ID   PRMG_RHOJR              Reviewed;         549 AA.
AC   Q0SJK2;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable chaperonin-like protein PrmG {ECO:0000303|PubMed:23171424};
GN   Name=prmG; Synonyms=groL1 {ECO:0000312|EMBL:ABG92284.1};
GN   OrderedLocusNames=RHA1_ro00448 {ECO:0000312|EMBL:ABG92284.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000312|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN   [2]
RP   FUNCTION.
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: Probably plays an essential role in the productive folding of
CC       PrmA, and thus in the formation of the active PrmABCD complex.
CC       {ECO:0000305|PubMed:23171424}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; CP000431; ABG92284.1; -; Genomic_DNA.
DR   RefSeq; WP_005242375.1; NC_008268.1.
DR   AlphaFoldDB; Q0SJK2; -.
DR   SMR; Q0SJK2; -.
DR   STRING; 101510.RHA1_ro00448; -.
DR   EnsemblBacteria; ABG92284; ABG92284; RHA1_ro00448.
DR   KEGG; rha:RHA1_ro00448; -.
DR   PATRIC; fig|101510.16.peg.476; -.
DR   eggNOG; COG0459; Bacteria.
DR   HOGENOM; CLU_016503_3_0_11; -.
DR   OMA; DGIEFDH; -.
DR   Proteomes; UP000008710; Chromosome.
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; Reference proteome.
FT   CHAIN           1..549
FT                   /note="Probable chaperonin-like protein PrmG"
FT                   /id="PRO_0000442971"
SQ   SEQUENCE   549 AA;  58079 MW;  9A730E47E76DEC96 CRC64;
     MAKELRYNTD ARARLEHGVN ALADAVKVTL GPKGRNAVLE KLTGPPTITN DGVTIAREIQ
     LREPFANMGA QLVKEVAMKT NGVVGDGTTT ATVLAQAMVR EGLRSVDAGA NPMRVRRGIE
     RAVSVVVDSL HEQASQIGGQ SDLQRIATLA ASDDEVIGHA ISKAVDYVGK SGVVTTEESD
     TLGLSVDIVD GIEFDHGYIS GYMVTDPERM EAVHTNPLIL LTNKKITQVQ DIMPSIEVAK
     RADRPLVVLA EEVDGPALQL LVGGNMHKTM QSVVVRAPGF GHRRVAELED LAVALGGHVI
     AKDTGIELSE ISVEHLGSCD RITVTENETT IVGGHGDQRL LDARIAQLES QHERAKIEAD
     QESLELRIAR LTGRVAVIRV GGATSVELKE RMLRVEDALA ATRAAVEAGI VSGGGTALAQ
     SHRALADLDL TGDEAIGCDV VRRALAEPLR WIAINAGFDG DEVVEVVAGL PLGHGFNALT
     GEYGDMFDDG VIDPFKVTRA ALESAASIAA LLITTETAVV EEVLGNPGAI MAPGFGDLAE
     GMVRPSNIY