0051087; F:chaperone binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd00446; GrpE; 1.
DR   Gene3D; 2.30.22.10; -; 1.
DR   Gene3D; 3.90.20.20; -; 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; PTHR21237; 1.
DR   Pfam; PF01025; GrpE; 1.
DR   PRINTS; PR00773; GRPEPROTEIN.
DR   SUPFAM; SSF51064; SSF51064; 1.
DR   SUPFAM; SSF58014; SSF58014; 1.
DR   PROSITE; PS01071; GRPE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           33..225
FT                   /note="GrpE protein homolog 2, mitochondrial"
FT                   /id="PRO_0000043073"
FT   MOD_RES         142
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TAA5"
SQ   SEQUENCE   225 AA;  25463 MW;  089490A18AD9F2B4 CRC64;
     MAVRSLWACR LRVQRLLAWS AAWESKGWPL PFSTATQRTA GEDCRSEDPP DELGPPLAER
     ALRVKAVKLE KEVQDLTVRY QRAVADCENI RRRTQRCVED AKIFGIQSFC KDLVEVADIL
     EKTTECISEE SEPEDQKLTL EKVFRGLLLL EAKLKSVFAK HGLEKLTPIG DKYDPHEHEL
     ICHVPAGVGV QPGTVALVRQ DGYKLHGRTI RLARVEVAVE SQRRL