CH60_LEGPH
ID CH60_LEGPH Reviewed; 548 AA.
AC Q5ZXP3; P26878;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 106.
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}, htpB, mopA;
GN OrderedLocusNames=lpg0688;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2117582; DOI=10.1128/iai.58.9.3154-3157.1990;
RA Sampson J.S., O'Connor S.P., Holloway B.P., Plikaytis B.B., Carlone G.M.,
RA Mayer L.W.;
RT "Nucleotide sequence of htpB, the Legionella pneumophila gene encoding the
RT 58-kilodalton (kDa) common antigen, formerly designated the 60-kDa common
RT antigen.";
RL Infect. Immun. 58:3154-3157(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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 -!- FUNCTION: May play a protective role against the defense mechanisms
CC generated by the infected macrophages.
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=AAU26777.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M91673; AAA25298.1; -; Genomic_DNA.
DR EMBL; AE017354; AAU26777.1; ALT_INIT; Genomic_DNA.
DR PIR; A41468; A41468.
DR RefSeq; WP_011214899.1; NC_002942.5.
DR RefSeq; YP_094724.1; NC_002942.5.
DR AlphaFoldDB; Q5ZXP3; -.
DR SMR; Q5ZXP3; -.
DR STRING; 272624.lpg0688; -.
DR PaxDb; Q5ZXP3; -.
DR PRIDE; Q5ZXP3; -.
DR EnsemblBacteria; AAU26777; AAU26777; lpg0688.
DR KEGG; lpn:lpg0688; -.
DR PATRIC; fig|272624.6.peg.709; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_6; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044175; C:host cell endosome membrane; IDA:CAFA.
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:0046812; F:host cell surface binding; IDA:CAFA.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044650; P:adhesion of symbiont to host cell; IDA:CAFA.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; IDA:CAFA.
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; Stress response.
FT CHAIN 1..548
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063408"
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 478..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 194..199
FT /note="FDRGYI -> LIAVH (in Ref. 1; AAA25298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 58165 MW; 5A5C2D322F6251C2 CRC64;
MAKELRFGDD ARLQMLAGVN ALADAVQVTM GPRGRNVVLE KSYGAPTVTK DGVSVAKEIE
FEHRFMNMGA QMVKEVASKT SDTAGDGTTT ATVLARSILV EGHKAVAAGM NPMDLKRGID
KAVLAVTKKL QAMSKPCKDS KAIAQVGTIS ANSDEAIGAI IAEAMEKVGK EGVITVEDGN
GLENELSVVE GMQFDRGYIS PYFINNQQNM SCELEHPFIL LVDKKVSSIR EMLSVLEGVA
KSGRPLLIIA EDVEGEALAT LVVNNMRGIV KVCAVKAPGF GDRRKAMLQD IAILTKGQVI
SEEIGKSLEG ATLEDLGSAK RIVVTKENTT IIDGEGKATE INARITQIRA QMEETTSDYD
REKLQERVAK LAGGVAVIKV GAATEVEMKE KKARVEDALH ATRAAVEEGI VAGGGVALIR
AQKALDSLKG DNDDQNMGIN ILRRAIESPM RQIVTNAGYE ASVVVNKVAE HKDNYGFNAA
TGEYGDMVEM GILDPTKVTR MALQNAASVA SLMLTTECMV ADLPKKEEGV GAGDMGGMGG
MGGMGGMM
