ID   CH10_THEBR              Reviewed;          94 AA.
AC   Q60023;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 87.
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   Thermoanaerobacter brockii (Thermoanaerobium brockii).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=29323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RT8.G4;
RX   PubMed=9795109; DOI=10.1016/s0378-1119(98)00382-5;
RA   Truscott K.N., Scopes R.K.;
RT   "Sequence analysis and heterologous expression of the groE genes from
RT   Thermoanaerobacter sp. Rt8.G4.";
RL   Gene 217:15-23(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-42, CHARACTERIZATION, AND MASS SPECTROMETRY.
RC   STRAIN=RT8.G4;
RX   PubMed=7912671; DOI=10.1111/j.1432-1033.1994.tb18866.x;
RA   Truscott K.N., Hoej P.B., Scopes R.K.;
RT   "Purification and characterization of chaperonin 60 and chaperonin 10 from
RT   the anaerobic thermophile Thermoanaerobacter brockii.";
RL   Eur. J. Biochem. 222:277-284(1994).
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   -!- MASS SPECTROMETRY: Mass=10254; Mass_error=0.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:7912671};
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00580, ECO:0000305}.
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DR   EMBL; U56021; AAB00558.1; -; Genomic_DNA.
DR   PIR; S72613; S72613.
DR   AlphaFoldDB; Q60023; -.
DR   SMR; Q60023; -.
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; IPR018369; Chaprnonin_Cpn10_CS.
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.
DR   PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Direct protein sequencing.
FT   CHAIN           1..94
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174882"
SQ   SEQUENCE   94 AA;  10253 MW;  8DBC9C96861DCB84 CRC64;
     MRLKPLGDRV VVKVIQAEEV TKGGVILPGT AKEKPQQGEV VAVGTGEYID GKKVELEVKV
     GDRVIFSKYA GTEVKLDGEE YLLLRESDIL AIIE