ID   PRMG_GORST              Reviewed;         391 AA.
AC   Q768S8;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable chaperonin-like protein PrmG {ECO:0000303|PubMed:23171424};
DE   Flags: Fragment;
GN   Name=prmG {ECO:0000305};
OS   Gordonia sp. (strain TY-5).
OC   Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=235467;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TY-5 {ECO:0000312|EMBL:BAD03963.1};
RX   PubMed=14645271; DOI=10.1128/jb.185.24.7120-7128.2003;
RA   Kotani T., Yamamoto T., Yurimoto H., Sakai Y., Kato N.;
RT   "Propane monooxygenase and NAD+-dependent secondary alcohol dehydrogenase
RT   in propane metabolism by Gordonia sp. strain TY-5.";
RL   J. Bacteriol. 185:7120-7128(2003).
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 PrmC, 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}.
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; AB112920; BAD03963.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q768S8; -.
DR   SMR; Q768S8; -.
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   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.
PE   3: Inferred from homology;
KW   Chaperone.
FT   CHAIN           1..>391
FT                   /note="Probable chaperonin-like protein PrmG"
FT                   /id="PRO_0000442970"
FT   REGION          153..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         391
FT                   /evidence="ECO:0000312|EMBL:BAD03963.1"
SQ   SEQUENCE   391 AA;  42289 MW;  8E2602F15EFFEEAB CRC64;
     MAKELRYNAE ARLRLERGVN ALADAVKVTL GPKGRNAVLE KLTGPPTITN DGVTIAREIQ
     LRDPFANMGA QLVKEVAMKT NGVVGDGTTT ATVLAQAMVR EGLRAVEQGA NPMRVRRGIE
     RAVTAVLGSL TEQAVQIGGR SDLERIARWP PATTRWSVRS SPPPSNTSAR TASSPPRRAT
     HSGCRSRSST ASEFDHGYIS GYMVTNPERM EAVLDNPVVL LTNKKITSVQ EIMPAIEVAK
     RADRPLLVLA EDVDGPALQL LVGGNMHNTM RSVVVRAPGF GHRRIAELED LSVALGGHVI
     AKDTGIELSE VSMEHLGTVM RVTVTENETT IVGAHGEQEL VDARVRHLEA QLERARIDAD
     RDALELRIAR MTGRVAVIRV GGVTSVELKE R