CH60_CHLTE
ID CH60_CHLTE Reviewed; 545 AA.
AC Q8KF02;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}; OrderedLocusNames=CT0530;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM71772.1; -; Genomic_DNA.
DR RefSeq; NP_661430.1; NC_002932.3.
DR RefSeq; WP_010932217.1; NC_002932.3.
DR PDB; 5DA8; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b=1-545.
DR PDBsum; 5DA8; -.
DR AlphaFoldDB; Q8KF02; -.
DR SMR; Q8KF02; -.
DR STRING; 194439.CT0530; -.
DR PRIDE; Q8KF02; -.
DR EnsemblBacteria; AAM71772; AAM71772; CT0530.
DR KEGG; cte:CT0530; -.
DR PATRIC; fig|194439.7.peg.498; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_10; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000001007; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Isomerase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..545
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063331"
FT BINDING 30..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 87..91
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 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 65..84
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 89..108
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 113..133
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5DA8"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 339..353
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 361..374
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 386..409
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:5DA8"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 417..421
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 422..428
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 434..446
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 449..456
FT /evidence="ECO:0007829|PDB:5DA8"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 463..472
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:5DA8"
FT TURN 481..484
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:5DA8"
FT TURN 489..493
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:5DA8"
FT HELIX 498..516
FT /evidence="ECO:0007829|PDB:5DA8"
FT STRAND 518..524
FT /evidence="ECO:0007829|PDB:5DA8"
SQ SEQUENCE 545 AA; 58080 MW; F2263E3CAEA5F7E4 CRC64;
MTAKDILFDA EARTKLKVGV DKLANAVKVT LGPAGRNVLI DKKFGAPTST KDGVTVAKEI
ELVDPVENMG AQMVREVASK TSDVAGDGTT TATVLAQAIY REGLKNVTAG ARPIDLKRGI
DRAVKEVVAE LRNISRSISG KKEIAQVGTI SANNDPEIGE LIAEAMDKVG KDGVITVEEA
KGMETELKVV EGMQFDRGYL SPYFVTNSET MEAELDEALI LIHDKKISNM KELLPILEKA
AQSGRPLLII AEDIEGEALA TLVVNKLRGT LKVAAVKAPG FGDRRKAMLE DIAILTGGTV
ISEEKGYKLE NATMAYLGQA ARITIDKDNT TIVEGKGKQE EIKARINEIK GQIEKSTSDY
DTEKLQERLA KLSGGVAVLK IGASTEVEMK EKKARVEDAL HATRAAVQEG IVVGGGVALI
RAAKGLAKAV ADNEDQKTGI EIIRRALEEP LRQIVANTGT TDGAVVLEKV KNAEGDYGFN
ARTEQYENLI EAGVVDPTKV TRSALENAAS VASILLTTEA AITDVKEDKA DMPAMPPGGM
GGGMY
