MIMG_MYCS2
ID MIMG_MYCS2 Reviewed; 549 AA.
AC A0QTV4;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Chaperonin-like protein MimG {ECO:0000303|PubMed:23171424};
GN Name=mimG {ECO:0000303|PubMed:23171424};
GN Synonyms=groL {ECO:0000312|EMBL:ABK75509.1};
GN OrderedLocusNames=MSMEG_1978 {ECO:0000312|EMBL:ABK75509.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 700084 / mc(2)155;
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:0000269|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; CP000480; ABK75509.1; -; Genomic_DNA.
DR RefSeq; WP_003893353.1; NZ_SIJM01000020.1.
DR RefSeq; YP_886342.1; NC_008596.1.
DR AlphaFoldDB; A0QTV4; -.
DR SMR; A0QTV4; -.
DR STRING; 246196.MSMEI_1934; -.
DR EnsemblBacteria; ABK75509; ABK75509; MSMEG_1978.
DR GeneID; 66733408; -.
DR KEGG; msm:MSMEG_1978; -.
DR PATRIC; fig|246196.19.peg.1955; -.
DR eggNOG; COG0459; Bacteria.
DR OMA; DGIEFDH; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000000757; 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; Reference proteome.
FT CHAIN 1..549
FT /note="Chaperonin-like protein MimG"
FT /id="PRO_0000442978"
SQ SEQUENCE 549 AA; 58047 MW; 17CF811ECD557561 CRC64;
MAKELRFNSD ARARLEQGVN ALADAVKVTL GPKGRNAILE KLTGPPTITN DGVTIAREIQ
LRDPFANMGA QLVKEVAMKT NGVVGDGTTT ATVLAQAMVR EGLAAVEAGA NPMRVRRGIE
RTVPVVVESL RSHSVEVGSS SDLRRIAALA ASDDEAIGDV IAAAVEHVGK TGVVTTEESD
TLGMAVDVVD GIEFDHGYTS GYMVTDPERM EAVLDNPLIL LTNKKISQVQ EIMPTLEVAK
RADRPLVVIA EDVDGPALQL LVGGNMHKTM QSVVVRAPGF GHRRVAELED LAVALGGHVI
AKDTGIDLGE VAREHLGSCD RLTATESDTT IVGPRGHQNL VDARVAQLEV QRERARIDAD
RDILDLRIAR LTGRVAVIRV GGATSVELKE RMLRVEDALA ATRAALEAGI VSGGGTALAQ
AHRVLDAVEL VGDEAIGRDV VRRALSEPLR WIAFNAGFEG GDVVDVVADL PLGHGFNALT
GEYGDMFEEG IIDPFKVTRA ALESAASIAA LLITTETAVV EEILGQPGAI MAPGFGDLAE
GMVRPSNIY
