CH60_TREPA
ID CH60_TREPA Reviewed; 544 AA.
AC P23033; O83073;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 141.
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};
DE AltName: Full=Common antigen;
DE Short=CA;
DE AltName: Full=TP4 antigen;
DE Short=TP-4;
DE AltName: Full=TPN60;
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA, Tp4;
GN OrderedLocusNames=TP_0030;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nichols;
RA Hindersson P.;
RL Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
RN [3]
RP PROTEIN SEQUENCE OF 2-23.
RC STRAIN=Nichols;
RX PubMed=1971618; DOI=10.1128/jb.172.6.2862-2870.1990;
RA Houston L.S., Cook R.G., Norris S.J.;
RT "Isolation and characterization of a Treponema pallidum major 60-kilodalton
RT protein resembling the groEL protein of Escherichia coli.";
RL J. Bacteriol. 172:2862-2870(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 is one of the most abundant proteins of T.pallidum
CC and is highly antigenic.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; X54111; CAA38048.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65026.1; -; Genomic_DNA.
DR PIR; H71374; H71374.
DR RefSeq; WP_010881479.1; NC_021490.2.
DR AlphaFoldDB; P23033; -.
DR SMR; P23033; -.
DR IntAct; P23033; 5.
DR STRING; 243276.TPANIC_0030; -.
DR PRIDE; P23033; -.
DR EnsemblBacteria; AAC65026; AAC65026; TP_0030.
DR GeneID; 57878572; -.
DR KEGG; tpa:TP_0030; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_12; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000000811; 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 ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1971618"
FT CHAIN 2..544
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063587"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 86..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 414
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 3..4
FT /note="KQ -> NE (in Ref. 1; CAA38048)"
FT /evidence="ECO:0000305"
FT CONFLICT 525..526
FT /note="PE -> GQ (in Ref. 1; CAA38048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 57981 MW; CA0AC145AA96E71E CRC64;
MAKQLLFNEE ARKKLLSGVE QISSAVKVTL GPKGRNVLLE KGYGAPTVTK DGVSVAKEVE
LEDPFENMGA QLLKEVATKT NDVAGDGTTT ATVLAYSMVR EGLKAVAAGM TPLELKRGMD
KAVAIAVDDI KQNSKGIKSN EEVAHVASVS ANNDKEIGRI LASAIEKVGN DGVIDVDEAQ
TMETVTEFVE GMQFDRGYIS SYFVTDRDRM ETVYENPYIL IYDKSISTMK DLLPLLEKIA
QTGRPLLIIA EDVEGEALAT LVVNSLRGTL KTCAVKAPGF GDRRKEMLED IAILSGGQVI
SEDLGLKLES ADIALLGQAK SVKVDKENTT IIDGSGKSKD IKDRIEQIKK QIEASTSDYD
SEKLKERLAK LSGGVAVIKI GAVTEVEMKE KKHRVEDALN ATRAAIEEGI VAGGGLALIQ
AAAALEKADL SGLTPDEAVG FKIVRRALEE PIRQISENAG IDGAVVAEKA KEKRGIGFDA
SKMEWVDMIK VGIIDPAKVT RSALQNAASV SGLLLTTECA IAAIPEKSSS TPPAPDMGGM
GGMY
