CH603_PARUW
ID CH603_PARUW Reviewed; 534 AA.
AC Q6MBR6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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}; OrderedLocusNames=pc1259;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(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; BX908798; CAF23983.1; -; Genomic_DNA.
DR RefSeq; WP_011175809.1; NC_005861.1.
DR AlphaFoldDB; Q6MBR6; -.
DR SMR; Q6MBR6; -.
DR STRING; 264201.pc1259; -.
DR EnsemblBacteria; CAF23983; CAF23983; PC_RS06075.
DR KEGG; pcu:PC_RS06075; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_0; -.
DR OMA; YWIASNA; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000000529; 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; 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.
DR TIGRFAMs; TIGR02348; GroEL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..534
FT /note="Chaperonin GroEL 3"
FT /id="PRO_0000063473"
FT BINDING 31..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 479..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 534 AA; 56480 MW; 1018DD2D795ADD3D CRC64;
MSIPKEIIFE EEAREFLLKG IKKLADVVAF TLGPKGRNVG LEKSWGAPTI TNDGASIIRD
IQLEDKYENM GVAMAKEVVQ KIKEKCGDGT TSGALLLRSL VEAGIKNISS GASPIGIKRG
MDKAVEVVVK AIEKAAIPVK TKQETRNVAV VSASGNQEIG ELIAEAMEKV SNSGAITIEE
GKGTETSIEV VKGMKFDRGY VSPYLCTNLE KMIVEMDHAQ ILLVDKKISS IHELLPVLQA
TAASGRELLI IAEDIDGDAL STLVVNKLRG TLKVAAVKAP GFGDRRKAML QDIATLTAAT
VVSEELGISL KEIPATALGS AEKVTVTKES TTIVGGTGAQ EDIAARIKQI DAEINLAQSS
YDKEKLEERR AKLSGGVAVI RVGAATETEM KQKKQMFDDS LNSTKAALEE GIVPGGGVAL
LNASKTLGQL KLEGDEAVGA KIVLQACETP IKQIVQNTGF DGSVVLNEVL NSPANFGFNA
LTEKVEDLIA AGVIDPAKVI KNTLTYAAST AGIVLLSEAL IADADDEEEE NSTK
