CH10_CHLTA
ID CH10_CHLTA Reviewed; 102 AA.
AC Q3KMQ8; O84113;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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;
GN OrderedLocusNames=CTA_0118;
OS Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=315277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2196231; DOI=10.1128/iai.58.8.2701-2705.1990;
RA Morrison R.P., Su H., Lyng K., Yuan Y.;
RT "The Chlamydia trachomatis hyp operon is homologous to the groE stress
RT response operon of Escherichia coli.";
RL Infect. Immun. 58:2701-2705(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT genitotropic strains.";
RL Infect. Immun. 73:6407-6418(2005).
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; M31739; AAA03203.1; -; Unassigned_DNA.
DR EMBL; CP000051; AAX50364.1; -; Genomic_DNA.
DR PIR; B60273; B60273.
DR RefSeq; WP_009872382.1; NC_007429.1.
DR AlphaFoldDB; Q3KMQ8; -.
DR SMR; Q3KMQ8; -.
DR EnsemblBacteria; AAX50364; AAX50364; CTA_0118.
DR GeneID; 66303432; -.
DR KEGG; cta:CTA_0118; -.
DR HOGENOM; CLU_132825_2_1_0; -.
DR OMA; EVKYSGE; -.
DR Proteomes; UP000002532; 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; Stress response.
FT CHAIN 1..102
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174732"
SQ SEQUENCE 102 AA; 11183 MW; 19961A370F903AB6 CRC64;
MSDQATTLKI KPLGDRILVK REEEASTARG GIILPDTAKK KQDRAEVLAL GTGKKDDKGQ
QLPFEVQVGD IVLIDKYSGQ ELTVEGEEYV IVQMSEVIAV LQ
