ID Q2TPL4_9RICK Unreviewed; 290 AA. AC Q2TPL4; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 14-DEC-2022, entry version 58. DE RecName: Full=60 kDa chaperonin {ECO:0000256|RuleBase:RU000419}; DE Flags: Fragment; GN Name=groEL {ECO:0000313|EMBL:AAW52263.1}; OS Wolbachia endosymbiont of Drosophila simulans. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=77038 {ECO:0000313|EMBL:AAW52263.1}; RN [1] {ECO:0000313|EMBL:AAW52263.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16339946; DOI=10.1099/mic.0.28313-0; RA Casiraghi M., Bordenstein S.R., Baldo L., Lo N., Beninati T., RA Wernegreen J.J., Werren J.H., Bandi C.; RT "Phylogeny of Wolbachia pipientis based on gltA, groEL and ftsZ gene RT sequences: clustering of arthropod and nematode symbionts in the F RT supergroup, and evidence for further diversity in the Wolbachia tree."; RL Microbiology 151:4015-4022(2005). RN [2] {ECO:0000313|EMBL:AAW52263.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16267140; DOI=10.1093/molbev/msj049; RA Baldo L., Bordenstein S., Wernegreen J.J., Werren J.H.; RT "Widespread recombination throughout Wolbachia genomes."; RL Mol. Biol. Evol. 23:437-449(2006). CC -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential CC role in assisting protein folding. The GroEL-GroES system forms a nano- CC cage that allows encapsulation of the non-native substrate proteins and CC provides a physical environment optimized to promote and accelerate CC protein folding. {ECO:0000256|RuleBase:RU000419}. CC -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric CC rings stacked back-to-back. Interacts with the co-chaperonin GroES. CC {ECO:0000256|RuleBase:RU000419}. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000256|ARBA:ARBA00006607, ECO:0000256|RuleBase:RU000418}. 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; AY714800; AAW52263.1; -; Genomic_DNA. DR AlphaFoldDB; Q2TPL4; -. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0042026; P:protein refolding; IEA:InterPro. DR Gene3D; 1.10.560.10; -; 1. DR Gene3D; 3.30.260.10; -; 1. DR Gene3D; 3.50.7.10; -; 1. DR InterPro; IPR001844; Cpn60/GroEL. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. PE 3: Inferred from homology; KW Chaperone {ECO:0000256|ARBA:ARBA00023186}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAW52263.1" FT NON_TER 290 FT /evidence="ECO:0000313|EMBL:AAW52263.1" SQ SEQUENCE 290 AA; 30992 MW; E228A799D31EDCDD CRC64; VAAMVDSTVG ATAGPRGNTI GISKPYGGPE VTKDGYKVMK GIKPEKPLHS AIVSTIAQSA SQCNDKVGDG TTTCSILTSN MIMEASKSIA AGNDRICIKN GIQKAKDVIL KEITSMSRTI SLEKMDEVAQ VAIISANGDK DIGNSIADAV KKVGKEGVIT VEESKGSKEL EVELTTGMQF DRGYLSPYFV TNNEKMSVEL DDPYLLITEK KLNIIQPLLP ILEAIFKSGK PLFIIAEDVE GEALSTLVIN KLRGLKVAAV KAPGFGDRRK EMLEDIAALT GAKYVIKDEL //