ID   CH10_CLAM3              Reviewed;          98 AA.
AC   A5CU64;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=CMM_2568;
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382;
RX   PubMed=18192381; DOI=10.1128/jb.01595-07;
RA   Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA   Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O.,
RA   Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.,
RA   Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O.,
RA   Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT   in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN02651.1; -; Genomic_DNA.
DR   RefSeq; WP_012039257.1; NC_009480.1.
DR   AlphaFoldDB; A5CU64; -.
DR   SMR; A5CU64; -.
DR   STRING; 443906.CMM_2568; -.
DR   PRIDE; A5CU64; -.
DR   EnsemblBacteria; CAN02651; CAN02651; CMM_2568.
DR   GeneID; 56886912; -.
DR   KEGG; cmi:CMM_2568; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_2_0_11; -.
DR   OMA; EVKYSGE; -.
DR   OrthoDB; 1965002at2; -.
DR   Proteomes; UP000001564; 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..98
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_1000025235"
SQ   SEQUENCE   98 AA;  10534 MW;  64525504C8C4F0C3 CRC64;
     MSVSIKPLED RIVIQQVEAE QTTASGLVIP DTAKEKPQEG EVVAVGPGRI DDNGNRVPLD
     VAVGDKVIYS KYGGTEVKYD GQDLLVLSAR DVLAVIER