CH60_CAUVN
ID CH60_CAUVN Reviewed; 547 AA.
AC B8H163; P48211;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=CCNA_00721;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN LEVELS, OPERON STRUCTURE, AND
RP INDUCTION.
RX PubMed=8821938; DOI=10.1046/j.1365-2958.1996.347879.x;
RA Avedissian M., Gomes S.L.;
RT "Expression of the groESL operon is cell-cycle controlled in Caulobacter
RT crescentus.";
RL Mol. Microbiol. 19:79-89(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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 -!- DEVELOPMENTAL STAGE: Decreases slightly during the first hour of the
CC cell cycle then increases to maximal levels by 2 hours, at the protein
CC level.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:8821938}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; L41394; AAB18635.1; -; Genomic_DNA.
DR EMBL; CP001340; ACL94186.1; -; Genomic_DNA.
DR RefSeq; WP_010918571.1; NC_011916.1.
DR RefSeq; YP_002516094.1; NC_011916.1.
DR AlphaFoldDB; B8H163; -.
DR SMR; B8H163; -.
DR PRIDE; B8H163; -.
DR EnsemblBacteria; ACL94186; ACL94186; CCNA_00721.
DR GeneID; 7330530; -.
DR KEGG; ccs:CCNA_00721; -.
DR PATRIC; fig|565050.3.peg.711; -.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR PhylomeDB; B8H163; -.
DR Proteomes; UP000001364; 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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..547
FT /note="Chaperonin GroEL"
FT /id="PRO_0000378279"
FT REGION 528..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT CONFLICT 45
FT /note="G -> A (in Ref. 1; AAB18635)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..224
FT /note="FE -> SR (in Ref. 1; AAB18635)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="Missing (in Ref. 1; AAB18635)"
FT /evidence="ECO:0000305"
FT CONFLICT 426..428
FT /note="LAG -> SA (in Ref. 1; AAB18635)"
FT /evidence="ECO:0000305"
FT CONFLICT 524..532
FT /note="EAPKKGGGA -> VSPQEGRRR (in Ref. 1; AAB18635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 57397 MW; 03FCE8BADD5C7DB4 CRC64;
MAAKDVYFSS DARDKMLRGV NILANAVKVT LGPKGRNVVI EKSFGAPRTT KDGVSVAKEI
ELADKFENLG AQMIREVASK TNDKAGDGTT TATVLAQAIV QEGLKSVAAG MNPMDLKRGI
DKAVAIAIED IKTSSKKVTT NAEIAQVGTI SANGDKEVGE MIAKAMDKVG NEGVITVEEA
KTAETELDVV EGMQFDRGYL SPYFITNADK MEVQLEEPLI LLFEKKLSSL QPLLPVLEAV
VQSGRPLLII AEDVEGEALA TLVVNKLRGG LRVAAVKAPG FGDRRKAMLE DIAILTGAQV
VSEDIGIKLE NVSLEMLGRA KKVSITKDDT TIVDGVGEKA DIEARIAQIK RQIEDTTSDY
DKEKLQERLA KLAGGVAVIR VGGSTEVEVK EKKDRVDDAL NATRAAADEG IVPGGGTALL
KASKALAGVV GDNDDQTAGI AIVRRALQAP IRQIAENAGV EGSIVVGKIL ENDNSAFGFN
AQTEQYVDLV VDGVIDPAKV VRTALQNAAS VAGLLITTEA AIVEAPKKGG GAPAGGGMPG
GMGDMDF
