GenomeNet

Database: UniProt
Entry: C1AHN1
LinkDB: C1AHN1
Original site: C1AHN1 
ID   CH10_MYCBT              Reviewed;         100 AA.
AC   C1AHN1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   29-OCT-2014, entry version 32.
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=JTY_3488;
OS   Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=561275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX   PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA   Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT   "Whole genome sequence analysis of Mycobacterium bovis bacillus
RT   Calmette-Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine
RT   substrains.";
RL   Vaccine 27:1710-1716(2009).
CC   -!- FUNCTION: Binds to Cpn60 in the presence of Mg-ATP and suppresses
CC       the ATPase activity of the latter. {ECO:0000255|HAMAP-
CC       Rule:MF_00580}.
CC   -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring.
CC       {ECO:0000255|HAMAP-Rule:MF_00580}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580}.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family.
CC       {ECO:0000255|HAMAP-Rule:MF_00580}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP010918; BAH27760.1; -; Genomic_DNA.
DR   RefSeq; YP_002646528.1; NC_012207.1.
DR   ProteinModelPortal; C1AHN1; -.
DR   SMR; C1AHN1; 2-100.
DR   STRING; 561275.JTY_3488; -.
DR   EnsemblBacteria; BAH27760; BAH27760; JTY_3488.
DR   GeneID; 7563283; -.
DR   KEGG; mbt:JTY_3488; -.
DR   PATRIC; 18026885; VBIMycBov85238_3804.
DR   eggNOG; COG0234; -.
DR   HOGENOM; HOG000133897; -.
DR   KO; K04078; -.
DR   OMA; DEGENRI; -.
DR   OrthoDB; EOG6GFGSD; -.
DR   BioCyc; MBOV561275:GHDN-3525-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.30.33.40; -; 1.
DR   HAMAP; MF_00580; CH10; 1.
DR   InterPro; IPR020818; Chaperonin_Cpn10.
DR   InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR   InterPro; IPR011032; GroES-like.
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;
KW   Chaperone; Complete proteome; Cytoplasm.
FT   CHAIN         1    100       10 kDa chaperonin.
FT                                /FTId=PRO_1000146911.
SQ   SEQUENCE   100 AA;  10804 MW;  DE448187A56103FE CRC64;
     MAKVNIKPLE DKILVQANEA ETTTASGLVI PDTAKEKPQE GTVVAVGPGR WDEDGEKRIP
     LDVAEGDTVI YSKYGGTEIK YNGEEYLILS ARDVLAVVSK
//
DBGET integrated database retrieval system