ID Q877G8_METMI Unreviewed; 543 AA. AC Q877G8; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 146. DE SubName: Full=Chaperonin {ECO:0000313|EMBL:AAM21720.1}; OS Methanococcus maripaludis (Methanococcus deltae). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=39152 {ECO:0000313|EMBL:AAM21720.1}; RN [1] {ECO:0000313|EMBL:AAM21720.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LL {ECO:0000313|EMBL:AAM21720.1}; RX PubMed=12628000; DOI=10.1042/BJ20030230; RA Kusmierczyk A.R., Martin J.; RT "Nucleotide-dependent protein folding in the type II chaperonin from the RT mesophilic archaeon Methanococcus maripaludis."; RL Biochem. J. 371:669-673(2003). RN [2] {ECO:0007829|PDB:3KFB, ECO:0007829|PDB:3KFE} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH ADP AND ATP ANALOG, RP AND DISULFIDE BONDS. RX PubMed=20573955; DOI=10.1074/jbc.M110.125344; RA Pereira J.H., Ralston C.Y., Douglas N.R., Meyer D., Knee K.M., Goulet D.R., RA King J.A., Frydman J., Adams P.D.; RT "Crystal structures of a group II chaperonin reveal the open and closed RT states associated with the protein folding cycle."; RL J. Biol. Chem. 285:27958-27966(2010). RN [3] {ECO:0007829|PDB:3IYF, ECO:0007829|PDB:3LOS} RP STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=20090755; DOI=10.1038/nature08701; RA Zhang J., Baker M.L., Schroder G.F., Douglas N.R., Reissmann S., Jakana J., RA Dougherty M., Fu C.J., Levitt M., Ludtke S.J., Frydman J., Chiu W.; RT "Mechanism of folding chamber closure in a group II chaperonin."; RL Nature 463:379-383(2010). RN [4] {ECO:0007829|PDB:3IZH, ECO:0007829|PDB:3IZI} RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 7-240 AND 268-519. RX PubMed=21241893; DOI=10.1016/j.cell.2010.12.017; RA Douglas N.R., Reissmann S., Zhang J., Chen B., Jakana J., Kumar R., RA Chiu W., Frydman J.; RT "Dual action of ATP hydrolysis couples lid closure to substrate release RT into the group II chaperonin chamber."; RL Cell 144:240-252(2011). RN [5] {ECO:0007829|PDB:3J02, ECO:0007829|PDB:3J03} RP STRUCTURE BY ELECTRON MICROSCOPY (4.80 ANGSTROMS) OF 7-240 AND 269-519. RX PubMed=21565698; DOI=10.1016/j.str.2011.03.005; RA Zhang J., Ma B., DiMaio F., Douglas N.R., Joachimiak L.A., Baker D., RA Frydman J., Levitt M., Chiu W.; RT "Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound RT state leading to lid closure."; RL Structure 19:633-639(2011). RN [6] {ECO:0007829|PDB:3RUQ, ECO:0007829|PDB:3RUS} RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) IN COMPLEX WITH ADP AND ATP ANALOG. RX PubMed=22193720; DOI=10.1038/emboj.2011.468; RA Pereira J.H., Ralston C.Y., Douglas N.R., Kumar R., Lopez T., RA McAndrew R.P., Knee K.M., King J.A., Frydman J., Adams P.D.; RT "Mechanism of nucleotide sensing in group II chaperonins."; RL EMBO J. 31:731-740(2012). RN [7] {ECO:0007829|PDB:3J3X} RP STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS) OF 1-532. RX PubMed=23592445; DOI=10.1002/pro.2267; RA DiMaio F., Zhang J., Chiu W., Baker D.; RT "Cryo-EM model validation using independent map reconstructions."; RL Protein Sci. 22:865-868(2013). RN [8] {ECO:0007829|PDB:5W74, ECO:0007829|PDB:5W79} RP X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) IN COMPLEX WITH ADP AND MG(2+). RA Dalton K.M., Lopez T., Liu C., Ralston C.Y., Pereira J.H., Chartron J.W., RA McAndrew R.P., Douglas N.R., Adams P.D., Pande V.S., Frydman J.; RT "The Conformational Cycle of the Group II Chaperonin Termini."; RL Submitted (JUN-2017) to the PDB data bank. RN [9] {ECO:0007829|PDB:7R9E, ECO:0007829|PDB:7R9H} RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 16-522. RX PubMed=34362932; DOI=10.1038/s41467-021-25099-0; RA Zhao Y., Schmid M.F., Frydman J., Chiu W.; RT "CryoEM reveals the stochastic nature of individual ATP binding events in a RT group II chaperonin."; RL Nat. Commun. 