CH10_BUCAI
ID CH10_BUCAI Reviewed; 96 AA.
AC P25749;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 119.
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}, mopB, symS;
GN OrderedLocusNames=BU018;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1347769; DOI=10.1128/jb.174.6.1869-1874.1992;
RA Ohtaka C., Nakamura H., Ishikawa H.;
RT "Structures of chaperonins from an intracellular symbiont and their
RT functional expression in Escherichia coli groE mutants.";
RL J. Bacteriol. 174:1869-1874(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; X61150; CAA43459.1; -; Genomic_DNA.
DR EMBL; BA000003; BAB12745.1; -; Genomic_DNA.
DR RefSeq; NP_239859.1; NC_002528.1.
DR RefSeq; WP_009873979.1; NC_002528.1.
DR AlphaFoldDB; P25749; -.
DR SMR; P25749; -.
DR STRING; 107806.10038710; -.
DR EnsemblBacteria; BAB12745; BAB12745; BAB12745.
DR KEGG; buc:BU018; -.
DR PATRIC; fig|107806.10.peg.30; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_1_1_6; -.
DR OMA; RSINMTI; -.
DR Proteomes; UP000001806; 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; Reference proteome.
FT CHAIN 1..96
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174712"
SQ SEQUENCE 96 AA; 10244 MW; 23D60F9E3DD40645 CRC64;
MKIRPLHDRV LVKRQEVESK SAGGIVLTGS AAGKSTRGTV TAVGKGRVLD NGDIKPLDVK
VGDVVIFNEG YGAKTEKIDN EELLILTESD ILAIVE
