CH605_PARXL
ID CH605_PARXL Reviewed; 546 AA.
AC Q13IM9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Chaperonin GroEL 5 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 5 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 5 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 5 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL5 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL5 {ECO:0000255|HAMAP-Rule:MF_00600};
GN OrderedLocusNames=Bxeno_C0132; ORFNames=Bxe_C0135;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000272; ABE36060.1; -; Genomic_DNA.
DR RefSeq; WP_011493320.1; NZ_CP008761.1.
DR AlphaFoldDB; Q13IM9; -.
DR SMR; Q13IM9; -.
DR STRING; 266265.Bxe_C0135; -.
DR PRIDE; Q13IM9; -.
DR EnsemblBacteria; ABE36060; ABE36060; Bxe_C0135.
DR KEGG; bxb:DR64_8292; -.
DR KEGG; bxe:Bxe_C0135; -.
DR PATRIC; fig|266265.5.peg.7917; -.
DR eggNOG; COG0459; Bacteria.
DR OMA; TGAQLMR; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000001817; Chromosome 3.
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 5"
FT /id="PRO_0000256890"
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 546 AA; 57367 MW; 837E2D1843B6F365 CRC64;
MAAKEIIFSD VARSKLVEGV NILANAVKVT LGPKGRNVVL ERSFGSPVVT KDGVSVAKEI
ELPDRVQNIG AQLVKEVASR TSDAAGDGTT TATVLAQAIV REGQKYVAAG LNPLDLKRGI
DKAVVAAIDE LKKISKPTTT SKEIAQVATI SANGEESIGQ RIAEAIDRVG KEGVITVEDG
KSLDDELDVV EGLQFDRGYL SPYFINDQDK QVAVLDNPYV LLHDKKVSNI RDLLPVLEQV
AKASRPLLII AEDVEGEALA TLVVNNIRGI LKTVAVKAPG FGDRRKALLE DIAILTGGQV
IAEETGLTLE KATLAELGQA KRIEVGKENT TVIDGAGEHK NIEARVKQIR AQIDEASSDY
DREKLQERVA KLAGGVAVIK VGGATEIEVK EKKDRVDDAL HATRAAVEEG IVPGGGVALI
RVRNAISGLK GANADQDAGI KIVLRALEEP LRQIVTNAGE EASVVVAKVA EGSGNFGYNA
QTGEYGDLVE SGVLDPTKVT RTALQNAASV AALLLTTDAT VYEAPKDPAP ATSAAGPGAP
GAGYDF
