CH60_BARHE
ID CH60_BARHE Reviewed; 547 AA.
AC O33963; O87267;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
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}, mopA;
GN OrderedLocusNames=BH13530;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=9274034; DOI=10.1099/00221287-143-8-2807;
RA Haake D.A., Summers T.A., McCoy A.M., Schwartzman W.;
RT "Heat shock response and groEL sequence of Bartonella henselae and
RT Bartonella quintana.";
RL Microbiology 143:2807-2815(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RA Callison J.A., Smitherman L.S., Read A.J., Birtles R.J., Minnick M.F.;
RT "Characterization of the Bartonella bacilliformis groES-EL operon.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-543.
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RA Marston E.L., Sumner J.W., Regnery R.L.;
RT "Evaluation of intraspecies genetic variation within the 60 kDa heat shock
RT protein (groEL) gene of Bartonella species: a new phylogenetic analysis
RT tool.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-408.
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=9230387; DOI=10.1128/jcm.35.8.2087-2092.1997;
RA Sumner J.W., Nicholson W.L., Massung R.F.;
RT "PCR amplification and comparison of nucleotide sequences from the groESL
RT heat shock operon of Ehrlichia species.";
RL J. Clin. Microbiol. 35:2087-2092(1997).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD04238.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U78514; AAB69094.1; -; Genomic_DNA.
DR EMBL; AJ749669; CAG44447.1; -; Genomic_DNA.
DR EMBL; BX897699; CAF28126.1; -; Genomic_DNA.
DR EMBL; AF014829; AAD04238.1; ALT_INIT; Genomic_DNA.
DR EMBL; U96734; AAB65637.1; -; Genomic_DNA.
DR RefSeq; WP_011181151.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; O33963; -.
DR SMR; O33963; -.
DR STRING; 283166.BH13530; -.
DR PaxDb; O33963; -.
DR PRIDE; O33963; -.
DR EnsemblBacteria; CAF28126; CAF28126; BH13530.
DR GeneID; 64157520; -.
DR KEGG; bhe:BH13530; -.
DR eggNOG; COG0459; Bacteria.
DR OMA; TDTDKME; -.
DR Proteomes; UP000000421; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Stress response.
FT CHAIN 1..547
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063283"
FT REGION 526..547
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 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 547 AA; 57625 MW; EDE25D566D5B10D2 CRC64;
MAAKEVKFGR EARERLLRGV DILANAVKVT LGPKGRNVVI DKSFGAPRIT KDGVSVAKEI
ELEDKFENMG AQMLREVASK TNDIAGDGTT TATVLGQAIV QEGVKAVAAG MNPMDLKRGI
DAAVDEVVAN LFKKAKKIQT SAEIAQVGTI SANGAAEIGK MIADAMEKVG NEGVITVEEA
KTAETELEVV EGMQFDRGYL SPYFVTNAEK MVADLDDPYI LIHEKKLSNL QSLLPVLEAV
VQSGKPLLII AEDVEGEALA TLVVNKLRGG LKIAAVKAPG FGDRRKAMLE DIAILTSGQV
ISEDVGIKLE NVTLDMLGRA KKVNISKENT TIIDGAGQKS EINARVNQIK VQIEETTSDY
DREKLQERLA KLAGGVAVIR VGGATEVEVK EKKDRVDDAL NATRAAVEEG IVAGGGTALL
RAANALTVKG SNPDQEAGIN IVRRALQAPA RQIATNAGEE AAIIVGKVLE NNADTFGYNT
ATGEFGDLIA LGIVDPVKVV RSALQNAASI ASLLITTEAM VAEVPKKDTP VPPMPGGGMG
GMGGMDF
