ID C4L8Y6_TOLAT Unreviewed; 197 AA.
AC C4L8Y6;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=Tola_2258 {ECO:0000313|EMBL:ACQ93856.1};
OS Tolumonas auensis (strain DSM 9187 / TA4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Tolumonas.
OX NCBI_TaxID=595494 {ECO:0000313|EMBL:ACQ93856.1, ECO:0000313|Proteomes:UP000009073};
RN [1] {ECO:0000313|Proteomes:UP000009073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA Beller H.;
RT "Complete sequence of Tolumonas auensis DSM 9187.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACQ93856.1, ECO:0000313|Proteomes:UP000009073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RX PubMed=22180815; DOI=10.4056/sigs.2184986;
RA Chertkov O., Copeland A., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P.,
RA Bruce D., Goodwin L., Han C., Tapia R., Saunders E., Schmutz J.,
RA Brettin T., Larimer F., Land M., Hauser L., Spring S., Rohde M.,
RA Kyrpides N.C., Ivanova N., Goker M., Beller H.R., Klenk H.P., Woyke T.;
RT "Complete genome sequence of Tolumonas auensis type strain (TA 4).";
RL Stand. Genomic Sci. 5:112-120(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; CP001616; ACQ93856.1; -; Genomic_DNA.
DR RefSeq; WP_015879324.1; NC_012691.1.
DR AlphaFoldDB; C4L8Y6; -.
DR STRING; 595494.Tola_2258; -.
DR KEGG; tau:Tola_2258; -.
DR eggNOG; COG0576; Bacteria.
DR HOGENOM; CLU_057217_6_0_6; -.
DR OrthoDB; 9789811at2; -.
DR Proteomes; UP000009073; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01151};
KW Reference proteome {ECO:0000313|Proteomes:UP000009073};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000256|RuleBase:RU000639}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 36..70
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 197 AA; 21613 MW; 88A4A750684335C1 CRC64;
MTNQEQVQEP INQETQTADQ QETVAIEGVA IDSAYVVELE QKLEQASSIA AEEKDRALRT
VAEMENLRRR TALDVEKAHK FALEKFVTEL LPVLDNLERT IQVADKQNDA VKPLLEGVEL
TLKSMANSVA KFGVIALDPQ GQAFDPNQHQ AMSMIENGDV APNTVIAVMQ KGYELNGRVI
RPAMVMVSKA PAASAEV
//
