ID A0A2V0N4U8_9MYCO Unreviewed; 540 AA. AC A0A2V0N4U8; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 19-JAN-2022, entry version 13. DE RecName: Full=Chaperonin GroEL {ECO:0000256|HAMAP-Rule:MF_00600}; DE EC=5.6.1.7 {ECO:0000256|HAMAP-Rule:MF_00600}; DE AltName: Full=60 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00600}; DE AltName: Full=Chaperonin-60 {ECO:0000256|HAMAP-Rule:MF_00600}; DE Short=Cpn60 {ECO:0000256|HAMAP-Rule:MF_00600}; GN Name=groL2 {ECO:0000313|EMBL:GBE65377.1}; GN Synonyms=groEL {ECO:0000256|HAMAP-Rule:MF_00600}, groL GN {ECO:0000256|HAMAP-Rule:MF_00600}; GN ORFNames=MFM001_18390 {ECO:0000313|EMBL:GBE65377.1}; OS Mycobacterium sp. MFM001. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; unclassified Mycobacterium. OX NCBI_TaxID=2049453 {ECO:0000313|EMBL:GBE65377.1, ECO:0000313|Proteomes:UP000256682}; RN [1] {ECO:0000313|EMBL:GBE65377.1, ECO:0000313|Proteomes:UP000256682} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MFM001 {ECO:0000313|EMBL:GBE65377.1, RC ECO:0000313|Proteomes:UP000256682}; RX PubMed=29885807; DOI=10.1016/j.vetmic.2018.05.010; RA Kayanuma H., Ogihara K., Yoshida S., Yamamoto K., Wada T., Yamamoto T., RA Tsuyuki Y., Madarame H.; RT "Disseminated nontuberculous mycobacterial disease in a cat caused by RT Mycobacterium sp. strain MFM001."; RL Vet. Microbiol. 220:90-96(2018). 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:0000256|HAMAP-Rule:MF_00600, CC ECO:0000256|RuleBase:RU000419}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H(2)O + a folded polypeptide = ADP + phosphate + an CC unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00600, ECO:0000256|RuleBase:RU000419}. CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}. CC Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600}. Secreted, capsule CC {ECO:0000256|ARBA:ARBA00025702}. Secreted, cell wall CC {ECO:0000256|ARBA:ARBA00004191}. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000256|ARBA:ARBA00006607, ECO:0000256|HAMAP-Rule:MF_00600, CC ECO:0000256|RuleBase:RU000418}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00600}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:GBE65377.1}. 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; BFAB01000004; GBE65377.1; -; Genomic_DNA. DR EnsemblBacteria; GBE65377; GBE65377; MFM001_18390. DR Proteomes; UP000256682; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. 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; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00600}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00600}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00600}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00600}. FT NP_BIND 29..32 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT NP_BIND 86..90 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT NP_BIND 476..478 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT COILED 344..364 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 384..407 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 413 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" FT BINDING 492 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00600" SQ SEQUENCE 540 AA; 56716 MW; E3227B3335D9858E CRC64; MAKTIAYDEE ARRGLERGLN SLADAVKVTL GPKGRNVVLE KKWGAPTITN DGVSIAKEIE LEDPYEKIGA ELVKEVAKKT DDVAGDGTTT ATVLAQALVK EGLRNVAAGA NPLGLKRGIE KAVEKVTETL LKGAKEVETK EQIAATAAIS AGDQSIGDLI AEAMDKVGNE GVITVEESNT FGLQLELTEG MRFDKGYISG YFVTDAERQE AVLEEPYILL VSSKVSTVKD LLPLLEKVIQ AGKPLLIIAE DVEGEALSTL VVNKIRGTFK SVAVKAPGFG DRRKAMLQDM AILTGGQVIS EEVGLTLENA DLSLLGKARK VVVTKDETTI VEGAGDTDAI AGRVAQIRQE IENSDSDYDR EKLQERLAKL AGGVAVIKAG AATEVELKER KHRIEDAVRN AKAAVEEGIV AGGGVTLLQA APTLDELKLS GDEATGANIV KVALEAPLKQ IAFNSGLEPG VVAEKVRNSP AGTGLNAATG EYEDLLKAGV ADPVKVTRSA LQNAASIAGL FLTTEAVVAD KPEKEKAAMP GGGDMGGMDF //