ID   CH602_ECOK1             Reviewed;         545 AA.
AC   Q19NJ4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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};
GN   Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   OrderedLocusNames=Ecok1_R_48900; ORFNames=APECO1_O1R91, O1R_91;
OS   Escherichia coli O1:K1 / APEC.
OG   Plasmid pAPEC-O1-R.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16940062; DOI=10.1128/aac.00569-06;
RA   Johnson T.J., Wannemeuhler Y.M., Scaccianoce J.A., Johnson S.J.,
RA   Nolan L.K.;
RT   "Complete DNA sequence, comparative genomics, and prevalence of an IncHI2
RT   plasmid occurring among extraintestinal pathogenic Escherichia coli
RT   isolates.";
RL   Antimicrob. Agents Chemother. 50:3929-3933(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ517526; ABF67773.1; -; Genomic_DNA.
DR   RefSeq; WP_000719078.1; NC_009838.1.
DR   AlphaFoldDB; Q19NJ4; -.
DR   SMR; Q19NJ4; -.
DR   PRIDE; Q19NJ4; -.
DR   EnsemblBacteria; ABF67773; ABF67773; APECO1_O1R91.
DR   KEGG; ecv:APECO1_O1R91; -.
DR   HOGENOM; CLU_016503_3_0_6; -.
DR   OMA; PYILINQ; -.
DR   Proteomes; UP000008216; Plasmid pAPEC-O1-R.
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; Plasmid.
FT   CHAIN           1..545
FT                   /note="Chaperonin GroEL 2"
FT                   /id="PRO_0000332000"
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         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;  57206 MW;  AEA8D879DE2E5AC4 CRC64;
     MAAKDIRFGE DARARMVRGV NVLANAVKAT LGPKGRNVVL EKSFGAPTIT KDGVSVAKEI
     ELADKFENMG AQMVKEVASK TSDNAGDGTT TATVLAQALI REGMKAVAAG MNPMDLKRGI
     DKAVTSAVEE LKKISKPCST SKEIAQVGSI SANSDTDIGE LIAKAMDKVG KEGVITVEEG
     SGLENELDVV EGMQFDRGYL SPYFINNPQS MQAELEDPFI LLHDKKISNV RDLLPILEGV
     AKAGKPLLIV AEDVEGEALA TLVVNTIRGI VKVCAVKAPG FGDRRKAMLE DMAILTGGTV
     ISEEVGLSLE KATINDLGRA KKVQVSKENT TIIDGAGDTA DIEARIKQIK AQIEETTSDY
     DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG IVPGGGVALI
     RAKAAIAELK GANEDQNHGI AIALRAMEAP LREIVTNAGD EPSVVLNRVA EGTGAFGYNA
     ANGEFGDMIE FGILDPTKVT RSALQNAASI AGLMITTEAM VAEAPKKEEP AAPGGGMGGM
     GGMDF