CH602_MYCVP
ID CH602_MYCVP Reviewed; 541 AA.
AC A1T352;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Mvan_0764;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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: Secreted, capsule {ECO:0000250|UniProtKB:P9WPE7}.
CC Cell surface {ECO:0000250|UniProtKB:P9WPE7}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:P9WPE7}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; CP000511; ABM11602.1; -; Genomic_DNA.
DR RefSeq; WP_011778038.1; NC_008726.1.
DR AlphaFoldDB; A1T352; -.
DR SMR; A1T352; -.
DR STRING; 350058.Mvan_0764; -.
DR PRIDE; A1T352; -.
DR EnsemblBacteria; ABM11602; ABM11602; Mvan_0764.
DR KEGG; mva:Mvan_0764; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_11; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000009159; Chromosome.
DR GO; GO:0042603; C:capsule; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; Cell wall; Chaperone; Isomerase; Nucleotide-binding;
KW Reference proteome; Secreted.
FT CHAIN 1..541
FT /note="Chaperonin GroEL 2"
FT /id="PRO_0000332030"
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 476..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 541 AA; 56513 MW; E5FFE95FF94BD3C3 CRC64;
MSKIIAYDEE ARRGLERGLN ALADAVKVTL GPKGRNVVLE KKWGAPTITN DGVSIAKEIE
LEDPYEKIGA ELVKEVAKKT DDVAGDGTTT ATVLAQALVR EGLRNVAAGA NPLGLKRGIE
KAVEKVTETL LKSAKEVETK EQIAATAAIS AGDTQIGELI AEAMDKVGNE GVITVEESNT
FGLQLELTEG MRFDKGYISG YFVTDAERQE AVLEDPYILL VSSKVSTVKD LLPLLEKVIQ
AGKPLLIIAE DVEGEALSTL VVNKIRGTFK SVAVKAPGFG DRRKAMLQDI AILTGGQVVS
EEVGLSLETA DVALLGTARK VVVTKDETTI VEGAGDSDAI AGRVAQIRAE IENSDSDYDR
EKLQERLAKL AGGVAVIKAG AATEVELKER KHRIEDAVRN AKAAVEEGIV AGGGVALLQS
APSLDELNLT GDEATGANIV RVALSAPLKQ IAFNGGLEPG VVAEKVTNLP AGHGLNAATG
EYEDLLKAGV ADPVKVTRSA LQNAASIAAL FLTTEAVVAD KPEKAAAPAG DPTGGMGGMD
F
