(data stored in ACNUC7421 zone)

SWISSPROT: A8LCK3_FRASN

ID   A8LCK3_FRASN            Unreviewed;       540 AA.
AC   A8LCK3;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=60 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00600, ECO:0000256|RuleBase:RU000419};
DE   AltName: Full=GroEL protein {ECO:0000256|HAMAP-Rule:MF_00600};
DE   AltName: Full=Protein Cpn60 {ECO:0000256|HAMAP-Rule:MF_00600};
GN   Name=groL {ECO:0000256|HAMAP-Rule:MF_00600};
GN   Synonyms=groEL {ECO:0000256|HAMAP-Rule:MF_00600};
GN   OrderedLocusNames=Franean1_0175 {ECO:0000313|EMBL:ABW09642.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09642.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- FUNCTION: Prevents misfolding and promotes the refolding and
CC       proper assembly of unfolded polypeptides generated under stress
CC       conditions. {ECO:0000256|HAMAP-Rule:MF_00600,
CC       ECO:0000256|RuleBase:RU000419}.
CC   -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of
CC       7 subunits. {ECO:0000256|HAMAP-Rule:MF_00600,
CC       ECO:0000256|RuleBase:RU000419}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000256|HAMAP-Rule:MF_00600, ECO:0000256|RuleBase:RU000418}.
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DR   EMBL; CP000820; ABW09642.1; -; Genomic_DNA.
DR   RefSeq; WP_012157619.1; NC_009921.1.
DR   STRING; 298653.Franean1_0175; -.
DR   EnsemblBacteria; ABW09642; ABW09642; Franean1_0175.
DR   KEGG; fre:Franean1_0175; -.
DR   eggNOG; ENOG4105CJ9; Bacteria.
DR   eggNOG; COG0459; LUCA.
DR   HOGENOM; HOG000076290; -.
DR   KO; K04077; -.
DR   OMA; TDTDKME; -.
DR   OrthoDB; 265347at2; -.
DR   BioCyc; FSP298653:G1G9X-173-MONOMER; -.
DR   Proteomes; UP000001313; Chromosome.
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; A8LCK3.
DR   SWISS-2DPAGE; A8LCK3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00600};
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00600};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00600};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313}.
FT   COILED      344    364       {ECO:0000256|SAM:Coils}.
FT   COILED      387    407       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   540 AA;  56839 MW;  E9014AD1C68E720B CRC64;
     MPKIIAFDEE ARRGLERGMN QLADAVKVTL GPKGRNVVLE KKWGVPTITN DGVSIAKEIE
     LEDPYEKIGA ELVKEVAKKT NDVAGDGTTT ATILAQALVR EGLRNVAAGA NPMGLKKGIE
     AAVERVSEEL SSVAKDVETK EQIASTASIS AGDPAIGSMI AEAMDKVGKE GVITVEESNT
     FGLELELTEG MRFDKGYISP YFVTDTDRME AVLDDPYILI ANSKISAVKD LLPILEKVMQ
     AGKPLAIISE DVEGEALATL VVNKIRGTFK STAVKAPGFG DRRKAMLTDI AVLTGGQVIS
     EDVGLKLEGT TVDLLGRARK VVITKDETTI VEGAGDADQI AGRVNQIRNE IEKSDSDYDR
     EKLQERLAKL AGGVAVIKVG AATEVELKEK KHRIEDAVSN AKAAVEEGIV AGGGVALLQA
     ATSAFEKLDL SGDEATGANI VRLALEAPIK QIAFNSGLEG GVVVEKVRNL PTGHGLNAAT
     GEYVDMVATG IIDPAKVTRS ALQNAASIAG LFLTTEAVIA DKPEKDKAPA MPGGGGEMDF
//

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