ID   CH10_RICPU              Reviewed;          95 AA.
AC   C4K2U0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 54.
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};
GN   OrderedLocusNames=RPR_07275;
OS   Rickettsia peacockii (strain Rustic).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=562019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rustic;
RX   PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA   Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT   "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT   with virulent Rickettsia rickettsii: identification of virulence factors.";
RL   PLoS ONE 4:E8361-E8361(2009).
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; CP001227; ACR47885.1; -; Genomic_DNA.
DR   RefSeq; WP_012737041.1; NC_012730.1.
DR   AlphaFoldDB; C4K2U0; -.
DR   SMR; C4K2U0; -.
DR   EnsemblBacteria; ACR47885; ACR47885; RPR_07275.
DR   KEGG; rpk:RPR_07275; -.
DR   HOGENOM; CLU_132825_1_0_5; -.
DR   OMA; KVFYRQW; -.
DR   Proteomes; UP000005015; Chromosome.
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   3: Inferred from homology;
KW   Chaperone; Cytoplasm.
FT   CHAIN           1..95
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_1000212124"
SQ   SEQUENCE   95 AA;  10535 MW;  A398F45294BD5ABE CRC64;
     MSFKPLHDRI AIKPIEQEEK TKGGIIIPDT VKEKPMQGEI VAVGNGIRNK KGEIHPLELK
     VGDKVLYGKW AGTEIEIKGT KLIVMKESDV FGIIN