CH601_SYNP6
ID CH601_SYNP6 Reviewed; 544 AA.
AC P12834; Q5N141;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Chaperonin GroEL 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=cpn60, groL, groL1 {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
GN OrderedLocusNames=syc1789_d;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-300.
RX PubMed=3041005; DOI=10.1016/0022-2836(87)90667-x;
RA Cozens A.L., Walker J.E.;
RT "The organization and sequence of the genes for ATP synthase subunits in
RT the cyanobacterium Synechococcus 6301. Support for an endosymbiotic origin
RT of chloroplasts.";
RL J. Mol. Biol. 194:359-383(1987).
RN [3]
RP SIMILARITY TO CHAPERONINS.
RX PubMed=2505234; DOI=10.1093/nar/17.15.6392;
RA Cookson M.J., Baird P.N., Hall L.M., Coates A.R.M.;
RT "Identification of two unknown reading frames in Synechococcus 6301 as
RT homologues of the 10k and 65k antigen genes of Mycobacterium tuberculosis
RT and related heat shock genes in E. coli and Coxiella burnetii.";
RL Nucleic Acids Res. 17:6392-6392(1989).
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; AP008231; BAD79979.1; -; Genomic_DNA.
DR EMBL; X05925; CAA29360.1; -; Genomic_DNA.
DR RefSeq; WP_011244099.1; NC_006576.1.
DR AlphaFoldDB; P12834; -.
DR SMR; P12834; -.
DR STRING; 269084.syc1789_d; -.
DR EnsemblBacteria; BAD79979; BAD79979; syc1789_d.
DR KEGG; syc:syc1789_d; -.
DR eggNOG; COG0459; Bacteria.
DR OMA; TDTDKME; -.
DR PRO; PR:P12834; -.
DR Proteomes; UP000001175; 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; 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.
FT CHAIN 1..544
FT /note="Chaperonin GroEL 1"
FT /id="PRO_0000063567"
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 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 544 AA; 57980 MW; 75CF9DDF02B194B9 CRC64;
MAKRIIYNEN ARRALEKGID ILAEAVAVTL GPKGRNVVLE KKFGAPQIIN DGVTIAKEIE
LEDHIENTGV ALIRQAASKT NDAAGDGTTT ATVLAHAVVK EGLRNVAAGA NAILLKRGID
KATNFLVEQI KSHARPVEDS KSIAQVGAIS AGNDFEVGQM IADAMDKVGK EGVISLEEGK
SMTTELEVTE GMRFDKGYIS PYFATDTERM EAVFDEPFIL ITDKKIGLVQ DLVPVLEQVA
RAGRPLVIIA EDIEKEALAT LVVNRLRGVL NVAAVKAPGF GDRRKAMLED IAVLTGGQLI
TEDAGLKLDT TKLDQLGKAR RITITKDNTT IVAEGNEAAV KARVDQIRRQ IEETESSYDK
EKLQERLAKL SGGVAVVKVG AATETEMKDR KLRLEDAINA TKAAVEEGIV PGGGTTLAHL
APQLEEWATA NLSGEELTGA QIVARALTAP LKRIAENAGL NGAVISERVK ELPFDEGYDA
SNNQFVNMFT AGIVDPAKVT RSALQNAASI AAMVLTTECI VVDKPEPKEK APAGAGGGMG
DFDY
