(data stored in ACNUC7421 zone)

SWISSPROT: CH60_LEGPC

ID   CH60_LEGPC              Reviewed;         548 AA.
AC   A5IGM1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 74.
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=LPC_2606;
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: Prevents misfolding and promotes the refolding and proper
CC       assembly of unfolded polypeptides generated under stress conditions.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of 7
CC       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; CP000675; ABQ56521.1; -; Genomic_DNA.
DR   SMR; A5IGM1; -.
DR   EnsemblBacteria; ABQ56521; ABQ56521; LPC_2606.
DR   KEGG; lpc:LPC_2606; -.
DR   HOGENOM; HOG000076290; -.
DR   KO; K04077; -.
DR   OMA; TDTDKME; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   CDD; cd03344; GroEL; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
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_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5IGM1.
DR   SWISS-2DPAGE; A5IGM1.
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..548
FT                   /note="60 kDa chaperonin"
FT                   /id="PRO_1000025802"
SQ   SEQUENCE   548 AA;  58121 MW;  F5D24B2AB01817D7 CRC64;
     MAKELRFGDD ARLQMLAGVN ALADAVQVTM GPRGRNVVLE KSYGAPTVTK DGVSVAKEIE
     FEHRFMNMGA QMVKEVASKT SDTAGDGTTT ATVLARSILV EGHKAVAAGM NPMDLKRGID
     KAVLAVTKKL QAMSKPCKDS KAIAQVGTIS ANSDEAIGAI IAEAMEKVGK EGVITVEDGN
     GLENELSVVE GMQFDRGYIS PYFINNQQNM SCELEHPFIL LVDKKVSSIR EMLSVLEGVA
     KSGRPLLIIA EDVEGEALAT LVVNNMRGIV KVCAVKAPGF GDRRKAMLQD IAILTKGQVI
     SEEIGKSLEG ATLEDLGSAK RIVVTKENTT VIDGEGKATE INARIAQIRA QMEETTSDYD
     REKLQERVAK LAGGVAVIKV GAATEVEMKE KKARVEDALH ATRAAVEEGI VAGGGVALIR
     AQKALDSLKG DNDDQNMGIN ILRRAIESPM RQIVTNAGYE ASVVVNKVAE HKDNYGFNAA
     TGEYGDMVEM GILDPTKVTR MALQNAASVA SLMLTTECMV ADLPKKEEGV GAGDMGGMGG
     MGGMGGMM
//

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