(data stored in ACNUC7421 zone)

SWISSPROT: CH10_LEGPC

ID   CH10_LEGPC              Reviewed;          96 AA.
AC   A5IGM2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 67.
DE   RecName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=GroES protein {ECO:0000255|HAMAP-Rule:MF_00580};
DE   AltName: Full=Protein Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Name=groS {ECO:0000255|HAMAP-Rule:MF_00580};
GN   Synonyms=groES {ECO:0000255|HAMAP-Rule:MF_00580};
GN   OrderedLocusNames=LPC_2607;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to Cpn60 in the presence of Mg-ATP and suppresses the
CC       ATPase activity of the latter. {ECO:0000255|HAMAP-Rule:MF_00580}.
CC   -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; CP000675; ABQ56522.1; -; Genomic_DNA.
DR   RefSeq; WP_010946424.1; NC_009494.2.
DR   SMR; A5IGM2; -.
DR   EnsemblBacteria; ABQ56522; ABQ56522; LPC_2607.
DR   KEGG; lpc:LPC_2607; -.
DR   HOGENOM; HOG000133897; -.
DR   KO; K04078; -.
DR   OMA; PGRIDDN; -.
DR   BioCyc; LPNE400673:LPC_RS03890-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; A5IGM2.
DR   SWISS-2DPAGE; A5IGM2.
KW   Chaperone; Cytoplasm.
FT   CHAIN           1..96
FT                   /note="10 kDa chaperonin"
FT                   /id="PRO_1000025290"
SQ   SEQUENCE   96 AA;  10475 MW;  E3AB920050F63639 CRC64;
     MKIRPLHDRV VVRRMEEERT TAGGIVIPDS ATEKPMRGEI IAVGAGKVLE NGDVRALAVK
     VGDVVLFGKY SGTEVKVDGK ELVVMREDDI MGVIEK
//

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