CH60_XANOR
ID CH60_XANOR Reviewed; 546 AA.
AC Q5GUT1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}; OrderedLocusNames=XOO4288;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
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; AE013598; AAW77542.1; -; Genomic_DNA.
DR RefSeq; WP_011260602.1; NC_006834.1.
DR PDB; 6KFV; X-ray; 3.22 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-526.
DR PDBsum; 6KFV; -.
DR AlphaFoldDB; Q5GUT1; -.
DR SMR; Q5GUT1; -.
DR STRING; 291331.XOO4288; -.
DR EnsemblBacteria; AAW77542; AAW77542; XOO4288.
DR KEGG; xoo:XOO4288; -.
DR HOGENOM; CLU_016503_3_0_6; -.
DR OMA; PYILINQ; -.
DR Proteomes; UP000006735; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Isomerase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..546
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063609"
FT REGION 526..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 479..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 89..109
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 113..132
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 186..196
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:6KFV"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:6KFV"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 256..267
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 282..296
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 339..353
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 386..409
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:6KFV"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 417..424
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 434..447
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 449..458
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:6KFV"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:6KFV"
FT TURN 488..492
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:6KFV"
FT HELIX 497..514
FT /evidence="ECO:0007829|PDB:6KFV"
FT STRAND 517..523
FT /evidence="ECO:0007829|PDB:6KFV"
SQ SEQUENCE 546 AA; 57156 MW; FDD178E436CBB5E1 CRC64;
MAAKDIRFGE DARTRMVRGV NVLANAVKAT LGPKGRNVVL EKSFGAPTIT KDGVSVAKEI
ELADKFENMG AQMVKEVASK TNDNAGDGTT TATVLAQALI REGAKAVAAG MNPMDLKRGI
DQAVKAAVVE LKNISKPTTD DKAIAQVGTI SANSDESIGN IIAEAMKKVG KEGVITVEEG
SGLENELDVV EGMQFDRGYL SPYFINNQQS QSADLDDPFI LLHDKKISNV RDLLPVLEGV
AKAGKPLLIV AEEVEGEALA TLVVNTIRGI VKVVAVKAPG FGDRRKAMLE DMAVLTGGTV
ISEEVGLALE KATIKDLGRA KKVQVSKENT TIIDGAGDSA AIESRVGQIK TQIEDTSSDY
DREKLQERVA KLAGGVAVIK VGASTEIEMK EKKARVEDAL HATRAAVEEG VVPGGGVALV
RALVAVGNLT GANEDQTHGI QIALRAMEAP LREIVANAGE EPSVILNKVK EGTGNYGYNA
ANGEFGDMVE FGILDPTKVT RSALQNAASI AGLMITTEAM VADAPKKDEP AMPAGGGMGG
MGGMDF
