ID   B4ECT8_BURCJ            Unreviewed;        97 AA.
AC   B4ECT8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 105.
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=groES1 {ECO:0000313|EMBL:CAR53470.1}, groS
GN   {ECO:0000256|HAMAP-Rule:MF_00580}, groS1
GN   {ECO:0000313|EMBL:CAR53470.1};
GN   ORFNames=BCAL3147 {ECO:0000313|EMBL:CAR53470.1};
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia;
OC   Burkholderia cepacia complex.
OX   NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR53470.1, ECO:0000313|Proteomes:UP000001035};
RN   [1] {ECO:0000313|EMBL:CAR53470.1, ECO:0000313|Proteomes:UP000001035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC   CF5610 {ECO:0000313|Proteomes:UP000001035};
RX   PubMed=18931103; DOI=10.1128/JB.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(2009).
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}.
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DR   EMBL; AM747720; CAR53470.1; -; Genomic_DNA.
DR   RefSeq; WP_004186661.1; NC_011000.1.
DR   AlphaFoldDB; B4ECT8; -.
DR   SMR; B4ECT8; -.
DR   GeneID; 305377996; -.
DR   GeneID; 99792688; -.
DR   KEGG; bcj:BCAL3147; -.
DR   eggNOG; COG0234; Bacteria.
DR   HOGENOM; CLU_132825_1_0_4; -.
DR   BioCyc; BCEN216591:G1G1V-3490-MONOMER; -.
DR   Proteomes; UP000001035; 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:UP000001035}.
SQ   SEQUENCE   97 AA;  10490 MW;  BA5E8E4E9207063D CRC64;
     MNLRPLHDRV IVKRLDQETK TASGIVIPDA AAEKPDQGEV LAIGPGKRDD KGAPIALDVK
     VGDRVLFGKY AGQTVKVDGQ ELLVMREEDI MAVVNAK
//