ID   CH101_RHOPA             Reviewed;          98 AA.
AC   P60366;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Co-chaperonin GroES 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=10 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=Chaperonin-10 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE            Short=Cpn10 1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Name=groES1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groS1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   OrderedLocusNames=RPA1141;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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, ECO:0000305}.
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DR   EMBL; BX572596; CAE26584.1; -; Genomic_DNA.
DR   RefSeq; WP_011156705.1; NC_005296.1.
DR   AlphaFoldDB; P60366; -.
DR   SMR; P60366; -.
DR   STRING; 258594.RPA1141; -.
DR   PRIDE; P60366; -.
DR   EnsemblBacteria; CAE26584; CAE26584; RPA1141.
DR   GeneID; 66892162; -.
DR   KEGG; rpa:RPA1141; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_2_0_5; -.
DR   OMA; LGIFEND; -.
DR   PhylomeDB; P60366; -.
DR   BioCyc; RPAL258594:TX73_RS05825-MON; -.
DR   Proteomes; UP000001426; 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; Reference proteome.
FT   CHAIN           1..98
FT                   /note="Co-chaperonin GroES 1"
FT                   /id="PRO_0000174825"
SQ   SEQUENCE   98 AA;  10624 MW;  BABB27A48BBF351C CRC64;
     MAKINFRPLH DRVVVKRIDA ETKTKGGIII PDSAKEKPQE GQVIAVGPGG RDETGKLTPI
     DVKVGDRVLF GKWSGTEIKL DGEELLIMKE SDIMGVVG