CH10_SYNP6
ID CH10_SYNP6 Reviewed; 103 AA.
AC P07889;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Co-chaperonin GroES {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=Chaperonin-10 {ECO:0000255|HAMAP-Rule:MF_00580};
DE Short=Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580};
GN Name=groES {ECO:0000255|HAMAP-Rule:MF_00580};
GN Synonyms=groS {ECO:0000255|HAMAP-Rule:MF_00580};
GN OrderedLocusNames=syc1788_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 [GENOMIC DNA].
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 [2]
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 [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 the chaperonin GroEL, plays an essential role
CC in assisting protein folding. The GroEL-GroES system forms a nano-cage
CC that allows encapsulation of the non-native substrate proteins and
CC provides a physical environment optimized to promote and accelerate
CC protein folding. GroES binds to the apical surface of the GroEL ring,
CC thereby capping the opening of the GroEL channel. {ECO:0000255|HAMAP-
CC Rule:MF_00580}.
CC -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. Interacts with the
CC chaperonin GroEL. {ECO:0000255|HAMAP-Rule:MF_00580}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580}.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000255|HAMAP-
CC Rule:MF_00580, ECO:0000305}.
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DR EMBL; X05925; CAA29361.1; -; Genomic_DNA.
DR EMBL; AP008231; BAD79978.1; -; Genomic_DNA.
DR PIR; S10836; BVYCGS.
DR RefSeq; WP_011244098.1; NC_006576.1.
DR AlphaFoldDB; P07889; -.
DR SMR; P07889; -.
DR STRING; 269084.syc1788_d; -.
DR EnsemblBacteria; BAD79978; BAD79978; syc1788_d.
DR KEGG; syc:syc1788_d; -.
DR eggNOG; COG0234; Bacteria.
DR OMA; EVKYSGE; -.
DR Proteomes; UP000001175; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd00320; cpn10; 1.
DR Gene3D; 2.30.33.40; -; 1.
DR HAMAP; MF_00580; CH10; 1.
DR InterPro; IPR020818; Chaperonin_GroES.
DR InterPro; IPR037124; Chaperonin_GroES_sf.
DR InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR PANTHER; PTHR10772; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 1.
DR PRINTS; PR00297; CHAPERONIN10.
DR SMART; SM00883; Cpn10; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm.
FT CHAIN 1..103
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174875"
SQ SEQUENCE 103 AA; 10811 MW; FFED1DE5F515952F CRC64;
MAAVSLSVST VTPLGDRVFV KVAEAEEKTA GGIILPDNAK EKPQVGEIVA VGPGKRNDDG
SRQAPEVKIG DKVLYSKYAG TDIKLGNDDY VLLSEKDILA VVA