CH603_METCA
ID CH603_METCA Reviewed; 559 AA.
AC Q7WZ32; Q609N0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Chaperonin GroEL 3 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 3 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 3 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 3 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL3 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL3 {ECO:0000255|HAMAP-Rule:MF_00600}, mmoG;
GN OrderedLocusNames=MCA1202;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=12855730; DOI=10.1099/mic.0.26061-0;
RA Csaki R., Bodrossy L., Klem J., Murrell J.C., Kovacs K.L.;
RT "Genes involved in the copper-dependent regulation of soluble methane
RT monooxygenase of Methylococcus capsulatus (Bath): cloning, sequencing and
RT mutational analysis.";
RL Microbiology 149:1785-1795(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(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, ECO:0000305}.
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DR EMBL; AF525283; AAP80770.1; -; Genomic_DNA.
DR EMBL; AE017282; AAU92713.1; -; Genomic_DNA.
DR RefSeq; WP_010960489.1; NC_002977.6.
DR AlphaFoldDB; Q7WZ32; -.
DR SMR; Q7WZ32; -.
DR STRING; 243233.MCA1202; -.
DR EnsemblBacteria; AAU92713; AAU92713; MCA1202.
DR KEGG; mca:MCA1202; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_6; -.
DR OMA; RHIAREM; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0042026; P:protein refolding; IEA:InterPro.
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 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; 2.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..559
FT /note="Chaperonin GroEL 3"
FT /id="PRO_0000063418"
FT BINDING 88..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 507
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 559 AA; 59469 MW; FE0687AF7CBF5840 CRC64;
MAKEVVYRGS ARQRMMQGIE ILARAAIPTL GATGPSVMIQ HRADGLPPIS TRDGVTVANS
IVLKDRVANL GARLLRDVAG TMSREAGDGT TTAIVLARHI AREMFKSLAV GADPIALKRG
IDRAVARVSE DIGARAWRGD KESVILGVAA VATKGEPGVG RLLLEALDAV GVHGAVSIEL
GQRREDLLDV VDGYRWEKGY LSPYFVTDRA RELAELEDVY LLMTDREVVD FIDLVPLLEA
VTEAGGSLLI AADRVHEKAL AGLLLNHVRG VFKAVAVTAP GFGDKRPNRL LDLAALTGGR
AVLEAQGDRL DRVTLADLGR VRRAVVSADD TALLGIPGTE ASRARLEGLR LEAEQYRALK
PGQGSATGRL HELEEIEARI VGLSGKSAVY RVGGVTDVEM KERMVRIENA YRSVVSALEE
GVLPGGGVGF LGSMPVLAEL EARDADEARG IGIVRSALTE PLRIIGENSG LSGEAVVAKV
MDHANPGWGY DQESGSFCDL HARGIWDAAK VLRLALEKAA SVAGTFLTTE AVVLEIPDTD
AFAGFSAEWA AATREDPRV
