ID   MIMG_MYCGD              Reviewed;         549 AA.
AC   A0A0K0XCY8;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Chaperonin-like protein MimG {ECO:0000303|PubMed:23171424};
GN   Name=mimG {ECO:0000303|PubMed:23171424};
GN   ORFNames=AFA91_29085 {ECO:0000312|EMBL:AKS35289.1};
OS   Mycobacterium goodii (Mycolicibacterium goodii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=134601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X7B;
RX   PubMed=26278197; DOI=10.1016/j.jbiotec.2015.08.004;
RA   Yu B., Tao F., Li F., Hou J., Tang H., Ma C., Xu P.;
RT   "Complete genome sequence of Mycobacterium goodii X7B, a facultative
RT   thermophilic biodesulfurizing bacterium with industrial potential.";
RL   J. Biotechnol. 212:56-57(2015).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=12523;
RX   PubMed=23171424; DOI=10.1111/febs.12070;
RA   Furuya T., Hayashi M., Semba H., Kino K.;
RT   "The mycobacterial binuclear iron monooxygenases require a specific
RT   chaperonin-like protein for functional expression in a heterologous host.";
RL   FEBS J. 280:817-826(2013).
CC   -!- FUNCTION: Plays an essential role in the productive folding of MimA and
CC       MimC, and thus in the formation of the active MimABCD complex.
CC       {ECO:0000305|PubMed:23171424}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23171424}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; CP012150; AKS35289.1; -; Genomic_DNA.
DR   RefSeq; WP_049747750.1; NZ_CP012150.1.
DR   AlphaFoldDB; A0A0K0XCY8; -.
DR   SMR; A0A0K0XCY8; -.
DR   STRING; 134601.AFA91_29085; -.
DR   EnsemblBacteria; AKS35289; AKS35289; AFA91_29085.
DR   KEGG; mgo:AFA91_29085; -.
DR   PATRIC; fig|134601.6.peg.6012; -.
DR   OrthoDB; 265347at2; -.
DR   Proteomes; UP000062255; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
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   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.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm.
FT   CHAIN           1..549
FT                   /note="Chaperonin-like protein MimG"
FT                   /id="PRO_0000442979"
SQ   SEQUENCE   549 AA;  58156 MW;  59B15C926401299F CRC64;
     MAKELRFNSD ARARLEQGVN ALADAVKVTL GPKGRNAILE KLTGPPTITN DGVTIAREIQ
     LRDPFANMGA QLVKEVAMKT NGVVGDGTTT ATVLAQAMVR EGLEAVDAGA NPMRVRRGIE
     RTVPVVVESL RSHSVEVGSS ADLRRIAALA ASDDEAIGDV IAAAVEHVGK SGVVTTEESD
     TLGMAVDVVD GIEFDHGYTS GYMVTDPERM EAVLDNPLIL LTNKKISQVQ EIMPTLEVAK
     RADRPLVVIA EDVDGPALQL LVGGNMHKTM RSVVVRAPGF GHRRVAELED LAVALNGHVI
     AKDTGIELGE VTREHLGSCD RLTATENDTT IVGPHGLQNL VDARVAQLEA QRERARLDAD
     RDILDLRIAR LTGRVAVIRV GGATSVELKE RMLRVEDALA ATRAALEAGI VSGGGTALAQ
     AHRALDTLEL VGDEAIGRDV VRRALAEPLR WIAINAGFEG DDVVDVVADL PLGHGFNALT
     GEYGDMFEEG IIDPFKVTRA ALESAASIAA LLITTETAVV EEIVGQPGAI MAPGFGDLAE
     GMVRPSNIY