CH601_VIBVU
ID CH601_VIBVU Reviewed; 546 AA.
AC Q9ALA9;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Chaperonin GroEL 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN OrderedLocusNames=VV1_1260;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wong H.-C., Lu K.-H.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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; AY017169; AAG48876.1; -; Genomic_DNA.
DR EMBL; AE016795; AAO09716.1; -; Genomic_DNA.
DR RefSeq; WP_011079245.1; NC_004459.3.
DR AlphaFoldDB; Q9ALA9; -.
DR SMR; Q9ALA9; -.
DR PRIDE; Q9ALA9; -.
DR EnsemblBacteria; AAO09716; AAO09716; VV1_1260.
DR KEGG; vvu:VV1_1260; -.
DR HOGENOM; CLU_016503_3_0_6; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000002275; Chromosome 1.
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; 2.
DR SUPFAM; SSF52029; SSF52029; 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..546
FT /note="Chaperonin GroEL 1"
FT /id="PRO_0000063599"
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 CONFLICT 134
FT /note="L -> M (in Ref. 1; AAG48876)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="I -> F (in Ref. 1; AAG48876)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="G -> D (in Ref. 1; AAG48876)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="K -> I (in Ref. 1; AAG48876)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="K -> I (in Ref. 1; AAG48876)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="E -> K (in Ref. 1; AAG48876)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="G -> A (in Ref. 1; AAG48876)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="M -> GM (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 57516 MW; 92869B7E517B3D2A CRC64;
MAAKDVKFGN DARVKMLEGV NILADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI
ELEDKFQNMG AQMVKQVASQ ANDVAGDGTT TATVLAQAIV NEGLKAVAAG MNPMDLKRGI
DKAVAAAVEE LKALSKDCST STEIEQVGTI SANSDSSVGK IIAEAMEKVG RDGVITVEEG
QALHDELDVV EGMQFDRGYL SPYFINNQES GSVELESPFI LLVDKKISNI RELLPALEAV
AKASRPLLII AEDVEGEALA TLVVNNMRGI VKVAAVKAPG FGDRRKAMLQ DIAILTGGTV
ISEEVGLELE KATLEDLGQA KRVSITKENT TIIDGVGEEA MIQGRVAQIR QQIEDATSDY
DKEKLQERVA KLAGGVAVIK VGAATEVEMK EKKDRVEDAL HATRAAVEEG IVAGGGVALI
RAASKIVDLQ GDNEEQNVGI RVALRAMEAP LRQITKNAGD EESVVANNVR AGEGSYGYNA
ATGVYGDMLE MGILDPTKVT RSALQFAASV AGLMITTEAM VTDLPQKDSG MPDMGGMGGM
GGMGMM
