ID   CH10_CERSP              Reviewed;          95 AA.
AC   P25969; Q59772;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 102.
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   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HR;
RX   PubMed=8990302; DOI=10.1128/jb.179.2.487-495.1997;
RA   Lee W.T., Terlesky K.C., Tabita F.R.;
RT   "Cloning and characterization of two groESL operons of Rhodobacter
RT   sphaeroides: transcriptional regulation of the heat-induced groESL
RT   operon.";
RL   J. Bacteriol. 179:487-495(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-23.
RX   PubMed=1678280; DOI=10.1021/bi00247a013;
RA   Terlesky K.C., Tabita F.R.;
RT   "Purification and characterization of the chaperonin 10 and chaperonin 60
RT   proteins from Rhodobacter sphaeroides.";
RL   Biochemistry 30:8181-8186(1991).
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   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00580, ECO:0000305}.
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DR   EMBL; U37369; AAB41335.1; -; Genomic_DNA.
DR   RefSeq; WP_002719473.1; NZ_WTFI01000014.1.
DR   AlphaFoldDB; P25969; -.
DR   SMR; P25969; -.
DR   GeneID; 57469668; -.
DR   GeneID; 67446080; -.
DR   OMA; EVKYSGE; -.
DR   OrthoDB; 1965002at2; -.
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; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1678280"
FT   CHAIN           2..95
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174828"
SQ   SEQUENCE   95 AA;  10197 MW;  F82E1BA1E45BE15B CRC64;
     MAFKPLHDRV LVRRVQSDEK TKGGLIIPDT AKEKPAEGEV VSCGEGARKD SGELIAMSVK
     AGDRVLFGKW SGTEVTIDGA ELLIMKESDI LGILS