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CH601_SINFN
ID   CH601_SINFN             Reviewed;         542 AA.
AC   Q6W163; C3KPN2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=NGR_b05820; ORFNames=RNGR00380;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234b.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=14702322; DOI=10.1128/jb.186.2.535-542.2004;
RA   Streit W.R., Schmitz R.A., Perret X., Staehelin C., Deakin W.J., Raasch C.,
RA   Liesegang H., Broughton W.J.;
RT   "An evolutionary hot spot: the pNGR234b replicon of Rhizobium sp. strain
RT   NGR234.";
RL   J. Bacteriol. 186:535-542(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; AY316747; AAQ87505.1; -; Genomic_DNA.
DR   EMBL; CP000874; ACP22040.1; -; Genomic_DNA.
DR   RefSeq; WP_015886706.1; NC_012586.1.
DR   RefSeq; YP_002822793.1; NC_012586.1.
DR   AlphaFoldDB; Q6W163; -.
DR   SMR; Q6W163; -.
DR   EnsemblBacteria; ACP22040; ACP22040; NGR_b05820.
DR   KEGG; rhi:NGR_b05820; -.
DR   PATRIC; fig|394.7.peg.1028; -.
DR   HOGENOM; CLU_016503_3_0_5; -.
DR   OMA; PYILINQ; -.
DR   OrthoDB; 265347at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234b.
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 1"
FT                   /id="PRO_0000332057"
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;  58052 MW;  7EBC07968112CCF5 CRC64;
     MAAKEVRFHT DAREKMLRGV DILANAVKVT LGPKGRNVVL DKSFGAPRIT KDGVTVAKEV
     ELEDKFENMG AQMVREVASK TSDIAGDGTT TATVLAQAIV KEGAKAVASG MNPMDLKRGI
     DKAVDAIVEE LKTNARRVTK NDEIAQVGTI SANGDIEIGR FLAEAVEKVG NEGVITVEEA
     KTAVTELEVV EGMQFDRGYL SPYFVTNPDK MRVELEEPYL LIHEKKLSNL QALLPVLESV
     VQSGKPLLII AEDVEGEALA TPVVNKLRGG LKIAAVKAPG FGDRRKAMLE DIAILTGGTA
     ISEDLGIKLE NVTLNMLGRA KKVVVEKENT TIVDGAGSKS EIQGRVAQIR AQIEETTSDY
     DREKLQERLA KLAGGVAVIR VGGSTEVEVK ERKDRVDDAM HATRAAVEEG VLPGGGVALL
     RAVKALDSIR TENADQKHGI EIVRRALEAP VRQIAENAGA EGSIIVGKLR EKTEFGFGWN
     AQTNEFGDLY DQGVIDPVKV VRTALQDAAS VAGLLITTEA MVAEKPKKDA PLPPMPGGGM
     DF
 
 
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