CH10_CHLTR
ID CH10_CHLTR Reviewed; 102 AA.
AC P0C0Z8; O84113;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=11.2 kDa stress response protein;
DE AltName: Full=Chaperonin-10 {ECO:0000255|HAMAP-Rule:MF_00580};
DE Short=Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=Heat shock protein 10;
DE Short=HSP10;
GN Name=groES {ECO:0000255|HAMAP-Rule:MF_00580};
GN Synonyms=groS {ECO:0000255|HAMAP-Rule:MF_00580}, hypA, mopB;
GN OrderedLocusNames=CT_111;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=L2;
RX PubMed=1987066; DOI=10.1128/iai.59.1.79-90.1991;
RA Cerrone M.C., Ma J.J., Stephens R.S.;
RT "Cloning and sequence of the gene for heat shock protein 60 from Chlamydia
RT trachomatis and immunological reactivity of the protein.";
RL Infect. Immun. 59:79-90(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; M58027; AAA23127.1; -; Genomic_DNA.
DR EMBL; AE001273; AAC67702.1; -; Genomic_DNA.
DR PIR; B60273; B60273.
DR PIR; B71555; B71555.
DR RefSeq; NP_219614.1; NC_000117.1.
DR RefSeq; WP_009871458.1; NC_000117.1.
DR AlphaFoldDB; P0C0Z8; -.
DR SMR; P0C0Z8; -.
DR STRING; 813.O172_00600; -.
DR EnsemblBacteria; AAC67702; AAC67702; CT_111.
DR GeneID; 884062; -.
DR KEGG; ctr:CT_111; -.
DR PATRIC; fig|272561.5.peg.121; -.
DR HOGENOM; CLU_132825_2_1_0; -.
DR InParanoid; P0C0Z8; -.
DR OMA; EVKYSGE; -.
DR Proteomes; UP000000431; 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 GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
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; Stress response.
FT CHAIN 1..102
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174731"
FT VARIANT 48
FT /note="L -> V (in strain: L2)"
FT VARIANT 65
FT /note="E -> V (in strain: L2)"
FT VARIANT 70
FT /note="N -> D (in strain: L2)"
SQ SEQUENCE 102 AA; 11182 MW; 1798FAD70F903AB6 CRC64;
MSDQATTLKI KPLGDRILVK REEEASTARG GIILPDTAKK KQDRAEVLAL GTGKKDDKGQ
QLPFEVQVGN IVLIDKYSGQ ELTVEGEEYV IVQMSEVIAV LQ
