CH60_SODGM
ID CH60_SODGM Reviewed; 548 AA.
AC Q2NW94; Q93MH9; Q9AMB4; Q9ANR8;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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}, mopA;
GN OrderedLocusNames=SG0306;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11443086; DOI=10.1128/jb.183.15.4517-4525.2001;
RA Akman L., Rio R.V.M., Beard C.B., Aksoy S.;
RT "Genome size determination and coding capacity of Sodalis glossinidius, an
RT enteric symbiont of tsetse flies, as revealed by hybridization to
RT Escherichia coli gene arrays.";
RL J. Bacteriol. 183:4517-4525(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-534, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12530210; DOI=10.1016/s0965-1748(02)00063-2;
RA Haines L.R., Haddow J.D., Aksoy S., Gooding R.H., Pearson T.W.;
RT "The major protein in the midgut of teneral Glossina morsitans morsitans is
RT a molecular chaperone from the endosymbiotic bacterium Wigglesworthia
RT glossinidia.";
RL Insect Biochem. Mol. Biol. 32:1429-1438(2002).
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; AF321517; AAG49527.1; -; Genomic_DNA.
DR EMBL; AP008232; BAE73581.1; -; Genomic_DNA.
DR EMBL; AF404511; AAK92204.1; -; Genomic_DNA.
DR RefSeq; WP_011410169.1; NZ_LN854557.1.
DR AlphaFoldDB; Q2NW94; -.
DR SMR; Q2NW94; -.
DR STRING; 343509.SG0306; -.
DR PRIDE; Q2NW94; -.
DR EnsemblBacteria; BAE73581; BAE73581; SG0306.
DR KEGG; sgl:SG0306; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_6; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR BioCyc; SGLO343509:SGP1_RS02830-MON; -.
DR Proteomes; UP000001932; 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; Isomerase; Nucleotide-binding.
FT CHAIN 1..548
FT /note="Chaperonin GroEL"
FT /id="PRO_0000232499"
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"
FT CONFLICT 257
FT /note="E -> D (in Ref. 3; AAK92204)"
FT /evidence="ECO:0000305"
FT CONFLICT 545..548
FT /note="GGMM -> M (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 57558 MW; AC016296343FC6E6 CRC64;
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPVIT KDGVSVAREI
ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQSIV NEGLKAVAAG MNPMDLKRGI
DKAVIAAVEE LKKLSVPCSD SKAIAQVGTI SANADETVGT LIAEAMAKVG KEGVITVEEG
SGLQDELDVV EGMQFDRGYL SPYFVNKPET GAVELESPFI LLADKKISNI REMLPVLEAV
AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKIAAVKAPG FGDRRKAMLQ DIAILTAGTV
ISEEIGLELE KATLEDMGQA KRVVITKDTT TIIDGEGDKA LIDSRVTQIN QQRDEATSDY
DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI
RVANRIAELR GDNEDQNVGI KVARRAMEAP LRQIVANAGE EPSVIANKVK AGEGNTGYNA
ATEEYGNMID MGILDPTKVT RSALQYAASI AGLMITTECM VTDLPKEDKP DLGGAGGMGG
MGGMGGMM
