(data stored in ACNUC30630 zone)

SWISSPROT: CH10_BIFAA

ID   CH10_BIFAA              Reviewed;          97 AA.
AC   A1A040;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   11-DEC-2019, entry version 76.
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=BAD_0292;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-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; AP009256; BAF39073.1; -; Genomic_DNA.
DR   RefSeq; WP_011742802.1; NC_008618.1.
DR   SMR; A1A040; -.
DR   PRIDE; A1A040; -.
DR   EnsemblBacteria; BAF39073; BAF39073; BAD_0292.
DR   GeneID; 4556140; -.
DR   KEGG; bad:BAD_0292; -.
DR   eggNOG; ENOG4105K5Y; Bacteria.
DR   eggNOG; COG0234; LUCA.
DR   HOGENOM; HOG000133897; -.
DR   KO; K04078; -.
DR   OMA; PGRIDDN; -.
DR   BioCyc; BADO367928:G1G2R-318-MONOMER; -.
DR   Proteomes; UP000008702; Chromosome.
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; A1A040.
DR   SWISS-2DPAGE; A1A040.
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..97
FT                   /note="10 kDa chaperonin"
FT                   /id="PRO_1000025216"
SQ   SEQUENCE   97 AA;  10483 MW;  85FE81651A58BE64 CRC64;
     MSISLTPLED KIIVKQAEAE TQTASGLFIP DNAKEKPQQG EVLAVGPGRR NDAGERIPVD
     VKVGDKVLYS KYGGTEVHYQ GEDYLIVSAR DILAILG
//

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