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CH603_NITWN
ID   CH603_NITWN             Reviewed;         548 AA.
AC   Q3SPG4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Chaperonin GroEL 3 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin 3 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 3 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 3 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groEL3 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL3 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   OrderedLocusNames=Nwi_2574;
OS   Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS   NCIMB 11846 / Nb-255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX   PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA   Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA   Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA   Hickey W.J.;
RT   "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT   Nitrobacter winogradskyi Nb-255.";
RL   Appl. Environ. Microbiol. 72:2050-2063(2006).
CC   -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential
CC       role in assisting protein folding. The GroEL-GroES system forms a nano-
CC       cage that allows encapsulation of the non-native substrate proteins and
CC       provides a physical environment optimized to promote and accelerate
CC       protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC         unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00600};
CC   -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric
CC       rings stacked back-to-back. Interacts with the co-chaperonin GroES.
CC       {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}.
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DR   EMBL; CP000115; ABA05827.1; -; Genomic_DNA.
DR   RefSeq; WP_011315778.1; NC_007406.1.
DR   AlphaFoldDB; Q3SPG4; -.
DR   SMR; Q3SPG4; -.
DR   STRING; 323098.Nwi_2574; -.
DR   PRIDE; Q3SPG4; -.
DR   EnsemblBacteria; ABA05827; ABA05827; Nwi_2574.
DR   KEGG; nwi:Nwi_2574; -.
DR   eggNOG; COG0459; Bacteria.
DR   HOGENOM; CLU_016503_3_0_5; -.
DR   OMA; SSAMFDK; -.
DR   OrthoDB; 265347at2; -.
DR   Proteomes; UP000002531; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; Cpn60/GroEL.
DR   InterPro; IPR002423; Cpn60/GroEL/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;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..548
FT                   /note="Chaperonin GroEL 3"
FT                   /id="PRO_0000256938"
FT   BINDING         30..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         87..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         496
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   548 AA;  57757 MW;  D22DA4B3455ABE7F CRC64;
     MAAKDVKFSG DARQRMLRGV DILADAVKVT LGPKGRNVVI ERSFGAPRIT KDGVTVAKEI
     ELEDRFENMG AQMVREVASK TNDLAGDGTT TATVLAQAIV REGAKAVAAG MNPMDLKRGI
     DIAVAAVVKD IGKRAKAVAS SAEVAQVGTI SSNGDASIGK MIAQAMQKVG NDGVITVEEN
     KSLETDVDIV EGMKFDRGYL SPYFVTNAEK MAAELDDAYI LLHEKKLTGL QALLPVLEAV
     VKSGKPLLIV AEDVEGEALA ALVVNRLRGG LKVAAVKAPG FGDRRKAMLE DIAILTSGQL
     ISDELGMKLE NVTLNMLGRA KKVLIDKENT TIVNGAGKKK DIEARVGQIR ARIEETTSDY
     DREKLQERLA KLAGGVAVIR VGGATEIEVK EKKDRVEDAL NATRAAVEEG IVPGGGTALL
     RARKAVGRIN NDNSDVQAGI NIVLKALEAP IRQIAENAGV EGSIVVGKIL ENKTETFGFD
     AQKEEYVDMV AKGIIDPAKV VRTALQDASS IAGLLVTTEA MVAELPKDEP PAMPAGGGGM
     GGMGGMGF
 
 
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