(data stored in ACNUC30630 zone)

SWISSPROT: CH10_CORGB

ID   CH10_CORGB              Reviewed;          99 AA.
AC   A4QBT9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   11-DEC-2019, entry version 69.
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=cgR_0715;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
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; AP009044; BAF53686.1; -; Genomic_DNA.
DR   RefSeq; WP_003854559.1; NC_009342.1.
DR   SMR; A4QBT9; -.
DR   EnsemblBacteria; BAF53686; BAF53686; cgR_0715.
DR   KEGG; cgt:cgR_0715; -.
DR   HOGENOM; HOG000133897; -.
DR   KO; K04078; -.
DR   OMA; PGRIDDN; -.
DR   BioCyc; CGLU340322:G1G2L-755-MONOMER; -.
DR   Proteomes; UP000006698; 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; A4QBT9.
DR   SWISS-2DPAGE; A4QBT9.
KW   Chaperone; Cytoplasm.
FT   CHAIN           1..99
FT                   /note="10 kDa chaperonin"
FT                   /id="PRO_1000025244"
SQ   SEQUENCE   99 AA;  10769 MW;  678F9895E304F1E0 CRC64;
     MANVNIKPLE DKILVQINEA ETTTASGLVI PDSAKEKPQE ATVIAVGPGR FDDKGNRIPL
     DIKEDDVVIF SRYGGTEIKF GGVEYLLLSA RDILAIVEK
//

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