CH101_RHILO
ID CH101_RHILO Reviewed; 104 AA.
AC Q98IV4;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Co-chaperonin GroES 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=10 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=Chaperonin-10 1 {ECO:0000255|HAMAP-Rule:MF_00580};
DE Short=Cpn10 1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN Name=groES1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN Synonyms=groS1 {ECO:0000255|HAMAP-Rule:MF_00580};
GN OrderedLocusNames=mll2233;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(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; BA000012; BAB49412.1; -; Genomic_DNA.
DR RefSeq; WP_010910764.1; NC_002678.2.
DR AlphaFoldDB; Q98IV4; -.
DR SMR; Q98IV4; -.
DR STRING; 266835.14022804; -.
DR EnsemblBacteria; BAB49412; BAB49412; BAB49412.
DR GeneID; 66682827; -.
DR KEGG; mlo:mll2233; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_1_0_5; -.
DR OMA; MKETDIM; -.
DR OrthoDB; 1965002at2; -.
DR Proteomes; UP000000552; 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.
FT CHAIN 1..104
FT /note="Co-chaperonin GroES 1"
FT /id="PRO_0000174812"
SQ SEQUENCE 104 AA; 11178 MW; 29B9D984625C2258 CRC64;
MKFRPLHDRV VIRRAEGDTK SKGGIIIPDN AKEKPQEGEV IAVGPGARDE NGALVPLDVK
AGDLILFGKW SGTEVKIDGE DLLIMKEADI MGVIDKSVEA KKAA
