ID   TIM9_ZYGBA              Reviewed;          87 AA.
AC   P57745;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim9;
GN   Name=TIM9;
OS   Zygosaccharomyces bailii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=4954;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 685 / NCYC 563 / NRRL Y-12949;
RX   PubMed=11169759;
RX   DOI=10.1002/1097-0061(20010130)18:2<173::aid-yea663>3.0.co;2-f;
RA   Mollapour M., Piper P.W.;
RT   "Targeted gene deletion in Zygosaccharomyces bailii.";
RL   Yeast 18:173-186(2001).
CC   -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC       the import and insertion of multi-pass transmembrane proteins into the
CC       mitochondrial inner membrane. Also required for the transfer of beta-
CC       barrel precursors from the TOM complex to the sorting and assembly
CC       machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC       protein that protects the hydrophobic precursors from aggregation and
CC       guide them through the mitochondrial intermembrane space (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIM9 and 3 copies of
CC       TIM10, named soluble 70 kDa complex. Associates with the TIM22 complex,
CC       whose core is composed of TIM22 and TIM54. Interacts with the
CC       transmembrane regions of multi-pass transmembrane proteins in transit
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC       {ECO:0000250}.
CC   -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form
CC       2 disulfide bonds in the mitochondrial intermembrane space. However,
CC       during the transit of TIM9 from cytoplasm into mitochondrion, the Cys
CC       residues probably coordinate zinc, thereby preventing folding and
CC       allowing its transfer across mitochondrial outer membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR   EMBL; AF279260; AAG17695.1; -; Genomic_DNA.
DR   AlphaFoldDB; P57745; -.
DR   SMR; P57745; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.810; -; 1.
DR   InterPro; IPR004217; Tim10-like.
DR   InterPro; IPR035427; Tim10-like_dom_sf.
DR   Pfam; PF02953; zf-Tim10_DDP; 1.
DR   SUPFAM; SSF144122; SSF144122; 1.
PE   3: Inferred from homology;
KW   Chaperone; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Protein transport; Translocation; Transport;
KW   Zinc.
FT   CHAIN           1..87
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim9"
FT                   /id="PRO_0000193611"
FT   MOTIF           35..59
FT                   /note="Twin CX3C motif"
FT   DISULFID        35..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..55
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   87 AA;  10198 MW;  BBAB2C5D909347CD CRC64;
     MDSLNPREQQ EFSKLIEHKQ MKDFMRLYSN LVERCFTDCV NDFTSSKLTS KEQTCISRCS
     EKFLKHSERV GLRFQEQNAA MGQGLGR