ID   CH601_STRAL             Reviewed;         540 AA.
AC   Q00767;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Chaperonin GroEL 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=HSP58;
GN   Name=groEL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL1 {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 2-18 AND 59-93.
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; M76657; AAA26753.1; -; Genomic_DNA.
DR   PIR; B41325; B41325.
DR   AlphaFoldDB; Q00767; -.
DR   SMR; Q00767; -.
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 1"
FT                   /id="PRO_0000063544"
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         415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         479..481
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         495
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   540 AA;  56716 MW;  05229267BB7ECC73 CRC64;
     MAKILKFDED ARRALERGVN QLADTVKVTI GPKGRNVVID KKFGAPTITN DGVTIAREVE
     CDDPYENLGA QLVKEVATKT NDIAGDGTTT ATVLAQALVR EGLRNVAAGA SPAALKKGID
     AAVAAVSAEL LDTARPIDDK SDIAAVAALS AQDKQVGELI AEAMDKVGKD GVITVEESNT
     FGVDLDFTEG MAFDKGYLSP YMVTDQERME AVLDDPYILI HQGKIGSIQD LLPLLEKVIQ
     AGGSKPLLII AEDVEGEALS TLVVNKIRGT FNAVAVKAPG FGDRRKAMLG DMATLTGATV
     IAEEVGLKLD QAGLDVLGTA RRVTVTKDDT TIVDGGGNAE DVQGRVAQIK AEIESTDSDW
     DREKLQERLA KLAGGVCVIR VGAATEVELK ERKHRLEDAI SATRAAVEEG IVSGGGSALV
     HAVKVLDDNL GRTGDEATGV AVVRRAAVEP LRWIAENAGL EGYVITTKVA ELDKGQGFNA
     ATGEYGDLVK AGVIDPVKVT RSALENAASI ASLLLTTETL VVEKPAEEEP EAGHGHGHSH