ID   CH10_ALLVI              Reviewed;          96 AA.
AC   P31295;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 95.
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   Allochromatium vinosum (Chromatium vinosum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=1049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8444812; DOI=10.1128/jb.175.5.1514-1523.1993;
RA   Ferreyra R., Soncini F., Viale A.M.;
RT   "Cloning, characterization, and functional expression in Escherichia coli
RT   of chaperonin (groESL) genes from the phototrophic sulfur bacterium
RT   Chromatium vinosum.";
RL   J. Bacteriol. 175:1514-1523(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-20, AND CHARACTERIZATION.
RX   PubMed=1349470; DOI=10.1016/0003-9861(92)90503-o;
RA   Torres-Ruiz J.A., McFadden B.A.;
RT   "Purification and characterization of chaperonin 10 from Chromatium
RT   vinosum.";
RL   Arch. Biochem. Biophys. 295:172-179(1992).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=9790891; DOI=10.1006/prep.1998.0953;
RA   Dionisi H.M., Viale A.M.;
RT   "Purification and characterization of Chromatium vinosum GroEL and GroES
RT   proteins overexpressed in Escherichia coli cells lacking the endogenous
RT   groESL operon.";
RL   Protein Expr. Purif. 14:275-282(1998).
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; M99443; AAA23318.1; -; Genomic_DNA.
DR   PIR; A47073; A47073.
DR   AlphaFoldDB; P31295; -.
DR   SMR; P31295; -.
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..96
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174733"
SQ   SEQUENCE   96 AA;  10488 MW;  2DF41D3FC96986AC CRC64;
     MNIRPLHDRV VVRRMEEERL SAGGIVIPDS ATEKPIQGEI IAVGHGKILD NGSVRALDVK
     VGDSVLFGKY SGTEVKLDGK EFLVMREEDI MAVVEG