ID   CH601_PROM5             Reviewed;         587 AA.
AC   A2BVB2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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};
GN   Name=groEL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   OrderedLocusNames=P9515_05141;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000552; ABM71723.1; -; Genomic_DNA.
DR   RefSeq; WP_011819831.1; NC_008817.1.
DR   AlphaFoldDB; A2BVB2; -.
DR   SMR; A2BVB2; -.
DR   STRING; 167542.P9515_05141; -.
DR   EnsemblBacteria; ABM71723; ABM71723; P9515_05141.
DR   KEGG; pmc:P9515_05141; -.
DR   eggNOG; COG0459; Bacteria.
DR   HOGENOM; CLU_016503_3_0_3; -.
DR   OMA; PYILINQ; -.
DR   OrthoDB; 265347at2; -.
DR   Proteomes; UP000001589; Chromosome.
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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT   CHAIN           1..587
FT                   /note="Chaperonin GroEL 1"
FT                   /id="PRO_0000332046"
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         492
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   587 AA;  61972 MW;  AC58AAD9442374C5 CRC64;
     MPKQLSFSND SREALENGVN TVANAVKVTI GPKAKNVVIE RKFGSPDIVR DGSTVAKEIN
     LDNPISNLGA KLIEQVASKT KESAGDGTTT ATILTQIMVQ EGLKNIAAGA SPIELKKGME
     KGLDIVLEKL KSKSIKINGS DIQKVATVSA GGDEEIGSII SKAMDIVTSD GVITVEESQS
     LETELDITEG MSFDRGYSSP YFVTDQERQI CELENPKILI TDQKISTLTN LVPILEEIQK
     SSSPFLVLAE DIEGEALTTL VLNKNSGVLN VSAVRAPSFG ERRKAALEDI AILTGARLIS
     EDQSMKLEEV TINDLGKAKK ITISKDKTTI VAFDDTKDLV KARVEKLKRE VEITESEYDK
     DKINERIAKL AGGVALIKVG AATETEMKYK KLRIEDSLNA TKAAIEEGVV SGGGQTLIEI
     SEELSNLGKE KSVDLNTGIK IITKALLEPT KQIARNAGFN GDVVIADIKR LNKGFNANNG
     QYENLNQSGI LDPTKVIRLA LQDSVSIAAM ILTTEVAVAD IPEPEAPAPG GPGADPMGGM
     GGMGGMGGMG MPGMGGMGMP GMGGMGMPGM GGMGMPGMGG MGMPGMM