CH602_NOCFA
ID CH602_NOCFA Reviewed; 541 AA.
AC Q9AFA6; Q5YNW4;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Chaperonin GroEL 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Heat shock protein 60;
GN Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL, groL2 {ECO:0000255|HAMAP-Rule:MF_00600}, hsp60;
GN OrderedLocusNames=NFA_52750;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zimmermann O.S., Koechel H.G.;
RT "Nocardia farcinica heat shock protein 60 (hsp60) gene.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AF352577; AAK18613.1; -; Genomic_DNA.
DR EMBL; AP006618; BAD60127.1; -; Genomic_DNA.
DR RefSeq; WP_011211809.1; NC_006361.1.
DR AlphaFoldDB; Q9AFA6; -.
DR SMR; Q9AFA6; -.
DR STRING; 247156.NFA_52750; -.
DR PRIDE; Q9AFA6; -.
DR EnsemblBacteria; BAD60127; BAD60127; NFA_52750.
DR GeneID; 61135851; -.
DR KEGG; nfa:NFA_52750; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_11; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000006820; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..541
FT /note="Chaperonin GroEL 2"
FT /id="PRO_0000063464"
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 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 13
FT /note="R -> C (in Ref. 1; AAK18613)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="G -> S (in Ref. 1; AAK18613)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="A -> R (in Ref. 1; AAK18613)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="E -> V (in Ref. 1; AAK18613)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="N -> K (in Ref. 1; AAK18613)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="E -> R (in Ref. 1; AAK18613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 56407 MW; 91801667CE5203E0 CRC64;
MAKTIAYDEE ARRGLERGLN SLADAVKVTL GPKGRNVVLE KKWGAPTITN DGVSIAKEIE
LEDPYEKIGA ELVKEVAKKT DDVAGDGTTT ATVLAQALVR EGLRNVAAGA NPLGLKRGIE
KAVEAVTAKL LDTAKEVETK EQIAATAGIS AGDASIGELI AEAMDKVGKE GVITVEESNT
FGLQLELTEG MRFDKGYISG YFVTDPERQE AVLEDPYILL VGSKVSTVKD LLPLLEKVIQ
AGKPLLIIAE DVEGEALSTL VVNKIRGTFK SVAVKAPGFG DRRKAQLADI AILTGGEVIS
EEVGLSLETA GIELLGQARK VVVTKDETTI VEGAGDAEAI KGRVAQIRTE IENSDSDYDR
EKLQERLAKL AGGVAVIKAG AATEVELKER KHRIEDAVRN AKAAVEEGIV AGGGVALLQA
APALDELKLT GDEATGANIV RVALSAPLKQ IAFNAGLEPG VVAEKVSNLE AGHGLNADSG
EYEDLLAAGV ADPVKVTRSA LQNAASIAAL FLTTEAVVAD KPEKAAAPAG DPTGGMGGMD
F
