(data stored in ACNUC30630 zone)

SWISSPROT: CH60_DEIRA

ID   CH60_DEIRA              Reviewed;         548 AA.
AC   Q9RWQ9;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 118.
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=DR_0607;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-19.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=15249204; DOI=10.1016/j.bbrc.2004.06.062;
RA   Joshi B.S., Schmid R., Altendorf K., Apte S.K.;
RT   "Protein recycling is a major component of post-irradiation recovery in
RT   Deinococcus radiodurans strain R1.";
RL   Biochem. Biophys. Res. Commun. 320:1112-1117(2004).
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; AE000513; AAF10186.1; -; Genomic_DNA.
DR   PIR; G75499; G75499.
DR   RefSeq; NP_294330.1; NC_001263.1.
DR   RefSeq; WP_010887252.1; NZ_CP015081.1.
DR   SMR; Q9RWQ9; -.
DR   STRING; 243230.DR_0607; -.
DR   PRIDE; Q9RWQ9; -.
DR   EnsemblBacteria; AAF10186; AAF10186; DR_0607.
DR   GeneID; 1798289; -.
DR   KEGG; dra:DR_0607; -.
DR   PATRIC; fig|243230.17.peg.785; -.
DR   eggNOG; ENOG4105CJ9; Bacteria.
DR   eggNOG; COG0459; LUCA.
DR   HOGENOM; HOG000076290; -.
DR   InParanoid; Q9RWQ9; -.
DR   KO; K04077; -.
DR   OMA; TDTDKME; -.
DR   OrthoDB; 265347at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006458; P:'de novo' protein folding; IBA:GO_Central.
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; 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.
PE   1: Evidence at protein level;
DR   PRODOM; Q9RWQ9.
DR   SWISS-2DPAGE; Q9RWQ9.
KW   ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Nucleotide-binding; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:15249204"
FT   CHAIN           2..548
FT                   /note="60 kDa chaperonin"
FT                   /id="PRO_0000063355"
SQ   SEQUENCE   548 AA;  57778 MW;  EC8829C370F6675D CRC64;
     MAKQLVFDES ARRSLERGVN AVANAVKVTL GPRGRNVVIE KKFGSPTITK DGVTVAKEVE
     LEDKLENIGA QLLKEVASKT NDITGDGTTT ATVLGQAIVK EGLRNVAAGA NPLALKRGID
     KAVAVAIEEI KKLAVSVEDS EAIKKVAGIS ANDETVGQEI ASAMDKVGKE GVITIEESKG
     FDTEVDVVEG MQFDKGFINP YFITNPEKME AVLEDAYILI NEKKISNLKD MLPVLEKVAQ
     TGRPLLIIAE DVEGEALATL VVNKLRGTLN IAAVKAPGFG DRRKEMLRDI AAVTGGEVVS
     EDLGHKLENV GMEMLGRAAR IRITKDETTI VDGKGEQAQI DARVNAIKGE LDSTDSDYAR
     EKLQERLAKL SGGVAVIRVG AATETELKEK KHRYEDALST ARSAVEEGIV AGGGTTLLRV
     IPAVRKAAES LTGDEATGAR ILIRALEEPA RQIAANAGEE GSVIVNAVVG SDKARYGFNA
     ATGEYVEDMV AAGIVDPAKV TRTALQNAAS IGALILTTEA IVSDKPEKAA PAMPQGGGDM
     GGMGGMDF
//

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