ID   TIM13_CANGA             Reviewed;          95 AA.
AC   Q6FRE1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM13;
GN   Name=TIM13; OrderedLocusNames=CAGL0H09306g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC       the import and insertion of some multi-pass transmembrane proteins into
CC       the mitochondrial inner membrane. Also 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. The TIM8-
CC       TIM13 complex is non essential and only mediates the import of few
CC       proteins, while the predominant TIM9-TIM10 70 kDa complex is crucial
CC       and mediates the import of much more proteins (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIM8 and 3 copies of
CC       TIM13, 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 TIM13 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR380954; CAG60136.1; -; Genomic_DNA.
DR   RefSeq; XP_447203.1; XM_447203.1.
DR   AlphaFoldDB; Q6FRE1; -.
DR   SMR; Q6FRE1; -.
DR   STRING; 5478.XP_447203.1; -.
DR   EnsemblFungi; CAG60136; CAG60136; CAGL0H09306g.
DR   GeneID; 2888718; -.
DR   KEGG; cgr:CAGL0H09306g; -.
DR   CGD; CAL0131900; CAGL0H09306g.
DR   VEuPathDB; FungiDB:CAGL0H09306g; -.
DR   eggNOG; KOG1733; Eukaryota.
DR   HOGENOM; CLU_141397_0_1_1; -.
DR   InParanoid; Q6FRE1; -.
DR   OMA; RCISQCM; -.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140318; F:protein transporter activity; IEA:EnsemblFungi.
DR   GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IEA:EnsemblFungi.
DR   Gene3D; 1.10.287.810; -; 1.
DR   InterPro; IPR004217; Tim10-like.
DR   InterPro; IPR035427; Tim10-like_dom_sf.
DR   InterPro; IPR039238; Tim8/13.
DR   PANTHER; PTHR19338; PTHR19338; 1.
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; Reference proteome;
KW   Translocation; Transport; Zinc.
FT   CHAIN           1..95
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM13"
FT                   /id="PRO_0000228072"
FT   MOTIF           47..67
FT                   /note="Twin CX3C motif"
FT   DISULFID        47..67
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..63
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   95 AA;  10342 MW;  148F5B86C87285CE CRC64;
     MALFGGSSSQ APASATDNKV QAFKQQIAQE IAVANATDLV NKVSENCFEK CLQSPYKDGN
     EGCVDQCLAK YMRSWNVISK TYINRIQDAS TTGEI