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CH602_FRACC
ID   CH602_FRACC             Reviewed;         541 AA.
AC   Q2JAZ7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Chaperonin GroEL 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   OrderedLocusNames=Francci3_2175;
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(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; CP000249; ABD11545.1; -; Genomic_DNA.
DR   RefSeq; WP_011436592.1; NZ_JENI01000028.1.
DR   AlphaFoldDB; Q2JAZ7; -.
DR   SMR; Q2JAZ7; -.
DR   STRING; 106370.Francci3_2175; -.
DR   PRIDE; Q2JAZ7; -.
DR   EnsemblBacteria; ABD11545; ABD11545; Francci3_2175.
DR   KEGG; fra:Francci3_2175; -.
DR   eggNOG; COG0459; Bacteria.
DR   HOGENOM; CLU_016503_3_0_11; -.
DR   OrthoDB; 265347at2; -.
DR   PhylomeDB; Q2JAZ7; -.
DR   Proteomes; UP000001937; 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;
KW   Reference proteome.
FT   CHAIN           1..541
FT                   /note="Chaperonin GroEL 2"
FT                   /id="PRO_0000256912"
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         414
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         478..480
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   541 AA;  57500 MW;  DA932FD4C8B0DE90 CRC64;
     MPKIIAYEEE ARRGLERGMN QLAGAVKVTL GPKGRNVVLE KKWGVPAITN DGVSIAREIE
     LEDPYEKIGA EMVKEVAKKT DEVAGDGTTT ATVLAEALVH EGLRNVAAGA NPIALKRGIE
     LAVERVCGEL ANLSRELETK DQIASTASIS AGGDTAIGQI IAEAMDKVGR DGVITVEESN
     TFGLELELTE GMRFDKGYIS PYFITDQERM ECVLEDPYIL VANIKISLVK DLLPLLEKVM
     QAGRPLLVIA ENVEGEALAT LVVNKIRGTF RSVAVKAPGF GERRKAMLGD IAVLTGSQVI
     SEEVGLRLEN ADLDLLGRAR KVVVTKDDTT IIEGAGDPGR IAGRVSQIRS EIEKSDSDYD
     REKLQERLAR LAGGVAVIKA GAATEVELKE RKHRIEDAVR NAKAAVEEGI VPGGGVALLL
     ASGAVFDGLE VAEDERTGAE MVRRALTEPL RQIAVNAGLE GGVVVEKVRN LQPGWGLDAA
     TGEHVNMLEA GIIDPTKVTR SALQNAASIA GLFLTTEAVV AEKPEEKETA AAPAGGGGLE
     Y
 
 
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