(data stored in ACNUC7421 zone)

SWISSPROT: CH60_EDWI9

ID   CH60_EDWI9              Reviewed;         547 AA.
AC   C5BDK5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 46.
DE   RecName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=GroEL protein {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Protein Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groL {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN   OrderedLocusNames=NT01EI_0380;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Prevents misfolding and promotes the refolding and
CC       proper assembly of unfolded polypeptides generated under stress
CC       conditions. {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of
CC       7 subunits. {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
DR   EMBL; CP001600; ACR67621.1; -; Genomic_DNA.
DR   RefSeq; WP_015869827.1; NC_012779.2.
DR   SMR; C5BDK5; -.
DR   STRING; 634503.NT01EI_0380; -.
DR   PRIDE; C5BDK5; -.
DR   EnsemblBacteria; ACR67621; ACR67621; NT01EI_0380.
DR   GeneID; 7960160; -.
DR   KEGG; eic:NT01EI_0380; -.
DR   PATRIC; fig|634503.3.peg.344; -.
DR   eggNOG; ENOG4105CJ9; Bacteria.
DR   eggNOG; COG0459; LUCA.
DR   HOGENOM; HOG000076290; -.
DR   KO; K04077; -.
DR   OMA; TDTDKME; -.
DR   OrthoDB; POG091H00E7; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   Gene3D; 1.10.560.10; -; 2.
DR   Gene3D; 3.50.7.10; -; 1.
DR   HAMAP; MF_00600; CH60; 1.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR   InterPro; IPR001844; Chaprnin_Cpn60.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom.
DR   InterPro; IPR027413; GROEL-like_equatorial.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BDK5.
DR   SWISS-2DPAGE; C5BDK5.
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    547       60 kDa chaperonin.
FT                                /FTId=PRO_1000212196.
SQ   SEQUENCE   547 AA;  57394 MW;  5991926C445DAF97 CRC64;
     MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGSPAIT KDGVSVAREI
     ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAIV NEGLKAVAAG MNPMDLKRGI
     DKAVSAAVEE LKALSVPCSD SKAIAQVGTI SANADDTVGQ LIAEAMEKVG KEGVITVEEG
     TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV
     AKAGKPLLII AEDVEGEALA TLVVNNMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTAGTV
     ISEEIGMELE KATLEDLGQA KRVVINKDTT IIIDGVGEES AIQGRVAQIR QQIEEATSDY
     DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALV
     RVAAKLVDLK GINEEQNVGI KVALRAMESP LRQIVANAGE EPSVVTNNVK AGEGNYGYNA
     ATEQYGDMIE MGILDPTKVT RSALQYASSV AGLMITTECM VTDLPKEEKA DLGAAGMGGM
     GGMGGMM
//

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