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