CH60_BARBA
ID CH60_BARBA Reviewed; 544 AA.
AC P35635;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
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=7B2, Bb63, Bb65, groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
OS Bartonella bacilliformis.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=774;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B13;
RA Schreiber M.G.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Xu Y., Lu Z., Ihler G.;
RT "Molecular cloning, expression and sequencing of extracellular Bb63, a
RT immuno-reactive protein released by Bartonella bacilliformis.";
RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-37.
RX PubMed=1700634; DOI=10.4269/ajtmh.1990.43.373;
RA Knobloch J., Schreiber M.G.;
RT "Bb65, a major immunoreactive protein of Bartonella bacilliformis.";
RL Am. J. Trop. Med. Hyg. 43:373-379(1990).
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 -!- MISCELLANEOUS: This protein is a major antigen in patients with
CC bartonellosis, an infectious disease endemic in high altitude valleys
CC of the Andes.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; Z15160; CAA78859.1; -; Genomic_DNA.
DR EMBL; M98257; AAA22898.1; -; Genomic_DNA.
DR PIR; A60146; A60146.
DR PIR; S37039; S37039.
DR RefSeq; WP_005767840.1; NZ_LQXX01000007.1.
DR AlphaFoldDB; P35635; -.
DR SMR; P35635; -.
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 ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW Nucleotide-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1700634"
FT CHAIN 2..544
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063282"
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 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 10
FT /note="R -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="L -> M (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 34..36
FT /note="KGR -> VGV (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="A -> V (in Ref. 2; AAA22898)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="P -> A (in Ref. 2; AAA22898)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="R -> G (in Ref. 2; AAA22898)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 57617 MW; D67632ABC3A64D1E CRC64;
MAAKEVKFGR DARERLLRGV DILADAVKVT LGPKGRNVVI DKSFGAPRIT KDGVSVAKEI
ELENKFENMG AQMLREVASK TNDIAGDGTT TATVLGQAIV QEGVKAVAAS MNPMDLKRGI
DAAVEAVVAD LFKKAKKIQT SEEIAQVATI SANGAEDIGK MIADAMEKVG NEGVITVEEA
KTAETELEVV EGMQFDRGYL SPYFVTNSEK MMVDLDDPYI LIHEKKLSNL QSLLPVLEAV
AQSGKPLLII AEDVEGEALA TLVVNKLRGG LKIAAVKAPG FGDRRKAMLE DIAVLTSGQV
ISEDVGIKLE NVTLEMLGRA KKVHVSKETT TIVDGAGQKS EINARVSQIK AQIEETTSDY
DREKLQERLA KLAGGVAVIR VGGSTEVEVK EKKDRVDDAL NATRAAVEEG IVPGGGTPLL
RAAKALSIKG KNPDQEAGIG IIRRALQAPA RQIAHNAGEE AAVIVGKVLE NCSDTFGYNT
ATAQFRDLIS FGIVDPVKVV RSALQNAASI ASLLITTEAM VAEVPKKEAA APAMPGGGMG
GMDF
