ID   CH602_STRAL             Reviewed;         540 AA.
AC   Q00768;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 98.
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};
DE   AltName: Full=HSP56;
GN   Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL2 {ECO:0000255|HAMAP-Rule:MF_00600};
OS   Streptomyces albus G.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1682304; DOI=10.1128/jb.173.22.7382-7386.1991;
RA   Mazodier P., Guglielmi G., Davies J., Thompson C.J.;
RT   "Characterization of the groEL-like genes in Streptomyces albus.";
RL   J. Bacteriol. 173:7382-7386(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-11.
RX   PubMed=1682303; DOI=10.1128/jb.173.22.7374-7381.1991;
RA   Guglielmi G., Mazodier P., Thompson C.J., Davies J.;
RT   "A survey of the heat shock response in four Streptomyces species reveals
RT   two groEL-like genes and three groEL-like proteins in Streptomyces albus.";
RL   J. Bacteriol. 173:7374-7381(1991).
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; M76658; AAA26754.1; -; Genomic_DNA.
DR   PIR; C41325; C41325.
DR   AlphaFoldDB; Q00768; -.
DR   SMR; Q00768; -.
DR   PRIDE; Q00768; -.
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; IPR018370; Chaperonin_Cpn60_CS.
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.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW   Nucleotide-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1682303"
FT   CHAIN           2..540
FT                   /note="Chaperonin GroEL 2"
FT                   /id="PRO_0000063545"
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         476..478
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         492
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   540 AA;  56718 MW;  B068E766B7AD9E5C CRC64;
     MAKIIAFDEE ARRGLERGMN QLADAVKVTL GPKGRNVVLE KKWGAPTITN DGVSIAKEIE
     LEDPYEKIGA ELVKEVAKKT DDVAGDGTTT ATVLAQALVR EGLRNVAAGA NPMALKRGIE
     KAVEAVSSAL LEQAKDVETK EQIASTASIS AADTQIGELI AEAMDKVGKE GVITVEESQT
     FGLELELTEG MRFDKGYISA YFATDMERME ASLDDPYILI VNSKIGNVKD LLPLLEKVMQ
     SGKPLLIIAE DVEGEALSTL VVNKIRGTFK SVAVKAPGFG DRRKAMLGDI AILTGGTVIS
     EEVGLKLENA GLDLLGRARK VVITKDETTI VDGAGDTDQV NGRVAQIRAE IENSDSDYDR
     EKLQERLANV AGGVAVIKAG AATEVELKER KHRIEDAVRN AKAAVEEGIV AGGGVALLQA
     SSVFEKLELE GDEATGAAAV KLALEAPLKQ IAVNGGLEGG VVVEKVRNLS VGHGLNAATG
     QYVDMIAEGI LDPAKVTRSA LQNAASIAAL FLTTEAVIAD KPEKAAAAAP GGMPGGDMDF