GRPE_CHLTR
ID GRPE_CHLTR Reviewed; 190 AA.
AC P36424; O84400;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Protein GrpE {ECO:0000255|HAMAP-Rule:MF_01151};
DE AltName: Full=HSP-70 cofactor {ECO:0000255|HAMAP-Rule:MF_01151};
GN Name=grpE {ECO:0000255|HAMAP-Rule:MF_01151}; OrderedLocusNames=CT_395;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E/UW-5/Cx;
RX PubMed=8045424; DOI=10.1016/0378-1119(94)90322-0;
RA Schmiel D.H., Wyrick P.B.;
RT "Another putative heat-shock gene and aminoacyl-tRNA synthetase gene are
RT located upstream from the grpE-like and dnaK-like genes in Chlamydia
RT trachomatis.";
RL Gene 145:57-63(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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:0000255|HAMAP-
CC Rule:MF_01151}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP-
CC Rule:MF_01151}.
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DR EMBL; L25105; AAA23163.1; -; Genomic_DNA.
DR EMBL; AE001273; AAC67992.1; -; Genomic_DNA.
DR PIR; A71521; A71521.
DR RefSeq; NP_219905.1; NC_000117.1.
DR RefSeq; WP_009872625.1; NC_000117.1.
DR AlphaFoldDB; P36424; -.
DR SMR; P36424; -.
DR STRING; 813.O172_02150; -.
DR EnsemblBacteria; AAC67992; AAC67992; CT_395.
DR GeneID; 884720; -.
DR KEGG; ctr:CT_395; -.
DR PATRIC; fig|272561.5.peg.425; -.
DR HOGENOM; CLU_057217_5_2_0; -.
DR InParanoid; P36424; -.
DR OMA; YAYEKIA; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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 3: Inferred from homology;
KW Chaperone; Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..190
FT /note="Protein GrpE"
FT /id="PRO_0000113771"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 80
FT /note="P -> S (in strain: E/UW-5/Cx)"
FT VARIANT 185
FT /note="S -> G (in strain: E/UW-5/Cx)"
SQ SEQUENCE 190 AA; 21668 MW; 9BB97B8F44AD92B5 CRC64;
MTETPNTSSE EIQTSEPSPD NELQVLQQEN ANLKAELQEQ NDRYLMALAE AENSRKRLQK
ERTEMMQYAV ENALMDFLPP IESMEKALGF ASQTSEEVKN WAIGFQMILQ QFKQIFEEKG
VVEYSSKGEL FNPYLHEAVE IEETTTIPEG TILEEFTKGY KIGDRPIRVA KVKVAKLPAK
GNSDSNEEKE