ZIM17_YEAS1
ID ZIM17_YEAS1 Reviewed; 174 AA.
AC B3LPE4;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 42.
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=SCRG_03434;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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=EDV12539.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH408049; EDV12539.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B3LPE4; -.
DR SMR; B3LPE4; -.
DR EnsemblFungi; EDV12539; EDV12539; SCRG_03434.
DR HOGENOM; CLU_093902_1_0_1; -.
DR Proteomes; UP000008335; 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_0000377662"
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