CH602_SINFN
ID CH602_SINFN Reviewed; 542 AA.
AC Q6W1D5; C3KPG4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=NGR_b05100; ORFNames=RNGR00307;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY316747; AAQ87433.1; -; Genomic_DNA.
DR EMBL; CP000874; ACP21972.1; -; Genomic_DNA.
DR RefSeq; WP_012706571.1; NC_012586.1.
DR RefSeq; YP_002822725.1; NC_012586.1.
DR AlphaFoldDB; Q6W1D5; -.
DR SMR; Q6W1D5; -.
DR EnsemblBacteria; ACP21972; ACP21972; NGR_b05100.
DR KEGG; rhi:NGR_b05100; -.
DR PATRIC; fig|394.7.peg.953; -.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OMA; LKDQHMN; -.
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 2"
FT /id="PRO_0000332058"
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; 58238 MW; 6C2CA9D72010754D CRC64;
MAAKEVRFHT EAREKMLRGV DILANAVKVT LGPKGRNVVL DKSFGAPRIT KDGVTVAKEI
ELEDKFENMG AQMVREVASK TSDIAGDGTT TATVLAQAIV KEGAKAVASG MNPMDLKRGV
DKAVDAVVEE LRRNARKVTK NDEIAQVGTI SANGDTEIGR FLAEAMEKVG NEGVITVEEA
KTAVTELEVV EGMQFDRGYL SPYFVTNPDK MRVELEEPYV LIHEKKLSNL QALLPVLESV
VQSGKPLLII AEDVEGEALA TLVVNKLRGG LKVAAVKAPG FGDRRKAMLE DIAILTGGTA
ISEDLGIKLE NVTLDMLGRA KKVVVEKENT TIVDGAGSKT EIEGRVAQIK AQIEETTSDY
DREKLQERLA KLAGGVAVIR VGGSTEVEVK ERKDRVDDAM HATRAAVEEG VLPGGGVALL
RAVKALDRVQ TENPDQRHGI EIVRRAIEAP VRQIAENAGA EGSIIVGKLR EKTEFGYGWN
AQTNEFGDLF EQGVIDPVKV VRTALQDAAS VAGLLITTEA MVAEKPKKEA PVPPMPPGGM
DF
