ID   CH62_MAIZE              Reviewed;         576 AA.
AC   Q43298; Q43253;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Chaperonin CPN60-2, mitochondrial;
DE   AltName: Full=HSP60-2;
DE   Flags: Precursor;
GN   Name=CPN60II; Synonyms=CPNB;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. B73;
RA   Close P.S.;
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. MUTIND-FR7205024;
RA   Burt W.J.;
RL   Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Implicated in mitochondrial protein import and macromolecular
CC       assembly. May facilitate the correct folding of imported proteins. May
CC       also prevent misfolding and promote the refolding and proper assembly
CC       of unfolded polypeptides generated under stress conditions in the
CC       mitochondrial matrix.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; L21008; AAA33451.1; -; Genomic_DNA.
DR   EMBL; L21006; AAA33452.1; -; mRNA.
DR   EMBL; Z12115; CAA78101.1; -; mRNA.
DR   PIR; S26583; S26583.
DR   RefSeq; NP_001105690.1; NM_001112220.1.
DR   AlphaFoldDB; Q43298; -.
DR   SMR; Q43298; -.
DR   STRING; 4577.GRMZM2G416120_P01; -.
DR   PaxDb; Q43298; -.
DR   PRIDE; Q43298; -.
DR   EnsemblPlants; Zm00001eb046580_T001; Zm00001eb046580_P001; Zm00001eb046580.
DR   GeneID; 542707; -.
DR   Gramene; Zm00001eb046580_T001; Zm00001eb046580_P001; Zm00001eb046580.
DR   KEGG; zma:542707; -.
DR   MaizeGDB; 65675; -.
DR   eggNOG; KOG0356; Eukaryota.
DR   HOGENOM; CLU_016503_3_0_1; -.
DR   OMA; GSETFGF; -.
DR   OrthoDB; 415781at2759; -.
DR   Proteomes; UP000007305; Chromosome 1.
DR   ExpressionAtlas; Q43298; baseline and differential.
DR   Genevisible; Q43298; ZM.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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   HAMAP; MF_00600; CH60; 1.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
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.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; Stress response; Transit peptide.
FT   TRANSIT         1..34
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           35..576
FT                   /note="Chaperonin CPN60-2, mitochondrial"
FT                   /id="PRO_0000005015"
FT   CONFLICT        117
FT                   /note="T -> N (in Ref. 2; CAA78101)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="L -> P (in Ref. 2; CAA78101)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        258
FT                   /note="K -> R (in Ref. 2; CAA78101)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   576 AA;  60935 MW;  1039FB77D7895321 CRC64;
     MYRAAASLAS KARQAGSSSA ARQVGSRLAW SRNYAAKDIK FGVEARALML RGVEELADAV
     KVTMGPKGRN VVIEQSFGAP KVTKDGVTVA KSIEFKDRVK NVGASLVKQV ANATNDTAGD
     GTTCATVLTK AIFTEGCKSV AAGMNAMDLR RGISMAVDAV VTNLKGMARM ISTSEEIAQV
     GTISANGERE IGELIAKAME KVGKEGVITI ADGNTLYNEL EVVEGMKLDR GYISPYFITN
     SKAQKCELED PLILIHDKKV TNMHAVVKVL EMALKKQRPL LIVAEDVESE ALGTLIINKL
     RAGIKVCAVK APGFGENRKA NLQDLAILTG GEVITEELGM NLENVEPHML GSCKKVTVSK
     DDTVILDGAG DKKSIEERAD QIRSAVENST SDYDKEKLQE RLAKLSGGVA VLKIGGASEA
     EVGEKKDRVT DALNATKAAV EEGIVPGGGV ALLYASKELD KLQTANFDQK IGVQIIQNAL
     KTPVHTIASN AGVEGAVVVG KLLEQGNTDL GYDAAKDEYV DMVKAGIIDP LKVIRTALVD
     AASVSSLMTT TESIIVEIPK EEAPAPAMGG MGGMDY