CH10_THET8
ID CH10_THET8 Reviewed; 101 AA.
AC P61493; P45747; Q5SLM1; Q60017;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=TTHA0272;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=8543569; DOI=10.1093/oxfordjournals.jbchem.a124913;
RA Amada K., Yohda M., Odaka M., Endo I., Ishii N., Taguchi H., Yoshida M.;
RT "Molecular cloning, expression, and characterization of chaperonin-60 and
RT chaperonin-10 from a thermophilic bacterium, Thermus thermophilus HB8.";
RL J. Biochem. 118:347-354(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Erbeznik M., Joachimiak A.;
RT "Cloning and characterization of the GroESL operon in Thermus aquaticus
RT HB8.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-24.
RX PubMed=1682319; DOI=10.1016/s0021-9258(18)54588-9;
RA Taguchi H., Konishi J., Ishii N., Yoshida M.;
RT "A chaperonin from a thermophilic bacterium, Thermus thermophilus, that
RT controls refoldings of several thermophilic enzymes.";
RL J. Biol. Chem. 266:22411-22418(1991).
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 -!- INTERACTION:
CC P61493; Q5SLM2: groEL; NbExp=2; IntAct=EBI-15757522, EBI-15757498;
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; D45880; BAA08298.1; -; Genomic_DNA.
DR EMBL; U29483; AAA83440.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70095.1; -; Genomic_DNA.
DR PIR; B39313; B39313.
DR RefSeq; WP_011174076.1; NC_006461.1.
DR RefSeq; YP_143538.1; NC_006461.1.
DR PDB; 1WNR; X-ray; 2.90 A; A/B/C/D/E/F/G=9-101.
DR PDBsum; 1WNR; -.
DR AlphaFoldDB; P61493; -.
DR SMR; P61493; -.
DR DIP; DIP-48332N; -.
DR IntAct; P61493; 1.
DR STRING; 300852.55771654; -.
DR EnsemblBacteria; BAD70095; BAD70095; BAD70095.
DR GeneID; 3168828; -.
DR KEGG; ttj:TTHA0272; -.
DR PATRIC; fig|300852.9.peg.272; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_2_0_0; -.
DR OMA; EVKYSGE; -.
DR PhylomeDB; P61493; -.
DR EvolutionaryTrace; P61493; -.
DR Proteomes; UP000000532; 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; Direct protein sequencing;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1682319"
FT CHAIN 2..101
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174886"
FT CONFLICT 20
FT /note="R -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..87
FT /note="DGEE -> APRRT (in Ref. 2; AAA83440)"
FT /evidence="ECO:0000305"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1WNR"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:1WNR"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1WNR"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1WNR"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:1WNR"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1WNR"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1WNR"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1WNR"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1WNR"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1WNR"
SQ SEQUENCE 101 AA; 10996 MW; 49DCA870AC325063 CRC64;
MAAEVKTVIK PLGDRVVVKR IEEEPKTKGG IVLPDTAKEK PQKGKVIAVG TGRVLENGQR
VPLEVKEGDI VVFAKYGGTE IEIDGEEYVI LSERDLLAVL Q
