CH10_THET2
ID CH10_THET2 Reviewed; 101 AA.
AC P61492; P45747; Q60017;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
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=chpS, groS {ECO:0000255|HAMAP-Rule:MF_00580}, hsp10;
GN OrderedLocusNames=TT_C1713;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Boskocik J., Moreno R., Valpuesta J.M., Berenguer J.;
RT "Characterization of the cpn10-cpn60 chaperonine from Thermus thermophilus
RT HB27.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AJ250409; CAB65481.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS82055.1; -; Genomic_DNA.
DR RefSeq; WP_011174076.1; NC_005835.1.
DR PDB; 4V4O; X-ray; 2.80 A; O/P/Q/R/S/T/U/o/p/q/r/s/t/u=2-101.
DR PDBsum; 4V4O; -.
DR AlphaFoldDB; P61492; -.
DR SMR; P61492; -.
DR STRING; 262724.TT_C1713; -.
DR PRIDE; P61492; -.
DR EnsemblBacteria; AAS82055; AAS82055; TT_C1713.
DR GeneID; 3168828; -.
DR KEGG; tth:TT_C1713; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_2_0_0; -.
DR OMA; EVKYSGE; -.
DR OrthoDB; 1965002at2; -.
DR EvolutionaryTrace; P61492; -.
DR Proteomes; UP000000592; 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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..101
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174885"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:4V4O"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:4V4O"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4V4O"
SQ SEQUENCE 101 AA; 10996 MW; 49DCA870AC325063 CRC64;
MAAEVKTVIK PLGDRVVVKR IEEEPKTKGG IVLPDTAKEK PQKGKVIAVG TGRVLENGQR
VPLEVKEGDI VVFAKYGGTE IEIDGEEYVI LSERDLLAVL Q
