CH10_SYNE7
ID CH10_SYNE7 Reviewed; 103 AA.
AC P22880; Q31KS5;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
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=Synpcc7942_2314;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1975581; DOI=10.1128/jb.172.9.5079-5088.1990;
RA Webb R., Reddy K.J., Sherman L.A.;
RT "Regulation and sequence of the Synechococcus sp. strain PCC 7942 groESL
RT operon, encoding a cyanobacterial chaperonin.";
RL J. Bacteriol. 172:5079-5088(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; M58751; AAA27313.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58344.1; -; Genomic_DNA.
DR PIR; A36721; A36721.
DR RefSeq; WP_011244098.1; NC_007604.1.
DR AlphaFoldDB; P22880; -.
DR SMR; P22880; -.
DR STRING; 1140.Synpcc7942_2314; -.
DR PRIDE; P22880; -.
DR EnsemblBacteria; ABB58344; ABB58344; Synpcc7942_2314.
DR KEGG; syf:Synpcc7942_2314; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_2_1_3; -.
DR OMA; EVKYSGE; -.
DR OrthoDB; 1965002at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2314-MON; -.
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_0000174876"
FT CONFLICT 56
FT /note="R -> S (in Ref. 1; AAA27313)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 10811 MW; FFED1DE5F515952F CRC64;
MAAVSLSVST VTPLGDRVFV KVAEAEEKTA GGIILPDNAK EKPQVGEIVA VGPGKRNDDG
SRQAPEVKIG DKVLYSKYAG TDIKLGNDDY VLLSEKDILA VVA