ID   CH10_MYCAV              Reviewed;         100 AA.
AC   P60532; O86017;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 80.
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=groS {ECO:0000255|HAMAP-Rule:MF_00580}, mopB;
OS   Mycobacterium avium.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=485 Type 21;
RA   Creti R., Pietrobono R., Fattorini L., Orefici G.;
RT   "Sequence of the GroESL operon of Mycobacterium avium comprising the gene
RT   encoding the cpn10 protein and a portion of the gene encoding the cpn60-1
RT   protein.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25291 / DSM 44156 / NCTC 13034 / TMC 724;
RX   PubMed=10392775; DOI=10.1016/s0378-1135(99)00019-x;
RA   Cobb A.J., Frothingham R.;
RT   "The GroES antigens of Mycobacterium avium and Mycobacterium
RT   paratuberculosis.";
RL   Vet. Microbiol. 67:31-35(1999).
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; AF079544; AAC31921.1; -; Genomic_DNA.
DR   EMBL; AF071828; AAD23276.1; -; Genomic_DNA.
DR   RefSeq; WP_003873391.1; NZ_NSFM01000032.1.
DR   AlphaFoldDB; P60532; -.
DR   SMR; P60532; -.
DR   GeneID; 66695550; -.
DR   OMA; EVKYSGE; -.
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; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..100
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174784"
SQ   SEQUENCE   100 AA;  10748 MW;  A89FEDF7B9C389CB CRC64;
     MAKVNIKPLE DKILVQANEA ETTTASGLVI PDTAKEKPQE GTVVAVGPGR WDDDGAKRIP
     LDVSEGDTVI YSKYGGTEIK YNGEEYLILS ARDVLAVVSK