CH10_RIPO1
ID CH10_RIPO1 Reviewed; 103 AA.
AC Q8L373; B7JV02;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 90.
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=PCC8801_2855;
OS Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX NCBI_TaxID=41431;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lin R.-F., Huang T.-C.;
RT "Chaperonin containing sequence in Synechococcus RF-1.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 8801;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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}.
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DR EMBL; AF373777; AAM20895.1; -; Genomic_DNA.
DR EMBL; CP001287; ACK66854.1; -; Genomic_DNA.
DR RefSeq; WP_012596120.1; NC_011726.1.
DR AlphaFoldDB; Q8L373; -.
DR SMR; Q8L373; -.
DR STRING; 41431.PCC8801_2855; -.
DR EnsemblBacteria; ACK66854; ACK66854; PCC8801_2855.
DR KEGG; cyp:PCC8801_2855; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_2_1_3; -.
DR OMA; EVKYSGE; -.
DR OrthoDB; 1965002at2; -.
DR Proteomes; UP000008204; 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; Reference proteome.
FT CHAIN 1..103
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174877"
FT CONFLICT 101
FT /note="V -> I (in Ref. 1; AAM20895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 10888 MW; 57214169C45E9BB5 CRC64;
MAAISINVST VKPLGDRVFV KVSASEEKTA GGILLPDTAK EKPQIGEIVT VGPGKRNDDG
SRSEPEVKVG DKVLYSKYAG TDIKLGGEDY VLLSEKDILA VVD
