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Database: UniProt
Entry: G8C364_9MOLU
LinkDB: G8C364_9MOLU
Original site: G8C364_9MOLU 
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
//
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