ID CH601_TRIEI Reviewed; 561 AA.
AC Q119S1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=Tery_0270;
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
RX PubMed=25831533; DOI=10.1073/pnas.1422332112;
RA Walworth N., Pfreundt U., Nelson W.C., Mincer T., Heidelberg J.F., Fu F.,
RA Waterbury J.B., Glavina del Rio T., Goodwin L., Kyrpides N.C., Land M.L.,
RA Woyke T., Hutchins D.A., Hess W.R., Webb E.A.;
RT "Trichodesmium genome maintains abundant, widespread noncoding DNA in situ,
RT despite oligotrophic lifestyle.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4251-4256(2015).
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; CP000393; ABG49753.1; -; Genomic_DNA.
DR AlphaFoldDB; Q119S1; -.
DR SMR; Q119S1; -.
DR STRING; 203124.Tery_0270; -.
DR KEGG; ter:Tery_0270; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_3; -.
DR OrthoDB; 9766614at2; -.
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; 3.50.7.10; GroEL; 1.
DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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 NCBIfam; TIGR02348; GroEL; 1.
DR PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45633:SF41; CHAPERONIN GROEL 2; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT CHAIN 1..561
FT /note="Chaperonin GroEL 1"
FT /id="PRO_0000332097"
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 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 561 AA; 59163 MW; DFAED1BFCECF2D81 CRC64;
MAKIVEFDDK SRRSLERGIN TLADAVRITM GPKGRNVLLE KKYGAPQIVN DGITVAKDIE
LEDPLENTGA KLIQEVASKT KDIAGDGTTT ATVLAQSMIK EGLKNVAAGA NPVAVRRGIE
KTVSLLVKEI QTVAKPVEGE AIAQVATVSA GGDAEVGRMI SEAMDKVTKD GVITVEESKS
LSTDLEVVEG MQIDRGYLSP YFVTDQERLV VDFENARILI TDKKISSIQD LVPVLEKVAR
AGQSLLIIAE DIEGEALATL VVNKARGVLN VAAVKAPGFG DRRKAMLQDI AILTGGQLIS
EEVGLSLEMV DLDMMGIGRK ISINKDNTTI VADGGTAEEV KKRIAQIRKQ LGESDSDYDK
EKLQERIAKL AGGVAVIKVG AATETELKDR KLRIEDALNA TKAAVEEGIV PGGGTTLIHL
STKVEELKGS LNNEEEKIGA DIVRRALEAP LNQIANNSGV EGSVIVEKVR STDFSVGYNV
ITGEYEDLIA AGILDPAMVV RSALQNAGSI AGMVLTTEAV VVEKPEKKGA APDMDGGMGG
MGGMGGMGGM GGMGMPGMGM M
//
