CH10_LACLA
ID CH10_LACLA Reviewed; 94 AA.
AC P37283;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, 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}; OrderedLocusNames=LL0393;
GN ORFNames=L198515;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8486277; DOI=10.1016/0378-1119(93)90626-e;
RA Kim S.G., Batt C.A.;
RT "Cloning and sequencing of the Lactococcus lactis subsp. lactis groESL
RT operon.";
RL Gene 127:121-126(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(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; X71132; CAA50445.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK04491.1; -; Genomic_DNA.
DR PIR; JN0660; JN0660.
DR PIR; S32105; S32105.
DR RefSeq; NP_266549.1; NC_002662.1.
DR RefSeq; WP_003131589.1; NC_002662.1.
DR AlphaFoldDB; P37283; -.
DR SMR; P37283; -.
DR STRING; 272623.L198515; -.
DR PaxDb; P37283; -.
DR EnsemblBacteria; AAK04491; AAK04491; L198515.
DR GeneID; 60356372; -.
DR GeneID; 66441362; -.
DR KEGG; lla:L198515; -.
DR PATRIC; fig|272623.7.peg.427; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_2_1_9; -.
DR OMA; EVKYSGE; -.
DR Proteomes; UP000002196; 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..94
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174770"
SQ SEQUENCE 94 AA; 10221 MW; 291913B147CAA66B CRC64;
MLKPLENRVV LRVKEEEEKS MGGIVLTSAS QEKPQTAEVV AVGEGKTNHH GTLISPLVKV
GDTVIFEKFA GTTVKMDGEE FLILKDSDLL AIVE
