ID   CH10_CYAPA              Reviewed;         103 AA.
AC   Q37761;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=groES1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groES-A, groS-A, groS1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   and
GN   Name=groES2 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groES-B, groS-B, groS2 {ECO:0000255|HAMAP-Rule:MF_00580};
OS   Cyanophora paradoxa.
OG   Plastid; Cyanelle.
OC   Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX   NCBI_TaxID=2762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA   Bryant D.A.;
RT   "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL   Plant Mol. Biol. Rep. 13:327-332(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA   Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA   Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT   "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT   genetic complexity of a primitive plastid.";
RL   (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL   (eds.);
RL   Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
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: Plastid, cyanelle.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00580, ECO:0000305}.
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DR   EMBL; U30821; AAA81173.1; -; Genomic_DNA.
DR   EMBL; U30821; AAA81293.1; -; Genomic_DNA.
DR   PIR; T06830; T06830.
DR   RefSeq; NP_043142.1; NC_001675.1.
DR   RefSeq; NP_043262.1; NC_001675.1.
DR   AlphaFoldDB; Q37761; -.
DR   SMR; Q37761; -.
DR   GeneID; 801546; -.
DR   GeneID; 801651; -.
DR   GO; GO:0009842; C:cyanelle; 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   3: Inferred from homology;
KW   Chaperone; Cyanelle; Plastid.
FT   CHAIN           1..103
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174915"
SQ   SEQUENCE   103 AA;  11240 MW;  FF768479C0A90520 CRC64;
     MATVTLNVKT VRPLGERVLV KVSQSEEKTA GGILLPDTVK EKPQIGEIIA EGPGRRNDDG
     SFQPLEVTVN SKVLYSKYAG TDIKLENEEY VLLSEKDILA IIA