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GRPE2_BOVIN
ID   GRPE2_BOVIN             Reviewed;         224 AA.
AC   Q0P5N5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=GrpE protein homolog 2, mitochondrial;
DE   AltName: Full=Mt-GrpE#2;
DE   Flags: Precursor;
GN   Name=GRPEL2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) 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; BC119818; AAI19819.1; -; mRNA.
DR   RefSeq; NP_001069142.1; NM_001075674.1.
DR   AlphaFoldDB; Q0P5N5; -.
DR   SMR; Q0P5N5; -.
DR   STRING; 9913.ENSBTAP00000026575; -.
DR   PaxDb; Q0P5N5; -.
DR   PRIDE; Q0P5N5; -.
DR   Ensembl; ENSBTAT00000026575; ENSBTAP00000026575; ENSBTAG00000019950.
DR   GeneID; 514599; -.
DR   KEGG; bta:514599; -.
DR   CTD; 134266; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019950; -.
DR   eggNOG; KOG3003; Eukaryota.
DR   GeneTree; ENSGT00390000005589; -.
DR   HOGENOM; CLU_057217_0_1_1; -.
DR   InParanoid; Q0P5N5; -.
DR   OMA; KQAHNDA; -.
DR   OrthoDB; 1525208at2759; -.
DR   TreeFam; TF105284; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000019950; Expressed in oocyte and 104 other tissues.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
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..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           32..224
FT                   /note="GrpE protein homolog 2, mitochondrial"
FT                   /id="PRO_0000273550"
FT   MOD_RES         141
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TAA5"
SQ   SEQUENCE   224 AA;  25120 MW;  C7DF70D99C8EF0C5 CRC64;
     MAARLLWAVR RRMQPLAAHA ASEGRGWLHP FSTATQRTAG EDCNSEDPPD ELGPSLAERA
     LKLKAVKLEK EVQDLTVRYQ RAVADSENIR RRTQRCVEDA KIFGIQSFCK DLVEVADILE
     KTTECISEET EPADQKLTLE KIFRGLSLLE AKLKSVFAKH GLEKMTPIGD KYDPHEHELI
     CHVPAGVGVQ PGTVAFVRQD GYKLHGRTIR LAQVEVAVES QRRL
 
 
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