CH602_SALAI
ID CH602_SALAI Reviewed; 545 AA.
AC A8M497;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Chaperonin GroEL 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL2 {ECO:0000255|HAMAP-Rule:MF_00600};
GN OrderedLocusNames=Sare_4231;
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=391037;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000850; ABW00013.1; -; Genomic_DNA.
DR RefSeq; WP_012184250.1; NC_009953.1.
DR AlphaFoldDB; A8M497; -.
DR SMR; A8M497; -.
DR STRING; 391037.Sare_4231; -.
DR EnsemblBacteria; ABW00013; ABW00013; Sare_4231.
DR GeneID; 5704402; -.
DR KEGG; saq:Sare_4231; -.
DR PATRIC; fig|391037.6.peg.4271; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_11; -.
DR OMA; PYILINQ; -.
DR OrthoDB; 265347at2; -.
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.
FT CHAIN 1..545
FT /note="Chaperonin GroEL 2"
FT /id="PRO_0000332071"
FT REGION 526..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 86..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 477..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 545 AA; 57102 MW; 8430623E686D73CE CRC64;
MAKILSFSDD ARHQLEHGVN ALADAVKVTL GPRGRNVVLD KKFGAPTITN DGVTIAKEIE
LTNPYENLGA QLVKEVATKT NDVAGDGTTT ATVLAQALVR EGLRNVAAGA NPTGLKRGID
AAATKVSEEL LGKAVDVSDK AAIAHVATVS AQDSTIGELI AEAMERVGRD GVITVEEGST
LATELDVTEG LQFDKGFISP NFVTDAEGQE SVLEDAYILI TTQKISAIEE LLPLLEKVLQ
ESKPLLIIAE DVEGQALSTL VVNALRKTMK VCAVKAPGFG DRRKAMLQDM AILTGAELVA
PELGYKLDQV GLEVLGTARR VVVDKENTTI VDGGGQASDA EDRVAQIRKE IEASDSEWDR
EKLAERLAKL SGGIAVIRAG AATEVEMKER KHRIEDAIAA TKAAVEEGTV PGGGAALAQV
LPALDGDLGL TGDEQVGVSI VRKALIEPLR WIAQNAGHDG YVVVQKVAGK DWGHGLDAAT
GEYVDLAKAG ILDPVKVTRN AVANAASIAG LLLTTESLVV EKPQEPEPAA AGHGHGHGHQ
HGPGF
