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CH604_RHIEC
ID   CH604_RHIEC             Reviewed;         542 AA.
AC   Q2JYW6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Chaperonin GroEL 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 4 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groEL4 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL4 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   OrderedLocusNames=RHE_PF00330;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OG   Plasmid p42f.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000138; ABC94220.1; -; Genomic_DNA.
DR   RefSeq; WP_011428637.1; NC_007766.1.
DR   AlphaFoldDB; Q2JYW6; -.
DR   SMR; Q2JYW6; -.
DR   EnsemblBacteria; ABC94220; ABC94220; RHE_PF00330.
DR   GeneID; 61484363; -.
DR   KEGG; ret:RHE_PF00330; -.
DR   HOGENOM; CLU_016503_3_0_5; -.
DR   OMA; PYILINQ; -.
DR   Proteomes; UP000001936; Plasmid p42f.
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; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..542
FT                   /note="Chaperonin GroEL 4"
FT                   /id="PRO_0000332056"
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"
SQ   SEQUENCE   542 AA;  57696 MW;  5AA0279B8F377EEA CRC64;
     MAAKEVKFSV EAREKMLRGV DILANAVKVT LGPKGRNVVI DKSFGAPRIT KDGVSVAKEI
     ELEDKFENMG AQMVREVASK TSDIAGDGTT TATVLAQAIV KEGAKAVTSG MNPMDLKRGI
     DLAVSAIVEE LKANARKISN NAEIAQVGTI SANGDAEIGR FLAEAVQKVG NDGVITVEEA
     KTAETELEVV EGMQFDRGYL SPYFVTNADK MRVEFEDPYI LIHEKKLSNL QSMLPILEAV
     VQSGKPLLII AEDVEGEALA TLVVNKLRGG LKIAAVKAPG FGDRRKAMLE DIAILTAGTV
     ISEDLGIKLE NVTLNMLGRA KKITVEKENT TIIDGVGSKE EISGRIAQIK AQIEETTSDY
     DREKLQERLA KLAGGVAVIR VGGSTEVEVK EKKDRVDDAL HATRAAVEEG ILPGGGVALL
     RAVKALDNIK TANDDQRVGV EIVRRALEAP ARQIAENAGA EGSVVVGKLR EKSDFSYGWN
     AQTGEFGDLY AQGVIDPAKV VRTALQDASS IAGLLVTTEA MIAEKPKKDA PPAMPAGAGM
     DF
 
 
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