ID CH60_SERRU Reviewed; 539 AA. AC O66202; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 07-APR-2021, entry version 82. DE RecName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=GroEL protein {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=Protein Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600}; DE Flags: Fragment; GN Name=groL {ECO:0000255|HAMAP-Rule:MF_00600}; GN Synonyms=groEL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA; OS Serratia rubidaea (Serratia marinorubra). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=61652; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=JCM 1240; RX PubMed=12501307; DOI=10.2323/jgam.43.355; RA Harada H., Ishikawa H.; RT "Phylogenetical relationship based on groE genes among phenotypically RT related Enterobacter, Pantoea, Klebsiella, Serratia, and Erwinia species."; RL J. Gen. Appl. Microbiol. 43:355-361(1997). CC -!- FUNCTION: Prevents misfolding and promotes the refolding and proper CC assembly of unfolded polypeptides generated under stress conditions. CC {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of 7 CC subunits. {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000255|HAMAP-Rule:MF_00600}. 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; AB008143; BAA25219.1; -; Genomic_DNA. DR SMR; O66202; -. DR PRIDE; O66202; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0042026; P:protein refolding; IEA:InterPro. DR CDD; cd03344; GroEL; 1. DR Gene3D; 1.10.560.10; -; 1. DR Gene3D; 3.30.260.10; -; 1. DR Gene3D; 3.50.7.10; -; 1. DR HAMAP; MF_00600; CH60; 1. DR InterPro; IPR018370; Chaperonin_Cpn60_CS. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/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; SSF48592; SSF48592; 1. DR SUPFAM; SSF52029; SSF52029; 1. DR SUPFAM; SSF54849; SSF54849; 1. DR TIGRFAMs; TIGR02348; GroEL; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding. FT CHAIN 1..>539 FT /note="60 kDa chaperonin" FT /id="PRO_0000063526" FT NON_TER 539 SQ SEQUENCE 539 AA; 56640 MW; CE447B657515D4F0 CRC64; MAAKDVKFGN DARVKMLNGV NILADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAIV NEGLKAVAAG MNPMDLKRGI DKAVIAAVEE LKKLSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMEKVG KEGVITVEEG TGLQDELDVV EGMQFDRGYL SPYFINKPET GSVELESPFI LLADKKVSNI RELLPVLEAV AKAGKPLLIV AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTAGTV ISEEIGMELE KATLEDLGQA KRVVINKDTT IIIDGIGDEA TIQGRVAQIR QQIEEATSDY DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI RVASKIAELK GDNEDQNVGI KVALRAMEAP LRQIVINAGE EASVIANSVK AGEGSYGYNA YSEEYGDMIG MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKEDKA DMGAAGMGG //