CH60_FRATT
ID CH60_FRATT Reviewed; 544 AA.
AC Q5NEE1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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};
GN OrderedLocusNames=FTT_1696;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=NY 96-3369;
RX PubMed=16790773; DOI=10.1128/iai.00257-06;
RA Lee B.-Y., Horwitz M.A., Clemens D.L.;
RT "Identification, recombinant expression, immunolocalization in macrophages,
RT and T-cell responsiveness of the major extracellular proteins of
RT Francisella tularensis.";
RL Infect. Immun. 74:4002-4013(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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 Note=Released into the host cell cytosol during infection.
CC {ECO:0000269|PubMed:16790773}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; AY662300; AAT77113.1; -; Genomic_DNA.
DR EMBL; AJ749949; CAG46329.1; -; Genomic_DNA.
DR RefSeq; WP_003022663.1; NZ_CP010290.1.
DR RefSeq; YP_170601.1; NC_006570.2.
DR AlphaFoldDB; Q5NEE1; -.
DR SMR; Q5NEE1; -.
DR IntAct; Q5NEE1; 4.
DR STRING; 177416.FTT_1696; -.
DR ABCD; Q5NEE1; 2 sequenced antibodies.
DR DNASU; 3191101; -.
DR EnsemblBacteria; CAG46329; CAG46329; FTT_1696.
DR KEGG; ftu:FTT_1696; -.
DR eggNOG; COG0459; Bacteria.
DR OMA; TDTDKME; -.
DR Proteomes; UP000001174; 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 ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16790773"
FT CHAIN 2..544
FT /note="Chaperonin GroEL"
FT /id="PRO_0000332001"
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 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 544 AA; 57429 MW; 594923EC42BF9DA7 CRC64;
MAAKQVLFSD EARAKMLDGV NTLANAVKVT LGPKGRNVVL DKSFGTPTIT KDGVSVAKEI
ELEDKFENMG AQIVKEVASK TADVAGDGTT TATVLAQALL TEGLKAVAAG MNPMDLKRGI
DKATARLVEE LKALSKPCSD PKSIEQVGTI SANSDATVGK LIADAMAKVG KEGVITVEEG
KGFEDELDVV EGMQFDRGYL SPYFATNQEN MTTDLENPYI LIVDKKISNI RDLLPILEGV
SKSGRALLII AEDVESEALA TLVVNNMRGV VKVCAVKAPG FGDRRKAMLE DIATLTGATF
VSEDLSMKLE ETNMEHLGTA SRVQVTKDNT TIIDGAGEKE AIAKRINVIK ANIAEANSDY
DREKLQERLA KLSGGVAVIK VGAVTEAEMK EKKDRVDDAL HATRAAVEEG IVAGGGVALI
RAQKALDGLT GENDDQNYGI ALLRKAIEAP LRQIVSNAGG ESSVVVNQVK ANQGNYGYNA
ANDTYGDMVE MGILDPTKVT RSALQHAASI AGLMITTEAM IGEIKEAAPA MPMGGGMGGM
PGMM