12:4754-4754(2021). CC -!- INTERACTION: CC Q877G8; Q877G8: -; NbExp=5; IntAct=EBI-7612242, EBI-7612242; CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. CC {ECO:0000256|ARBA:ARBA00008020, ECO:0000256|RuleBase:RU004187}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY099402; AAM21720.1; -; Genomic_DNA. DR PDB; 3IYF; EM; 8.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-240, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=268-543. DR PDB; 3IZH; EM; 11.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=7-519. DR PDB; 3IZI; EM; 6.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=7-519. DR PDB; 3IZJ; EM; 6.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=7-519. DR PDB; 3IZK; EM; 4.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=7-240, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=268-519. DR PDB; 3IZL; EM; 6.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=7-240, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=268-519. DR PDB; 3IZM; EM; 7.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=7-519. DR PDB; 3IZN; EM; 6.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=7-240, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=268-519. DR PDB; 3J02; EM; 8.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=7-240, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=269-519. DR PDB; 3J03; EM; 4.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=7-240, A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=269-519. DR PDB; 3J3X; EM; 4.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-532. DR PDB; 3KFB; X-ray; 3.20 A; A/B/C/D/E/F/G/H=1-543. DR PDB; 3KFE; X-ray; 3.50 A; A/B/C/D/E/F/G/H=1-543. DR PDB; 3KFK; X-ray; 6.00 A; A/B/C/D=1-543. DR PDB; 3LOS; EM; 4.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-543. DR PDB; 3RUQ; X-ray; 2.80 A; A/B/C/D=1-543. DR PDB; 3RUS; X-ray; 2.34 A; A/B/C/D=1-543. DR PDB; 3RUV; X-ray; 2.24 A; A/B/C/D=1-543. DR PDB; 3RUW; X-ray; 2.70 A; A/B/C/D=1-543. DR PDB; 5W74; X-ray; 3.65 A; A/B/C/D/E/F/G/H=1-543. DR PDB; 5W79; X-ray; 3.12 A; A/B/C/D/E/F/G/H=1-543. DR PDB; 7R9E; EM; 4.00 A; J=18-522. DR PDB; 7R9H; EM; 6.30 A; J=18-522. DR PDB; 7R9I; EM; 6.40 A; J=18-522. DR PDB; 7R9J; EM; 6.30 A; J=18-522. DR PDB; 7R9K; EM; 4.10 A; J=18-522. DR PDB; 7R9M; EM; 4.00 A; J=18-522. DR PDB; 7R9O; EM; 4.00 A; J=18-522. DR PDB; 7R9U; EM; 4.40 A; J=18-522. DR PDB; 7RAK; EM; 3.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/U=16-522. DR PDBsum; 3IYF; -. DR PDBsum; 3IZH; -. DR PDBsum; 3IZI; -. DR PDBsum; 3IZJ; -. DR PDBsum; 3IZK; -. DR PDBsum; 3IZL; -. DR PDBsum; 3IZM; -. DR PDBsum; 3IZN; -. DR PDBsum; 3J02; -. DR PDBsum; 3J03; -. DR PDBsum; 3J3X; -. DR PDBsum; 3KFB; -. DR PDBsum; 3KFE; -. DR PDBsum; 3KFK; -. DR PDBsum; 3LOS; -. DR PDBsum; 3RUQ; -. DR PDBsum; 3RUS; -. DR PDBsum; 3RUV; -. DR PDBsum; 3RUW; -. DR PDBsum; 5W74; -. DR PDBsum; 5W79; -. DR AlphaFoldDB; Q877G8; -. DR EMDB; EMD-24324; -. DR EMDB; EMD-24325; -. DR EMDB; EMD-24326; -. DR EMDB; EMD-24327; -. DR EMDB; EMD-24328; -. DR EMDB; EMD-24329; -. DR EMDB; EMD-24330; -. DR EMDB; EMD-24331; -. DR EMDB; EMD-24363; -. DR EMDB; EMD-5137; -. DR EMDB; EMD-5138; -. DR EMDB; EMD-5140; -. DR EMDB; EMD-5244; -. DR EMDB; EMD-5245; -. DR EMDB; EMD-5246; -. DR EMDB; EMD-5247; -. DR EMDB; EMD-5248; -. DR EMDB; EMD-5249; -. DR EMDB; EMD-5250; -. DR EMDB; EMD-5258; -. DR EMDB; EMD-5645; -. DR SMR; Q877G8; -. DR DIP; DIP-29771N; -. DR MINT; Q877G8; -. DR GeneID; 2761905; -. DR BRENDA; 3.6.4.B10; 3262. DR BRENDA; 5.6.1.7; 3262. DR EvolutionaryTrace; Q877G8; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. DR CDD; cd03343; cpn60; 1. DR Gene3D; 3.50.7.10; GroEL; 1. DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1. DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 1. