ID   CH603_TRIV2             Reviewed;         545 AA.
AC   Q3M1B1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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};
GN   OrderedLocusNames=Ava_C0144;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OG   Plasmid pAnaC.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000121; ABA25232.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3M1B1; -.
DR   SMR; Q3M1B1; -.
DR   STRING; 240292.Ava_C0144; -.
DR   EnsemblBacteria; ABA25232; ABA25232; Ava_C0144.
DR   KEGG; ava:Ava_C0144; -.
DR   eggNOG; COG0459; Bacteria.
DR   HOGENOM; CLU_016503_3_0_3; -.
DR   OMA; HILITDR; -.
DR   Proteomes; UP000002533; Plasmid pAnaC.
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; 2.
DR   SUPFAM; SSF52029; SSF52029; 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; Plasmid.
FT   CHAIN           1..545
FT                   /note="Chaperonin GroEL 3"
FT                   /id="PRO_0000331963"
FT   REGION          526..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         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   545 AA;  58694 MW;  4F9640A69030CADA CRC64;
     MVKTILYKDT ARWTLEKGFD ALTEAVAVTL GPKGRNIVLE KKFGAPQIVN DGVTIAKEIE
     LEDPAENTGI SLLRQAASKT NDVAGDGTTT AIVLAHAMLK EGLRNVTAGA DPLTVKRGID
     KATEFVIEKI QEHARPIKDS RDIEQVATIS AGNDPEVGRI VAEAMERVGK EGVISLEEGR
     STTTELEVTE GMRFDRGYVS PYFVTDPERM EAVLEEPHIL ITDRKITMVQ DLVPILEQIA
     RTGKPLLIIA DDIEKEALAT LVVNHLRGVL RVAAVKAPGF GAQRKAVLED IAALTGGQVI
     SEDTGLKLEN VRLEMLGKAR RAIVTKDDTT IVAEGNEEAV KARIEQIRRQ IQEVESSYDK
     EKLQQRLAKL AGGVAVIKVG AATETELKDR KLRLEDAINA TKAAVEEGIV PGGGTTIAHI
     APQLEEWAKS QMKDEELTGT MIVARALYAP LRRIADNAGA NGAVIVERVR ELPFDEGYDA
     VANKFVNMFE AGIVDPAKVT RSALQNAASI GGMVLTTEGV VVEKPDKQAK APAGVGPGPG
     EGFDY