CH60_BACCE
ID CH60_BACCE Reviewed; 544 AA.
AC Q4MPR6; P83074;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 78.
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}; ORFNames=BCE_G9241_0261;
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G9241;
RX PubMed=15155910; DOI=10.1073/pnas.0402414101;
RA Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D.,
RA Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W.,
RA Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J.,
RA Peterson S.N., Weyant R.S., Galloway D.R., Read T.D., Popovic T.,
RA Fraser C.M.;
RT "Identification of anthrax toxin genes in a Bacillus cereus associated with
RT an illness resembling inhalation anthrax.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004).
RN [2]
RP PROTEIN SEQUENCE OF 2-21, AND INDUCTION.
RC STRAIN=DSM 626 / NCIMB 11796 / T;
RX PubMed=11851817; DOI=10.1046/j.1365-2672.2001.01478.x;
RA Browne N., Dowds B.C.A.;
RT "Heat and salt stress in the food pathogen Bacillus cereus.";
RL J. Appl. Microbiol. 91:1085-1094(2001).
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 -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:11851817}.
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; AAEK01000017; EAL14249.1; -; Genomic_DNA.
DR RefSeq; WP_001975554.1; NZ_VEFJ01000018.1.
DR AlphaFoldDB; Q4MPR6; -.
DR SMR; Q4MPR6; -.
DR STRING; 1396.DJ87_5738; -.
DR GeneID; 58161480; -.
DR eggNOG; COG0459; Bacteria.
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; Direct protein sequencing; Isomerase;
KW Nucleotide-binding; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11851817"
FT CHAIN 2..544
FT /note="Chaperonin GroEL"
FT /id="PRO_0000271238"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 86..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 476..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 4
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 9..10
FT /note="EE -> QQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 57460 MW; 2E4A70F70D53EA7C CRC64;
MAKDIKFSEE ARRSMLRGVD TLANAVKVTL GPKGRNVVLE KKFGSPLITN DGVTIAKEIE
LEDAFENMGA KLVAEVASKT NDVAGDGTTT ATVLAQAMIR EGLKNVTAGA NPMGLRKGIE
KAVTAAIEEL KTISKPIEGK SSIAQVAAIS AADEEVGQLI AEAMERVGND GVITLEESKG
FTTELDVVEG MQFDRGYASP YMITDSDKME AVLDNPYILI TDKKISNIQE ILPVLEQVVQ
QGKPLLIIAE DVEGEALATL VVNKLRGTFN VVAVKAPGFG DRRKAMLEDI AILTGGEVIT
EELGRDLKSA TVESLGRAGK VVVTKENTTV VEGIGNTQQI EARIGQIRAQ LEETTSEFDR
EKLQERLAKL AGGVAVIKVG AATETELKER KLRIEDALNS TRAAVEEGIV AGGGTSLMNV
YTKVASIVAE GDEATGINIV LRALEEPVRQ IAINAGLEGS VVVERLKGEK VGVGFNAATG
EWVNMLETGI VDPAKVTRSA LQNAASVAAM FLTTEAVVAD KPEPNAPAMP DMGGMGMGGM
GGMM
