ID   TIM9_MESCR              Reviewed;          93 AA.
AC   Q9XGX8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim9;
GN   Name=TIM9;
OS   Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum;
OC   Mesembryanthemum subgen. Cryophytum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10611480; DOI=10.1016/s0014-5793(99)01665-8;
RA   Bauer M.F., Rothbauer U., Muehlenbein N., Smith R.J.H., Gerbitz K.-D.,
RA   Neupert W., Brunner M., Hofmann S.;
RT   "The mitochondrial TIM22 preprotein translocase is highly conserved
RT   throughout the eukaryotic kingdom.";
RL   FEBS Lett. 464:41-47(1999).
CC   -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC       the import and insertion of multi-pass transmembrane proteins into the
CC       mitochondrial inner membrane. May also be required for the transfer of
CC       beta-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. The complex associates with the
CC       TIM22 component of the TIM22 complex. Interacts with multi-pass
CC       transmembrane proteins in transit (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; AF150112; AAD40018.1; -; mRNA.
DR   PIR; T51189; T51189.
DR   AlphaFoldDB; Q9XGX8; -.
DR   SMR; Q9XGX8; -.
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..93
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim9"
FT                   /id="PRO_0000193606"
FT   MOTIF           43..67
FT                   /note="Twin CX3C motif"
FT   DISULFID        43..67
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..63
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   93 AA;  10879 MW;  D5FB1952CEAF48E9 CRC64;
     MDKNMLGDLD NLPEEDKLKM ASMIEQLQIR DSLRMYNNLV ERCFTDCVDS FRRKTLDKQE
     ETCVKRCAEK FLKHSMRVGL RFAELNQGAA TTD