CH10_PORGI
ID CH10_PORGI Reviewed; 89 AA.
AC P42376;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=PG_0521;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7913687; DOI=10.1111/j.1574-6968.1994.tb06879.x;
RA Maeda H., Miyamoto M., Hongyou H., Kitanaka M., Nagai A., Kurihara H.,
RA Murayama Y.;
RT "Heat shock protein 60 (GroEL) from Porphyromonas gingivalis: molecular
RT cloning and sequence analysis of its gene and purification of the
RT recombinant protein.";
RL FEMS Microbiol. Lett. 119:129-135(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=381;
RX PubMed=8086460; DOI=10.1016/0167-4781(94)90265-8;
RA Hotokezaka H., Hayashida H., Ohara N., Nomaguchi H., Kobayashi K.,
RA Yamada T.;
RT "Cloning and sequencing of the groESL homologue from Porphyromonas
RT gingivalis.";
RL Biochim. Biophys. Acta 1219:175-178(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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; D17398; BAA04221.1; -; Genomic_DNA.
DR EMBL; D17342; BAA04160.1; -; Genomic_DNA.
DR EMBL; AE015924; AAQ65715.1; -; Genomic_DNA.
DR RefSeq; WP_004585060.1; NC_002950.2.
DR AlphaFoldDB; P42376; -.
DR SMR; P42376; -.
DR STRING; 242619.PG_0521; -.
DR EnsemblBacteria; AAQ65715; AAQ65715; PG_0521.
DR GeneID; 29256635; -.
DR GeneID; 57240622; -.
DR KEGG; pgi:PG_0521; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_2_0_10; -.
DR OMA; EVKYSGE; -.
DR OrthoDB; 1965002at2; -.
DR Proteomes; UP000000588; 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..89
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174802"
SQ SEQUENCE 89 AA; 9612 MW; 8DE8978E7645B92A CRC64;
MNIKPLADRV LVKPAAAEEK TVSGIIIPDS AKEKPLKGEV IAVGNGTKDE EMVLKAGDTV
LYGKYAGTEI ELEGEKYIIM RQNDVLAII
