(data stored in ACNUC7421 zone)

SWISSPROT: D6ZBR8_SEGRD

ID   D6ZBR8_SEGRD            Unreviewed;       541 AA.
AC   D6ZBR8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 47.
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=Srot_0408 {ECO:0000313|EMBL:ADG96895.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96895.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96895.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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; CP001958; ADG96895.1; -; Genomic_DNA.
DR   RefSeq; WP_013137351.1; NC_014168.1.
DR   STRING; 640132.Srot_0408; -.
DR   EnsemblBacteria; ADG96895; ADG96895; Srot_0408.
DR   KEGG; srt:Srot_0408; -.
DR   eggNOG; ENOG4105CJ9; Bacteria.
DR   eggNOG; COG0459; LUCA.
DR   HOGENOM; HOG000076290; -.
DR   KO; K04077; -.
DR   OMA; TDTDKME; -.
DR   OrthoDB; 265347at2; -.
DR   BioCyc; SROT640132:G1GLH-410-MONOMER; -.
DR   Proteomes; UP000002247; 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; D6ZBR8.
DR   SWISS-2DPAGE; D6ZBR8.
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:UP000002247};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00600};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   COILED      384    407       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   541 AA;  56206 MW;  B04B8A7ADD2949A1 CRC64;
     MAKIIAFDEE ARRGLERGLN ALADAVKVTL GPKGRNVVLE KKWGAPTITN DGVSIAKEIE
     LEDPYEKIGA ELVKEVAKKT DDVAGDGTTT ATVLAQALVK EGLRNVAAGA NPLGLKRGIE
     KAVEAVTEKL LSSAVKVDTK EQIAATAGIS AGDPAIGELI AEAHDKVGNN GVITVEESNT
     FGLQLELTEG LRFDKGYISG YFVTDPERQE AVLEDPYILL VSSKISTVKD LLPLLEKVIQ
     AGKPLVIIAE DVEGEALSTL VVNKIRGTFK SVAIKAPGFG DRRKAQLADI AILTGGEVIS
     EEVGLSLESA GLELLGRARQ VIVTKDETTI VEGAGDSSAI AGRVAQIKTE IENTDSDYDR
     EKLQERLAKL AGGVAIIKAG AATEVELKER KHRIEDAVRN AKAAVEEGIV AGGGSALLQA
     APALDSLGLS GDEATGANIV RVALEAPLKQ IAFNAGLEPG VVVDKVRNLP AGSGLNAATG
     EYEDLLAAGI NDPVKVTRSA LQNAASIAGL FLTTEAVVAD KPEKAAAPAG DPTGGMGDMG
     F
//

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