CH10_MYCLE
ID CH10_MYCLE Reviewed; 100 AA.
AC P24301;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Co-chaperonin GroES {ECO:0000255|HAMAP-Rule:MF_00580};
DE AltName: Full=10 kDa antigen;
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=chpA, groS {ECO:0000255|HAMAP-Rule:MF_00580}, mopB;
GN OrderedLocusNames=ML0380; ORFNames=B1620_C3_227, B229_C3_247;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-25.
RX PubMed=1730920; DOI=10.1084/jem.175.1.275;
RA Mehra V.L., Bloom B.R., Bajardi A.C., Grisso A.C., Sieling P.A., Alland D.,
RA Convit J., Fan X., Hunter S.W., Brennan P.J., Rea T.H., Modlin R.L.;
RT "A major T cell antigen of Mycobacterium leprae is a 10-kD heat-shock
RT cognate protein.";
RL J. Exp. Med. 175:275-284(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1354834; DOI=10.1111/j.1365-2958.1992.tb01372.x;
RA de Wit T.F.R., Bekelie S., Osland A., Miko T.L., Hermans P.W.M.,
RA van Soolingen D., Drijfhout J., Schoeningh R., Janson A.A.M., Thole J.E.R.;
RT "Mycobacteria contain two groEL genes: the second Mycobacterium leprae
RT groEL gene is arranged in an operon with groES.";
RL Mol. Microbiol. 6:1995-2007(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=8539620; DOI=10.1126/science.271.5246.203;
RA Mande S.C., Mehra V., Bloom B.R., Hol W.G.J.;
RT "Structure of the heat shock protein chaperonin-10 of Mycobacterium
RT leprae.";
RL Science 271:203-207(1996).
RN [6]
RP ERRATUM OF PUBMED:8539620.
RA Mande S.C., Mehra V., Bloom B.R., Hol W.G.J.;
RL Science 271:1655-1655(1996).
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; X59413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z11665; CAB63917.1; -; Genomic_DNA.
DR EMBL; U00015; AAC43227.1; -; Genomic_DNA.
DR EMBL; U00020; AAA17311.1; -; Genomic_DNA.
DR EMBL; AL583918; CAC29888.1; -; Genomic_DNA.
DR PIR; S25180; S25180.
DR PIR; S72818; S72818.
DR RefSeq; NP_301372.1; NC_002677.1.
DR RefSeq; WP_010907696.1; NC_002677.1.
DR PDB; 1LEP; X-ray; 3.50 A; A/B/C/D/E/F/G=2-100.
DR PDBsum; 1LEP; -.
DR AlphaFoldDB; P24301; -.
DR SMR; P24301; -.
DR STRING; 272631.ML0380; -.
DR EnsemblBacteria; CAC29888; CAC29888; CAC29888.
DR KEGG; mle:ML0380; -.
DR PATRIC; fig|272631.5.peg.642; -.
DR Leproma; ML0380; -.
DR eggNOG; COG0234; Bacteria.
DR HOGENOM; CLU_132825_2_0_11; -.
DR OMA; EVKYSGE; -.
DR EvolutionaryTrace; P24301; -.
DR Proteomes; UP000000806; 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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1730920"
FT CHAIN 2..100
FT /note="Co-chaperonin GroES"
FT /id="PRO_0000174786"
SQ SEQUENCE 100 AA; 10800 MW; A3BE12F8CA6764E2 CRC64;
MAKVKIKPLE DKILVQAGEA ETMTPSGLVI PENAKEKPQE GTVVAVGPGR WDEDGAKRIP
VDVSEGDIVI YSKYGGTEIK YNGEEYLILS ARDVLAVVSK
