ID G8C364_9MOLU Unreviewed; 218 AA.
AC G8C364;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Protein GrpE {ECO:0000256|HAMAP-Rule:MF_01151};
DE AltName: Full=HSP-70 cofactor {ECO:0000256|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000256|HAMAP-Rule:MF_01151,
GN ECO:0000313|EMBL:CCE66762.1};
GN ORFNames=MHM_02440 {ECO:0000313|EMBL:CCE66762.1};
OS Candidatus Mycoplasma haematominutum 'Birmingham 1'.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1116213 {ECO:0000313|EMBL:CCE66762.1};
RN [1] {ECO:0000313|EMBL:CCE66762.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Birmingham 1 {ECO:0000313|EMBL:CCE66762.1};
RA Barker E.N., Darby A.C., Helps C.R., Peters I.R., Hughes M.A.,
RA Radford A.D., Novacco M., Boretti F., Hofmann-Lehmann R., Tasker S.;
RT "Complete genome sequence of Candidatus Mycoplasma haemominutum.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCE66762.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Birmingham 1 {ECO:0000313|EMBL:CCE66762.1};
RA Barker E.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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|HAMAP-
CC Rule:MF_01151}.
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DR EMBL; HE613254; CCE66762.1; -; Genomic_DNA.
DR AlphaFoldDB; G8C364; -.
DR KEGG; mhb:MHM_02440; -.
DR PATRIC; fig|1116213.3.peg.259; -.
DR HOGENOM; CLU_070790_1_0_14; -.
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 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; IPR009012; GrpE_head.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF51064; Head domain of nucleotide exchange factor 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 Stress response {ECO:0000256|HAMAP-Rule:MF_01151,
KW ECO:0000313|EMBL:CCE66762.1}.
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..108
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 25169 MW; AB0805A39554050A CRC64;
MTVENSSKST QGTSEAPEVV EKELVEEESE GEKGIGKKKL SSFFSRRIEE LESKVAKYEA
QEKTLKDELN KKFLSAISKK SEEAIKLIQE KERELERKYL EKFEEQKKFI YESQLSELVD
IVARLEGVVK SASGNREVQN YLAGFRLFLT QFEQLFSSWN IAEIVPRLHQ EFDSEVMESL
ETTPVNEDSL KNKVVHIFSK GYKLHDRVIK LAQVRVGI
//