ID   CH10_MYCBO              Reviewed;         100 AA.
AC   P15020; A0A1R3Y454; X2BNN5;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 142.
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};
DE   AltName: Full=Immunogenic protein MPB57;
GN   Name=groES {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groS {ECO:0000255|HAMAP-Rule:MF_00580}, mopB;
GN   OrderedLocusNames=BQ2027_MB3452C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=BCG;
RX   PubMed=3056744; DOI=10.1016/0014-5793(88)80350-8;
RA   Yamaguchi R., Matsuo K., Yamazaki A., Nagai S., Terasaka K., Yamada T.;
RT   "Immunogenic protein MPB57 from Mycobacterium bovis BCG: molecular cloning,
RT   nucleotide sequence and expression.";
RL   FEBS Lett. 240:115-117(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-20.
RC   STRAIN=AN-5;
RX   PubMed=1900061; DOI=10.1128/iai.59.3.800-807.1991;
RA   Fifis T., Costopoulos C., Radford A.J., Bacic A., Wood P.R.;
RT   "Purification and characterization of major antigens from a Mycobacterium
RT   bovis culture filtrate.";
RL   Infect. Immun. 59:800-807(1991).
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; X13970; CAA32149.1; -; Genomic_DNA.
DR   EMBL; M35389; AAA25365.1; -; Genomic_DNA.
DR   EMBL; LT708304; SIU02080.1; -; Genomic_DNA.
DR   PIR; S01784; BVMY7B.
DR   RefSeq; NP_857092.1; NC_002945.3.
DR   RefSeq; WP_003418028.1; NC_002945.4.
DR   AlphaFoldDB; P15020; -.
DR   SMR; P15020; -.
DR   EnsemblBacteria; SIU02080; SIU02080; BQ2027_MB3452C.
DR   GeneID; 66599586; -.
DR   PATRIC; fig|233413.5.peg.3787; -.
DR   OMA; EVKYSGE; -.
DR   Proteomes; UP000001419; 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   Chaperone; Cytoplasm; Direct protein sequencing; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1900061,
FT                   ECO:0000269|PubMed:3056744"
FT   CHAIN           2..100
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174785"
FT   CONFLICT        16
FT                   /note="Q -> E (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95..99
FT                   /note="LAVVS -> VGRRF (in Ref. 1; CAA32149)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   100 AA;  10804 MW;  DE448187A56103FE CRC64;
     MAKVNIKPLE DKILVQANEA ETTTASGLVI PDTAKEKPQE GTVVAVGPGR WDEDGEKRIP
     LDVAEGDTVI YSKYGGTEIK YNGEEYLILS ARDVLAVVSK