CH60_ZYMMO
ID CH60_ZYMMO Reviewed; 546 AA.
AC P48220; Q5NL57;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
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=ZMO1929;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=7926837; DOI=10.1016/0378-1119(94)90232-1;
RA Barbosa M.F., Yomano L.P., Ingram L.O.;
RT "Cloning, sequencing and expression of stress genes from the ethanol-
RT producing bacterium Zymomonas mobilis: the groESL operon.";
RL Gene 148:51-57(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(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; L11654; AAA62399.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV90553.1; -; Genomic_DNA.
DR PIR; JC2564; JC2564.
DR RefSeq; WP_011241653.1; NZ_CP035711.1.
DR AlphaFoldDB; P48220; -.
DR SMR; P48220; -.
DR STRING; 264203.ZMO1929; -.
DR PRIDE; P48220; -.
DR EnsemblBacteria; AAV90553; AAV90553; ZMO1929.
DR GeneID; 58027632; -.
DR KEGG; zmo:ZMO1929; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OMA; SSAMFDK; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000001173; 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 Reference proteome.
FT CHAIN 1..546
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063617"
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 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 36..73
FT /note="RNVVLDKAFGAPRITKDGVSVAKEIELKDKFENMGAQM -> VTLFWTKPLV
FT LPYHQRWCFCRQRNRTERQVRKYGHRC (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="A -> P (in Ref. 1; AAA62399)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="T -> A (in Ref. 1; AAA62399)"
FT /evidence="ECO:0000305"
FT CONFLICT 545..546
FT /note="DF -> GGMDF (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 58122 MW; D7492F8AA2DED631 CRC64;
MAAKDVKFSR DARERILRGV DILADAVKVT LGPKGRNVVL DKAFGAPRIT KDGVSVAKEI
ELKDKFENMG AQMLREVASK TNDLAGDGTT TATVLAQAIV REGMKSVAAG MNPMDLKRGI
DLAATKVVES LRSRSKPVSD FNEVAQVGII SANGDEEVGR RIAEAMEKVG KEGVITVEEA
KGFDFELDVV EGMQFDRGYL SPYFITNPEK MVAELADPYI LIYEKKLSNL QSILPILESV
VQSGRPLLII AEDIEGEALA TLVVNKLRGG LKVAAVKAPG FGDRRKAMLE DIAILTKGEL
ISEDLGIKLE NVTLNMLGSA KRVSITKENT TIVDGAGDQS TIKDRVEAIR SQIEATTSDY
DREKLQERVA KLAGGVAVIK VGGATEVEVK ERKDRVDDAL HATRAAVQEG IVPGGGTALL
YATKTLEGLN GVNEDQQRGI DIVRRALQAP VRQIAQNAGF DGAVVAGKLI DGNDDKIGFN
AQTEKYEDLA ATGVIDPTKV VRTALQDAAS VAGLLITTEA AVGDLPEDKP APAMPGGMGG
MGGMDF
