ID   CH603_PSYIN             Reviewed;         544 AA.
AC   A1SYD3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Ping_2791;
OS   Psychromonas ingrahamii (strain 37).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000510; ABM04498.1; -; Genomic_DNA.
DR   RefSeq; WP_011771053.1; NC_008709.1.
DR   AlphaFoldDB; A1SYD3; -.
DR   SMR; A1SYD3; -.
DR   STRING; 357804.Ping_2791; -.
DR   EnsemblBacteria; ABM04498; ABM04498; Ping_2791.
DR   KEGG; pin:Ping_2791; -.
DR   eggNOG; COG0459; Bacteria.
DR   HOGENOM; CLU_016503_3_0_6; -.
DR   OrthoDB; 265347at2; -.
DR   Proteomes; UP000000639; 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..544
FT                   /note="Chaperonin GroEL 3"
FT                   /id="PRO_0000332053"
FT   BINDING         30..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         87..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         415
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   544 AA;  59018 MW;  6DE49AB98580EED2 CRC64;
     MSAKAIKFNH HAREKMLKGV NILADSVKVT LGPKGRNVVI AQKYSRPIIT KDGVTVAKEI
     ELIDPFENMG AQLTKEVAFQ ASDSAGDGTT TATVLTQAIV NEGVNAISAN MNPIDLKKGI
     DKCLHYALLE LNLLSQNCDN LEKAEQIATI SANGEEQIGK LIAQAMERIG TDGVVSVEDA
     QGYDDELIFK EGLAFDRGYL SPYFINNHEK STVELNNPSI LLLDDKLTHM EDLLPLLEKL
     ANNRNPLLVI AEDINNEVLS RIIGNNMKNN LKVTVIKSPA FGSRRTEILQ DLAIYTGGTV
     ISPEIGMDLS EVDTDKLGNA SKIIITDSNT TIVHGEGDPQ LIMQRIKQLN SQLLNSSSEY
     DQKKLAERVA KLSGAIAIIK VGAATEVAMK EKKDRVEDAL HATKAAIKEG IVPGGGVAYI
     RIAQTLASLE GDNPDQSFGI KILLKAMESP LKQIAKNAGN EPVEVLSTIK KQTGNFGFDA
     KNDRYGDMME FGIIDPTKVT RCALEFAASI ASLILTTEVM VADMEDNNAN HANHDHAHSL
     NCSH