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ZIM17_YEAS6
ID   ZIM17_YEAS6             Reviewed;         174 AA.
AC   B5VQB0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 39.
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=AWRI1631_140250;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
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=EDZ69887.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; ABSV01001936; EDZ69887.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B5VQB0; -.
DR   SMR; B5VQB0; -.
DR   Proteomes; UP000008988; 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_0000377663"
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
 
 
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