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. 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 InterPro; IPR012714; Thermosome_arc. DR NCBIfam; NF041082; thermosome_alpha; 1. DR NCBIfam; TIGR02339; thermosome_arch; 1. DR NCBIfam; NF041083; thermosome_beta; 1. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR PANTHER; PTHR11353:SF94; T-COMPLEX PROTEIN 1 SUBUNIT EPSILON; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3IYF, ECO:0007829|PDB:3IZH}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004187}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004187}; KW Metal-binding {ECO:0007829|PDB:3KFB, ECO:0007829|PDB:3KFE}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU004187}. FT BINDING 40 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3KFE, ECO:0007829|PDB:3RUQ" FT BINDING 40 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5W74" FT BINDING 59 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3RUS, ECO:0007829|PDB:3RUW" FT BINDING 60 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3RUV" FT BINDING 91 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3RUV, ECO:0007829|PDB:3RUW" FT BINDING 91 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3KFB, ECO:0007829|PDB:3KFE" FT BINDING 92 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3KFE, ECO:0007829|PDB:3RUQ" FT BINDING 92 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5W74" FT BINDING 93 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3KFE, ECO:0007829|PDB:3RUQ" FT BINDING 94 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3KFE, ECO:0007829|PDB:3RUQ" FT BINDING 95 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5W74" FT BINDING 95 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3KFE, ECO:0007829|PDB:3RUQ" FT BINDING 161 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3RUQ, ECO:0007829|PDB:3RUS" FT BINDING 386 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3KFB, ECO:0007829|PDB:3KFE" FT BINDING 386 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3RUV" FT BINDING 404 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3KFE, ECO:0007829|PDB:3RUQ" FT BINDING 404 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5W74" FT BINDING 405 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5W74" FT BINDING 474 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5W74" FT BINDING 490 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5W74" FT BINDING 490 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3KFE, ECO:0007829|PDB:3RUQ" FT BINDING 495 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5W74" FT BINDING 495 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:5W74" FT DISULFID 237..286 FT /evidence="ECO:0007829|PDB:3LOS" FT DISULFID 470..484 FT /evidence="ECO:0007829|PDB:3KFB, ECO:0007829|PDB:3KFE" SQ SEQUENCE 543 AA; 58215 MW; 3ED9187B0B2EEC89 CRC64; MSQQPGVLPE NMKRYMGRDA QRMNILAGRI IAETVRSTLG PKGMDKMLVD DLGDVVVTND GVTILREMSV EHPAAKMLIE VAKTQEKEVG DGTTTAVVVA GELLRKAEEL LDQNVHPTIV VKGYQAAAQK AQELLKTIAC EVGAQDKEIL TKIAMTSITG KGAEKAKEKL AEIIVEAVSA VVDDEGKVDK DLIKIEKKSG ASIDDTELIK GVLVDKERVS AQMPKKVTDA KIALLNCAIE IKETETDAEI RITDPAKLME FIEQEEKMLK DMVAEIKASG ANVLFCQKGI DDLAQHYLAK EGIVAARRVK KSDMEKLAKA TGANVITNIK DLSAQDLGDA GLVEERKISG DSMIFVEECK HPKAVTMLIR GTTEHVIEEV ARAVDDAVGV VGCTIEDGRI VSGGGSTEVE LSMKLREYAE GISGREQLAV RAFADALEVI PRTLAENAGL DAIEILVKVR AAHASNGNKC AGLNVFTGAV EDMCENGVVE PLRVKTQAIQ SAAESTEMLL RIDDVIAAEK LRGAPDMGDM GGMPGMGGMP GMM //