CH10_LISMO
ID CH10_LISMO Reviewed; 94 AA.
AC Q9AGE7; Q8Y5J2;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 118.
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}; OrderedLocusNames=lmo2069;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=11349060; DOI=10.1128/iai.69.6.3924-3932.2001;
RA Gahan C.G., O'Mahony J., Hill C.;
RT "Characterization of the groESL operon in Listeria monocytogenes:
RT utilization of two reporter systems (gfp and hly) for evaluating in vivo
RT expression.";
RL Infect. Immun. 69:3924-3932(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AF335323; AAK28537.1; -; Genomic_DNA.
DR EMBL; AL591982; CAD00147.1; -; Genomic_DNA.
DR PIR; AE1333; AE1333.
DR RefSeq; NP_465593.1; NC_003210.1.
DR RefSeq; WP_003726504.1; NZ_CP023861.1.
DR AlphaFoldDB; Q9AGE7; -.
DR SMR; Q9AGE7; -.
DR STRING; 169963.lmo2069; -.
DR PaxDb; Q9AGE7; -.
DR EnsemblBacteria; CAD00147; CAD00147; CAD00147.
DR GeneID; 61171340; -.
DR GeneID; 985586; -.
DR KEGG; lmo:lmo2069; -.
DR PATRIC; fig|169963.11.peg.2117; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_2_0_9; -.
DR OMA; EVKYSGE; -.
DR PhylomeDB; Q9AGE7; -.
DR BioCyc; LMON169963:LMO2069-MON; -.
DR Proteomes; UP000000817; 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.
FT CHAIN 1..94
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174782"
FT CONFLICT 48
FT /note="L -> P (in Ref. 1; AAK28537)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 94 AA; 10064 MW; A25A8AE9B526886A CRC64;
MLKPLGDRVV IEVLEAEEKT ASGIVLPDSA KEKPQSGKIV AVGSGRVLDN GTKEPLEVAE
GDTVIFAKYS GTEVTYEGTD YLILRESDIL AITK
