CH10_TREPR
ID CH10_TREPR Reviewed; 96 AA.
AC Q8KTR9;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Co-chaperonin GroES {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=Chaperonin-10 {ECO:0000255|HAMAP-Rule:MF_00580};
DE Short=Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580};
GN Name=groES {ECO:0000255|HAMAP-Rule:MF_00580};
GN Synonyms=groS {ECO:0000255|HAMAP-Rule:MF_00580};
OS Tremblaya princeps.
OC Bacteria; Proteobacteria; Betaproteobacteria; Candidatus Tremblaya.
OX NCBI_TaxID=189385;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12088995; DOI=10.1128/aem.68.7.3198-3205.2002;
RA Baumann L., Thao M.L., Hess J.M., Johnson M.W., Baumann P.;
RT "The genetic properties of the primary endosymbionts of mealybugs differ
RT from those of other endosymbionts of plant sap-sucking insects.";
RL Appl. Environ. Microbiol. 68:3198-3205(2002).
CC -!- FUNCTION: Together with the chaperonin GroEL, plays an essential role
CC in assisting protein folding. The GroEL-GroES system forms a nano-cage
CC that allows encapsulation of the non-native substrate proteins and
CC provides a physical environment optimized to promote and accelerate
CC protein folding. GroES binds to the apical surface of the GroEL ring,
CC thereby capping the opening of the GroEL channel. {ECO:0000255|HAMAP-
CC Rule:MF_00580}.
CC -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. Interacts with the
CC chaperonin GroEL. {ECO:0000255|HAMAP-Rule:MF_00580}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580}.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC Rule:MF_00580}.
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DR EMBL; AF481102; AAM75979.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KTR9; -.
DR SMR; Q8KTR9; -.
DR STRING; 1053648.TCP_024; -.
DR PRIDE; Q8KTR9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd00320; cpn10; 1.
DR Gene3D; 2.30.33.40; -; 1.
DR HAMAP; MF_00580; CH10; 1.
DR InterPro; IPR020818; Chaperonin_GroES.
DR InterPro; IPR037124; Chaperonin_GroES_sf.
DR InterPro; IPR011032; GroES-like_sf.
DR PANTHER; PTHR10772; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 1.
DR PRINTS; PR00297; CHAPERONIN10.
DR SMART; SM00883; Cpn10; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm.
FT CHAIN 1..96
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174888"
SQ SEQUENCE 96 AA; 10470 MW; DA81C121187E305E CRC64;
MSKIRPLGDR VVVKRSEDET KTPCGIVIPD SAAEKQDQGT VVALGPGKKD SEGARVPMEV
RLGDRVLFGK YAGQSIKVDD EDLMVMREED IVAVIE