ID   CH602_THEVL             Reviewed;         543 AA.
AC   P0A338; Q57002;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Chaperonin GroEL 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL2 {ECO:0000255|HAMAP-Rule:MF_00600};
OS   Thermostichus vulcanus (Synechococcus vulcanus).
OC   Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX   NCBI_TaxID=32053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8645726; DOI=10.1016/0167-4838(96)00037-4;
RA   Furuki M., Tanaka N., Hiyama T., Nakamoto H.;
RT   "Cloning, characterization and functional analysis of groEL-like gene from
RT   thermophilic cyanobacterium Synechococcus vulcanus, which does not form an
RT   operon with groES.";
RL   Biochim. Biophys. Acta 1294:106-110(1996).
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:0000255|HAMAP-Rule:MF_00600}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC         unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00600};
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: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}.
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DR   EMBL; D86384; BAA13082.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0A338; -.
DR   SMR; P0A338; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
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; 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; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT   CHAIN           1..543
FT                   /note="Chaperonin GroEL 2"
FT                   /id="PRO_0000063574"
FT   BINDING         29..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         86..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         478..480
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   543 AA;  57103 MW;  65171A43BD1CE3E1 CRC64;
     MAKLVAFHEE SRRSLERGIN ALADAVKITL GPKGRNVVLE KKYGAPQIVN DGVTIAKEIE
     LEDAYENTGA QLMREVAAKT NDVVGDGTTT ATVLAQALIR EGLKNVAAGT NPIALKRGME
     KAIKTIVDGI AEVAKPVEGD MIAQVATVSA GNDPEVGAMI SEAMAKVGKD GVITIEESKS
     LQTEMEIVEG MQFDRGYISP YFVTDPERMI VQLNNAYLLL TDKKITSIQD LIPTLERVAR
     SGRPLVIIAE DVEGEALATL VVNKLRGVLN VVAVKAPAFG ERRKAMLQDI AILTGGQVIS
     EEVGLTLEDV ELTMLGEASS VTVTKDTTIL VSEKGNKADI QKRVEQLKQQ LAETDSEYDK
     EKLQERIAKL VGGVAVIKVG AATETELKDR KLRLEDALNA TKAAVAEGIV PGGGVTLLHL
     ASRIDALLPS LSPEEQTGAR IVASALAAPV AQIADNAGAE GAVVVENVRA GDFNYGFNAA
     TGAYEDLVSA GIIDPAKVVR SALQNAGSIA GMVLTTEALV VEKPEPKPAA PANGGMGGMG
     GMM