ID   CH60_STAAN              Reviewed;         538 AA.
AC   P99083; Q99SL7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 114.
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};
GN   OrderedLocusNames=SA1836;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=N315;
RX   PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA   Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA   Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA   Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT   "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT   aureus during the post-exponential phase of growth.";
RL   J. Microbiol. Methods 60:247-257(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
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 + an unfolded polypeptide = ADP + phosphate + a
CC         folded 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; BA000018; BAB43116.1; -; Genomic_DNA.
DR   PIR; C89994; C89994.
DR   RefSeq; WP_000240642.1; NC_002745.2.
DR   AlphaFoldDB; P99083; -.
DR   SMR; P99083; -.
DR   EnsemblBacteria; BAB43116; BAB43116; BAB43116.
DR   KEGG; sau:SA1836; -.
DR   HOGENOM; CLU_016503_3_0_9; -.
DR   AbasyAtlas; P99083; -.
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:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   CDD; cd03344; GroEL; 1.
DR   FunFam; 1.10.560.10:FF:000001; 60 kDa chaperonin; 1.
DR   FunFam; 3.50.7.10:FF:000001; 60 kDa chaperonin; 1.
DR   Gene3D; 3.50.7.10; GroEL; 1.
DR   Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR   Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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   NCBIfam; TIGR02348; GroEL; 1.
DR   NCBIfam; NF000592; PRK00013.1; 1.
DR   NCBIfam; NF009487; PRK12849.1; 1.
DR   NCBIfam; NF009488; PRK12850.1; 1.
DR   NCBIfam; NF009489; PRK12851.1; 1.
DR   PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR   SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR   SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT   CHAIN           1..538
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063533"
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"
SQ   SEQUENCE   538 AA;  57572 MW;  A3D8595603DC9313 CRC64;
     MVKQLKFSED ARQAMLRGVD QLANAVKVTI GPKGRNVVLD KEFTAPLITN DGVTIAKEIE
     LEDPYENMGA KLVQEVANKT NEIAGDGTTT ATVLAQAMIQ EGLKNVTSGA NPVGLRQGID
     KAVKVAVEAL HENSQKVENK NEIAQVGAIS AADEEIGRYI SEAMEKVGND GVITIEESNG
     LNTELEVVEG MQFDRGYQSP YMVTDSDKMV AELERPYILV TDKKISSFQD ILPLLEQVVQ
     SNRPILIVAD EVEGDALTNI VLNRMRGTFT AVAVKAPGFG DRRKAMLEDL AILTGAQVIT
     DDLGLDLKDA SIDMLGTASK VEVTKDNTTV VDGDGDENSI DARVSQLKSQ IEETESDFDR
     EKLQERLAKL AGGVAVIKVG AASETELKER KLRIEDALNS TRAAVEEGIV AGGGTALVNV
     YQKVSEIEAE GDIETGVNIV LKALTAPVRQ IAENAGLEGS VIVERLKNAE PGVGFNAATN
     EWVNMLEAGI VDPTKVTRSA LQHAASVAAM FLTTEAVVAS IPEKNNDQPN MGGMPGMM
//