CH602_SYNY3
ID CH602_SYNY3 Reviewed; 552 AA.
AC P22034;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 156.
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=cpn60-2, groL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN OrderedLocusNames=sll0416;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1670771; DOI=10.1016/s0021-9258(18)52401-7;
RA Chitnis P.R., Nelson N.;
RT "Molecular cloning of the genes encoding two chaperone proteins of the
RT cyanobacterium Synechocystis sp. PCC 6803.";
RL J. Biol. Chem. 266:58-65(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [4]
RP PROTEIN SEQUENCE OF 2-10.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
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 -!- INDUCTION: By stress conditions e.g. heat shock.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; M57517; AAA27284.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA10240.1; -; Genomic_DNA.
DR PIR; S74322; S74322.
DR AlphaFoldDB; P22034; -.
DR SMR; P22034; -.
DR IntAct; P22034; 1.
DR STRING; 1148.1001103; -.
DR PaxDb; P22034; -.
DR PRIDE; P22034; -.
DR EnsemblBacteria; BAA10240; BAA10240; BAA10240.
DR KEGG; syn:sll0416; -.
DR eggNOG; COG0459; Bacteria.
DR InParanoid; P22034; -.
DR OMA; PYILINQ; -.
DR PhylomeDB; P22034; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW Nucleotide-binding; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298645"
FT CHAIN 2..552
FT /note="Chaperonin GroEL 2"
FT /id="PRO_0000063576"
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 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 152..153
FT /note="ND -> TN (in Ref. 1; AAA27284)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="Missing (in Ref. 1; AAA27284)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="D -> H (in Ref. 1; AAA27284)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="A -> R (in Ref. 1; AAA27284)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="A -> P (in Ref. 1; AAA27284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 57774 MW; 106B30E99515E8AA CRC64;
MSKLISFKDE SRRSLEAGIN ALADAVRITL GPKGRNVLLE KQYGAPQIVN DGITVAKEIE
LSNPEENAGA KLIQEVASKT KEIAGDGTTT ATIIAQALVR EGLRNVAAGA NPVALRRGIE
KVTTFLVQEI EAVAKPVEGS AIAQVATVSS GNDPEVGAMI ADAMDKVTKD GVITVEESKS
LNTELEVVEG MQIDRGYISP YFITDSDRQL VEFDNPLILI TDKKISAIAE LVPVLEAVAR
AGRPLLIIAE DIEGEALATL VVNKARGVLN VAAIKAPAFG DRRKAVLQDI AILTGGSVIS
EDIGLSLDTV SLDQLGQAVK ATLEKDNTIL VAGADKRASA GVKERIEQLR KEYAASDSDY
DKEKIQERIA KLAGGVAVIK VGAATETELK DRKLRIEDAL NATKAAVEEG IVPGGGTTLI
RLAGKIESFK AQLSNDEERV AADIIAKALE APLHQLASNA GVEGSVIVEK VKEATGNQGY
NVITGKIEDL IAAGIIDPAK VVRSALQNAA SIAGMVLTTE ALVVEKPEPA APAMPDMGGM
GGMGGMGGMG MM
