ID CH10_EHRS3 Reviewed; 98 AA. AC Q2GDC5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 04-NOV-2026, entry version 101. 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=NSE_0643; OS Ehrlichia sennetsu (strain ATCC VR-367 / Miyayama) (Neorickettsia OS sennetsu). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rickettsiales; Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=222891; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-367 / Miyayama; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(2006). 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}. 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; CP000237; ABD46286.1; -; Genomic_DNA. DR RefSeq; WP_011452027.1; NC_007798.1. DR AlphaFoldDB; Q2GDC5; -. DR SMR; Q2GDC5; -. DR STRING; 222891.NSE_0643; -. DR KEGG; nse:NSE_0643; -. DR eggNOG; COG0234; Bacteria. DR HOGENOM; CLU_132825_1_0_5; -. DR OMA; AEEFIIM; -. DR OrthoDB; 9806791at2; -. DR Proteomes; UP000001942; Chromosome. 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; IPR011032; GroES-like_sf. DR NCBIfam; NF001533; groES; 1. DR PANTHER; PTHR10772; 10 KDA HEAT SHOCK PROTEIN; 1. DR PANTHER; PTHR10772:SF63; 20 KDA CHAPERONIN, CHLOROPLASTIC; 1. DR Pfam; PF00166; Cpn10; 1. DR PRINTS; PR00297; CHAPERONIN10. DR SMART; SM00883; Cpn10; 1. DR SUPFAM; SSF50129; GroES-like; 1. PE 3: Inferred from homology; KW Chaperone; Cytoplasm; Reference proteome. FT CHAIN 1..98 FT /note="Co-chaperonin GroES" FT /id="PRO_1000025310" SQ SEQUENCE 98 AA; 10621 MW; 4EE66F4E9D7A0CA8 CRC64; MKVGLKMLHD QVLIRPHEEK DGAGGIYIPD SAKKKPTMGL VVAVGAGAKN SNGTFQPVCV KEGDIVLYRK WAGSEVEHDG VEYVVMKETD IIAIKEGK //