ID A4JC02_BURVG Unreviewed; 97 AA. AC A4JC02; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 02-SEP-2026, entry version 118. DE RecName: Full=Co-chaperonin GroES {ECO:0000256|HAMAP-Rule:MF_00580}; DE AltName: Full=10 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00580}; DE AltName: Full=Chaperonin-10 {ECO:0000256|HAMAP-Rule:MF_00580}; DE Short=Cpn10 {ECO:0000256|HAMAP-Rule:MF_00580}; GN Name=groES {ECO:0000256|HAMAP-Rule:MF_00580}; GN Synonyms=groS {ECO:0000256|HAMAP-Rule:MF_00580}; GN OrderedLocusNames=Bcep1808_0793 {ECO:0000313|EMBL:ABO53805.1}; OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia OS (strain R1808)). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; OC Burkholderia cepacia complex. OX NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO53805.1, ECO:0000313|Proteomes:UP000002287}; RN [1] {ECO:0000313|EMBL:ABO53805.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G4 {ECO:0000313|EMBL:ABO53805.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Tiedje J., Richardson P.; RT "Complete sequence of Chromosome1 of Burkholderia vietnamiensis G4."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP- CC Rule:MF_00580, ECO:0000256|RuleBase:RU000535}. CC -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. Interacts with the CC chaperonin GroEL. {ECO:0000256|HAMAP-Rule:MF_00580}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00580}. CC -!- SIMILARITY: Belongs to the GroES chaperonin family. CC {ECO:0000256|ARBA:ARBA00006975, ECO:0000256|HAMAP-Rule:MF_00580, CC ECO:0000256|RuleBase:RU000535}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000614; ABO53805.1; -; Genomic_DNA. DR AlphaFoldDB; A4JC02; -. DR SMR; A4JC02; -. DR KEGG; bvi:Bcep1808_0793; -. DR eggNOG; COG0234; Bacteria. DR HOGENOM; CLU_132825_1_0_4; -. DR Proteomes; UP000002287; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:TreeGrafter. DR GO; GO:0044183; F:protein folding chaperone; IEA:InterPro. DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:TreeGrafter. DR CDD; cd00320; cpn10; 1. DR FunFam; 2.30.33.40:FF:000001; 10 kDa chaperonin; 1. DR Gene3D; 2.30.33.40; GroES chaperonin; 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 NCBIfam; NF001527; PRK00364.1-2; 1. DR NCBIfam; NF001529; PRK00364.1-5; 1. DR NCBIfam; NF001531; PRK00364.2-2; 1. DR NCBIfam; NF001533; PRK00364.2-4; 1. DR NCBIfam; NF001534; PRK00364.2-5; 1. DR PANTHER; PTHR10772; 10 KDA HEAT SHOCK PROTEIN; 1. DR PANTHER; PTHR10772:SF58; CO-CHAPERONIN GROES; 1. DR Pfam; PF00166; Cpn10; 1. DR PRINTS; PR00297; CHAPERONIN10. DR SMART; SM00883; Cpn10; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR PROSITE; PS00681; CHAPERONINS_CPN10; 1. PE 3: Inferred from homology; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00580}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00580}; KW Reference proteome {ECO:0000313|Proteomes:UP000002287}. SQ SEQUENCE 97 AA; 10490 MW; BA5E8E4E9207063D CRC64; MNLRPLHDRV IVKRLDQETK TASGIVIPDA AAEKPDQGEV LAIGPGKRDD KGAPIALDVK VGDRVLFGKY AGQTVKVDGQ ELLVMREEDI MAVVNAK //