ID   CH10_LEGPN              Reviewed;          96 AA.
AC   P26879;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 100.
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}, htpA;
OS   Legionella pneumophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=446;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SVir;
RX   PubMed=2205580; DOI=10.1128/iai.58.10.3380-3387.1990;
RA   Hoffman P.S., Houston L., Butler C.A.;
RT   "Legionella pneumophila htpAB heat shock operon: nucleotide sequence and
RT   expression of the 60-kilodalton antigen in L. pneumophila-infected HeLa
RT   cells.";
RL   Infect. Immun. 58:3380-3387(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-24.
RC   STRAIN=AA100 / Serogroup 1;
RX   PubMed=8454334; DOI=10.1128/iai.61.4.1320-1329.1993;
RA   Abu Kwaik Y., Eisenstein B.I., Engleberg N.C.;
RT   "Phenotypic modulation by Legionella pneumophila upon infection of
RT   macrophages.";
RL   Infect. Immun. 61:1320-1329(1993).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M31917; AAA25297.1; -; Genomic_DNA.
DR   PIR; B41468; B41468.
DR   RefSeq; WP_010946424.1; NZ_UGOV01000002.1.
DR   AlphaFoldDB; P26879; -.
DR   SMR; P26879; -.
DR   STRING; 91892.BIZ52_03750; -.
DR   GeneID; 66489874; -.
DR   eggNOG; COG0234; Bacteria.
DR   OMA; EVKYSGE; -.
DR   OrthoDB; 1965002at2; -.
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   CHAIN           1..96
FT                   /note="Co-chaperonin GroES"
FT                   /id="PRO_0000174776"
SQ   SEQUENCE   96 AA;  10475 MW;  E3AB920050F63639 CRC64;
     MKIRPLHDRV VVRRMEEERT TAGGIVIPDS ATEKPMRGEI IAVGAGKVLE NGDVRALAVK
     VGDVVLFGKY SGTEVKVDGK ELVVMREDDI MGVIEK