CH10_ACEP3
ID CH10_ACEP3 Reviewed; 97 AA.
AC Q8GBD3; C7JC83;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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};
GN OrderedLocusNames=APA01_17860;
OS Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=634452;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01;
RX PubMed=16233284; DOI=10.1263/jbb.94.140;
RA Okamoto-Kainuma A., Yan W., Kadono S., Tayama K., Koizumi Y., Yanagida F.;
RT "Cloning and characterization of groESL operon in Acetobacter aceti.";
RL J. Biosci. Bioeng. 94:140-147(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01;
RX PubMed=19638423; DOI=10.1093/nar/gkp612;
RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT "Whole-genome analyses reveal genetic instability of Acetobacter
RT pasteurianus.";
RL Nucleic Acids Res. 37:5768-5783(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH99911.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB081586; BAC16231.1; -; Genomic_DNA.
DR EMBL; AP011121; BAH99911.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_026019247.1; NC_013209.1.
DR AlphaFoldDB; Q8GBD3; -.
DR SMR; Q8GBD3; -.
DR STRING; 634452.APA01_17860; -.
DR EnsemblBacteria; BAH99911; BAH99911; APA01_17860.
DR GeneID; 60376732; -.
DR GeneID; 66351960; -.
DR KEGG; apt:APA01_17860; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_1_0_5; -.
DR OMA; EVKYSGE; -.
DR Proteomes; UP000000948; 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..97
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174677"
SQ SEQUENCE 97 AA; 10514 MW; 4DF9365DE3CDA23E CRC64;
MTKFRPLHDR VVVRRLEGEQ KTAGGIIIPD TAQEKPMEGE VVAVGPGARN EQGQIVALDV
KAGDRVLFGK WSGTEVKIDG EELLIMKESD IMGVVTA
