ID E4SJY8_LACAR Unreviewed; 194 AA.
AC E4SJY8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Protein GrpE {ECO:0000256|HAMAP-Rule:MF_01151, ECO:0000256|RuleBase:RU000639};
DE AltName: Full=HSP-70 cofactor {ECO:0000256|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000256|HAMAP-Rule:MF_01151};
GN OrderedLocusNames=LA2_07075 {ECO:0000313|EMBL:ADQ59340.1};
OS Lactobacillus amylovorus (strain GRL 1112).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=695560 {ECO:0000313|EMBL:ADQ59340.1, ECO:0000313|Proteomes:UP000007033};
RN [1] {ECO:0000313|EMBL:ADQ59340.1, ECO:0000313|Proteomes:UP000007033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GRL 1112 {ECO:0000313|EMBL:ADQ59340.1,
RC ECO:0000313|Proteomes:UP000007033};
RX PubMed=21131492; DOI=10.1128/JB.01365-10;
RA Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.;
RT "Genome sequence of Lactobacillus amylovorus GRL1112.";
RL J. Bacteriol. 193:789-790(2011).
CC -!- FUNCTION: Participates actively in the response to hyperosmotic and
CC heat shock by preventing the aggregation of stress-denatured proteins,
CC in association with DnaK and GrpE. It is the nucleotide exchange factor
CC for DnaK and may function as a thermosensor. Unfolded proteins bind
CC initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK
CC hydrolyzes its bound ATP, resulting in the formation of a stable
CC complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the
CC release of the substrate protein, thus completing the reaction cycle.
CC Several rounds of ATP-dependent interactions between DnaJ, DnaK and
CC GrpE are required for fully efficient folding. {ECO:0000256|HAMAP-
CC Rule:MF_01151, ECO:0000256|RuleBase:RU000639}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|ARBA:ARBA00009054,
CC ECO:0000256|HAMAP-Rule:MF_01151, ECO:0000256|RuleBase:RU004478}.
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DR EMBL; CP002338; ADQ59340.1; -; Genomic_DNA.
DR RefSeq; WP_013438130.1; NC_014724.1.
DR AlphaFoldDB; E4SJY8; -.
DR GeneID; 66524025; -.
DR KEGG; lam:LA2_07075; -.
DR PATRIC; fig|695560.3.peg.1395; -.
DR HOGENOM; CLU_057217_6_3_9; -.
DR Proteomes; UP000007033; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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; GRPE PROTEIN; 1.
DR PANTHER; PTHR21237:SF23; GRPE PROTEIN HOMOLOG, MITOCHONDRIAL; 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|HAMAP-Rule:MF_01151};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000256|RuleBase:RU000639}.
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 194 AA; 22156 MW; F13A7C9BB2BCE6DD CRC64;
MSREEFPSEK DLDKKEKASE PKKAVKKEKA KDEEPKKDKE DQKLAKEIAD LKEKNKDLED
KYLRSEAEIQ NMQARYSKER AQLIKYESQS LAKDVLPAMD NLERALSVKA DDDVSKQLKK
GVQMTLDSLA KAMKDHGIVE IEAEGVKFDP TLHQAVQTVA AENDDQKDHV VQVLQKGYQY
KDRTLRPAMV VVAQ
//
