ID   ZIM17_YEAS7             Reviewed;         174 AA.
AC   A6ZSH0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Mitochondrial protein import protein ZIM17;
DE   AltName: Full=Mitochondrial import inner membrane translocase subunit TIM15;
DE   AltName: Full=mtHsp70 escort protein 1;
DE   AltName: Full=mtHsp70-associated motor and chaperone protein TIM15/ZIM17;
DE            Short=MMC;
DE   Flags: Precursor;
GN   Name=ZIM17; ORFNames=SCY_4881;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Involved in protein import into mitochondria. Acts as a
CC       Hsp70-specific chaperone that prevents self-aggregation of the matrix
CC       Hsp70 chaperones SSC1 (mtHSP70) and SSQ1, thereby maintaining their
CC       function in mitochondrial protein import and Fe/S protein biosynthesis.
CC       May act together with PAM18 as co-chaperone to facilitate recognition
CC       and folding of imported proteins by SSC1 in the mitochondrial matrix
CC       (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with SSC1; binds to the nucleotide-free state as
CC       well as to the ADP- or ATP-bound state of SSC1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC       Note=Soluble matrix protein loosely associated with the inner membrane.
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN62518.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AAFW02000068; EDN62518.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A6ZSH0; -.
DR   SMR; A6ZSH0; -.
DR   EnsemblFungi; EDN62518; EDN62518; SCY_4881.
DR   HOGENOM; CLU_093902_1_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR024158; Mt_import_TIM15.
DR   InterPro; IPR007853; Znf_DNL-typ.
DR   PANTHER; PTHR20922; PTHR20922; 1.
DR   Pfam; PF05180; zf-DNL; 1.
DR   PROSITE; PS51501; ZF_DNL; 1.
PE   3: Inferred from homology;
KW   Chaperone; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Protein transport; Transit peptide;
KW   Transport; Zinc; Zinc-finger.
FT   TRANSIT         1..47
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           48..174
FT                   /note="Mitochondrial protein import protein ZIM17"
FT                   /id="PRO_0000377664"
FT   ZN_FING         64..159
FT                   /note="DNL-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
SQ   SEQUENCE   174 AA;  19855 MW;  4707DD1CA1490691 CRC64;
     MIPRTRTLLQ SKIPITRYFA RCWAPRVRYN VCRTLPAAAL HTNIIAHNEV KKDDKKVHLG
     SFKVDKPKMM IAFTCKKCNT RSSHTMSKQA YEKGTVLISC PHCKVRHLIA DHLKIFHDHH
     VTVEQLMKAN GEQVSQDVGD LEFEDIPDSL KDVLGKYAKN NSENASQLPH PSQK