CH601_MYCBP
ID CH601_MYCBP Reviewed; 539 AA.
AC A1KPA8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Chaperonin GroEL 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000305};
DE AltName: Full=Chaperonin-60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=cpn60.1 {ECO:0000303|PubMed:31244785},
GN groL1 {ECO:0000255|HAMAP-Rule:MF_00600}; OrderedLocusNames=BCG_3487c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN [2]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH HUMAN
RP CD209.
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=21203928; DOI=10.1007/s13238-010-0101-3;
RA Carroll M.V., Sim R.B., Bigi F., Jaekel A., Antrobus R., Mitchell D.A.;
RT "Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG.";
RL Protein Cell 1:859-870(2010).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=BCG;
RX PubMed=31244785; DOI=10.3389/fmicb.2019.01149;
RA Zeng S., Constant P., Yang D., Baulard A., Lefevre P., Daffe M.,
RA Wattiez R., Fontaine V.;
RT "Cpn60.1 (GroEL1) contributes to mycobacterial crabtree effect:
RT implications for biofilm formation.";
RL Front. Microbiol. 10:1149-1149(2019).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 531-HIS--HIS-539.
RC STRAIN=BCG;
RX PubMed=32812602; DOI=10.1039/d0mt00101e;
RA Yang D., Klebl D.P., Zeng S., Sobott F., Prevost M., Soumillion P.,
RA Vandenbussche G., Fontaine V.;
RT "Interplays between copper and Mycobacterium tuberculosis GroEL1.";
RL Metallomics 12:1267-1277(2020).
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: Involved in copper homeostasis (PubMed:32812602). Binds
CC copper and may help maintaining copper homeostasis when copper is
CC present in excess, notably in the macrophage phagosome, by acting as a
CC metal storage protein (PubMed:32812602). Increases copper tolerance
CC during biofilm formation (PubMed:32812602). In vitro binds to human
CC CD209 (DC-SIGN) and may help mediate adherence to host cells
CC (PubMed:21203928). {ECO:0000269|PubMed:21203928,
CC ECO:0000269|PubMed:32812602}.
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 (By
CC similarity). Able to bind to host (human) CD209 in vitro
CC (PubMed:21203928). {ECO:0000255|HAMAP-Rule:MF_00600,
CC ECO:0000269|PubMed:21203928}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC Note=Although thought of as a cytoplasmic chaperone this protein has
CC been found to interact in vitro with a host extracellular protein.
CC {ECO:0000269|PubMed:21203928}.
CC -!- DISRUPTION PHENOTYPE: In the standard Sauton's medium containing 6%
CC glycerol, disruption mutant displays poor growth and very poor biofilm
CC phenotype with no full attachment on the medium-air interface at day 35
CC (PubMed:31244785). Mutant shows abnormal Crabtree effect. Mutant has a
CC compromised ability to down-regulate ATP and secretes more pyruvate,
CC acetate, succinate, and glutamate in the culture medium. Mutant has
CC higher intracellular pyruvate and produces more toxic methylglyoxal,
CC suggesting a glycolytic stress leading to growth stasis and
CC consequently biofilm failure (PubMed:31244785). Deletion of the gene
CC enhances copper susceptibility during biofilm growth (PubMed:32812602).
CC {ECO:0000269|PubMed:31244785, ECO:0000269|PubMed:32812602}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; AM408590; CAL73476.1; -; Genomic_DNA.
DR RefSeq; WP_003418021.1; NC_008769.1.
DR AlphaFoldDB; A1KPA8; -.
DR SMR; A1KPA8; -.
DR GeneID; 45427413; -.
DR KEGG; mbb:BCG_3487c; -.
DR HOGENOM; CLU_016503_3_0_11; -.
DR OMA; YWIASNA; -.
DR Proteomes; UP000001472; 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:0046872; F:metal ion binding; 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; Copper; Cytoplasm; Isomerase; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..539
FT /note="Chaperonin GroEL 1"
FT /id="PRO_0000332015"
FT BINDING 29..32
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 413
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 MUTAGEN 531..539
FT /note="Missing: Cannot bind copper."
FT /evidence="ECO:0000269|PubMed:32812602"
SQ SEQUENCE 539 AA; 55877 MW; 3E0B93164C091B63 CRC64;
MSKLIEYDET ARRAMEVGMD KLADTVRVTL GPRGRHVVLA KAFGGPTVTN DGVTVAREIE
LEDPFEDLGA QLVKSVATKT NDVAGDGTTT ATILAQALIK GGLRLVAAGV NPIALGVGIG
KAADAVSEAL LASATPVSGK TGIAQVATVS SRDEQIGDLV GEAMSKVGHD GVVSVEESST
LGTELEFTEG IGFDKGFLSA YFVTDFDNQQ AVLEDALILL HQDKISSLPD LLPLLEKVAG
TGKPLLIVAE DVEGEALATL VVNAIRKTLK AVAVKGPYFG DRRKAFLEDL AVVTGGQVVN
PDAGMVLREV GLEVLGSARR VVVSKDDTVI VDGGGTAEAV ANRAKHLRAE IDKSDSDWDR
EKLGERLAKL AGGVAVIKVG AATETALKER KESVEDAVAA AKAAVEEGIV PGGGASLIHQ
ARKALTELRA SLTGDEVLGV DVFSEALAAP LFWIAANAGL DGSVVVNKVS ELPAGHGLNV
NTLSYGDLAA DGVIDPVKVT RSAVLNASSV ARMVLTTETV VVDKPAKAED HDHHHGHAH
