CH60_BACSU
ID CH60_BACSU Reviewed; 544 AA.
AC P28598; O05526;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
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=BSU06030;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1350777; DOI=10.1128/jb.174.12.3993-3999.1992;
RA Schmidt A., Schiesswohl M., Voelker U., Hecker M., Schumann W.;
RT "Cloning, sequencing, mapping, and transcriptional analysis of the groESL
RT operon from Bacillus subtilis.";
RL J. Bacteriol. 174:3993-3999(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1350776; DOI=10.1128/jb.174.12.3981-3992.1992;
RA Li M., Wong S.L.;
RT "Cloning and characterization of the groESL operon from Bacillus
RT subtilis.";
RL J. Bacteriol. 174:3981-3992(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=1369494; DOI=10.1271/bbb.56.1995;
RA Tozawa Y., Yoshikawa H., Kawamura F., Itaya M., Takahashi H.;
RT "Isolation and characterization of the groES and groEL genes of Bacillus
RT subtilis Marburg.";
RL Biosci. Biotechnol. Biochem. 56:1995-2002(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=9455482; DOI=10.1093/dnares/4.5.335;
RA Kasahara Y., Nakai S., Ogasawara N., Yata K., Sadaie Y.;
RT "Sequence analysis of the groESL-cotA region of the Bacillus subtilis
RT genome, containing the restriction/modification system genes.";
RL DNA Res. 4:335-339(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RC STRAIN=168 / JH642;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(1997).
RN [7]
RP PROTEIN SEQUENCE OF 2-31.
RC STRAIN=168 / IS58;
RX PubMed=8012595; DOI=10.1099/00221287-140-4-741;
RA Voelker U., Engelmann S., Maul B., Riethdorf S., Voelker A., Schmid R.,
RA Mach H., Hecker M.;
RT "Analysis of the induction of general stress proteins of Bacillus
RT subtilis.";
RL Microbiology 140:741-752(1994).
RN [8]
RP PROTEIN SEQUENCE OF 2-31.
RC STRAIN=168 / IS58;
RX PubMed=1362210; DOI=10.1099/00221287-138-10-2125;
RA Voelker U., Mach H., Schmid R., Hecker M.;
RT "Stress proteins and cross-protection by heat shock and salt stress in
RT Bacillus subtilis.";
RL J. Gen. Microbiol. 138:2125-2135(1992).
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; M84965; AAA22531.1; -; Genomic_DNA.
DR EMBL; M81132; AAA22503.1; -; Genomic_DNA.
DR EMBL; D10972; BAA22519.1; -; Genomic_DNA.
DR EMBL; AB007637; BAA22747.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12422.1; -; Genomic_DNA.
DR EMBL; D88802; BAA19727.1; -; Genomic_DNA.
DR PIR; B41884; B41884.
DR RefSeq; NP_388484.1; NC_000964.3.
DR RefSeq; WP_003243151.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P28598; -.
DR SMR; P28598; -.
DR DIP; DIP-58540N; -.
DR IntAct; P28598; 1.
DR STRING; 224308.BSU06030; -.
DR jPOST; P28598; -.
DR PaxDb; P28598; -.
DR PRIDE; P28598; -.
DR EnsemblBacteria; CAB12422; CAB12422; BSU_06030.
DR GeneID; 938045; -.
DR KEGG; bsu:BSU06030; -.
DR PATRIC; fig|224308.179.peg.648; -.
DR eggNOG; COG0459; Bacteria.
DR InParanoid; P28598; -.
DR OMA; TDTDKME; -.
DR PhylomeDB; P28598; -.
DR BioCyc; BSUB:BSU06030-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
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; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1362210,
FT ECO:0000269|PubMed:8012595"
FT CHAIN 2..544
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063279"
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 15
FT /note="M -> N (in Ref. 3; BAA22519)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="V -> L (in Ref. 3; BAA22519)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="M -> L (in Ref. 3; BAA22519)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="A -> R (in Ref. 3; BAA22519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 57425 MW; 25B72B4E88FF381D CRC64;
MAKEIKFSEE ARRAMLRGVD ALADAVKVTL GPKGRNVVLE KKFGSPLITN DGVTIAKEIE
LEDAFENMGA KLVAEVASKT NDVAGDGTTT ATVLAQAMIR EGLKNVTAGA NPVGVRKGME
QAVAVAIENL KEISKPIEGK ESIAQVAAIS AADEEVGSLI AEAMERVGND GVITIEESKG
FTTELEVVEG MQFDRGYASP YMVTDSDKME AVLDNPYILI TDKKITNIQE ILPVLEQVVQ
QGKPLLLIAE DVEGEALATL VVNKLRGTFN AVAVKAPGFG DRRKAMLEDI AVLTGGEVIT
EDLGLDLKST QIAQLGRASK VVVTKENTTI VEGAGETDKI SARVTQIRAQ VEETTSEFDR
EKLQERLAKL AGGVAVIKVG AATETELKER KLRIEDALNS TRAAVEEGIV SGGGTALVNV
YNKVAAVEAE GDAQTGINIV LRALEEPIRQ IAHNAGLEGS VIVERLKNEE IGVGFNAATG
EWVNMIEKGI VDPTKVTRSA LQNAASVAAM FLTTEAVVAD KPEENGGGAG MPDMGGMGGM
GGMM
