ID A0A2V0N4U8_9MYCO Unreviewed; 540 AA. AC A0A2V0N4U8; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 10-OCT-2018, entry version 2. DE RecName: Full=60 kDa chaperonin {ECO:0000256|HAMAP-Rule:MF_00600, ECO:0000256|RuleBase:RU000419}; DE AltName: Full=GroEL protein {ECO:0000256|HAMAP-Rule:MF_00600}; DE AltName: Full=Protein 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. OX NCBI_TaxID=2049453 {ECO:0000313|EMBL:GBE65377.1}; RN [1] {ECO:0000313|EMBL:GBE65377.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MFM001 {ECO:0000313|EMBL:GBE65377.1}; RA Kayanuma H., Ogihara K., Yoshida S., Yamamoto K., Wada T., RA Yamamoto T., 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: Prevents misfolding and promotes the refolding and CC proper assembly of unfolded polypeptides generated under stress CC conditions. {ECO:0000256|HAMAP-Rule:MF_00600, CC ECO:0000256|RuleBase:RU000419}. CC -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of CC 7 subunits. {ECO:0000256|HAMAP-Rule:MF_00600, CC ECO:0000256|RuleBase:RU000419}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600}. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000256|HAMAP-Rule:MF_00600, ECO:0000256|RuleBase:RU000418}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 CDD; cd03344; GroEL; 1. DR Gene3D; 1.10.560.10; -; 2. DR Gene3D; 3.30.260.10; -; 2. 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; 2. 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|HAMAP-Rule:MF_00600}; KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00600}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00600}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00600}. FT COILED 344 364 {ECO:0000256|SAM:Coils}. FT COILED 384 407 {ECO:0000256|SAM:Coils}. 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 //