ID   TI13B_XENLA             Reviewed;          96 AA.
AC   Q8AVK1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim13-B;
GN   Name=timm13-b; Synonyms=tim13a-b, timm13a-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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 TIMM8-
CC       TIMM13 complex mediates the import of some proteins while the
CC       predominant TIMM9-TIMM10 70 kDa complex mediates the import of much
CC       more proteins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIMM8 (TIMM8A or
CC       TIMM8B) and 3 copies of TIMM13, named soluble 70 kDa complex.
CC       Associates with the TIM22 complex, whose core is composed of TIMM22 (By
CC       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 timm13-B from cytoplasm into mitochondrion, the
CC       Cys 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; BC042226; AAH42226.1; -; mRNA.
DR   RefSeq; NP_001079427.1; NM_001085958.1.
DR   AlphaFoldDB; Q8AVK1; -.
DR   SMR; Q8AVK1; -.
DR   DNASU; 379114; -.
DR   GeneID; 379114; -.
DR   KEGG; xla:379114; -.
DR   CTD; 379114; -.
DR   Xenbase; XB-GENE-6251644; timm13.S.
DR   OrthoDB; 1566384at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 379114; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:InterPro.
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   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..96
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim13-B"
FT                   /id="PRO_0000228068"
FT   MOTIF           47..70
FT                   /note="Twin CX3C motif"
FT   DISULFID        47..70
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..66
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   96 AA;  10605 MW;  45C8E79013B5D204 CRC64;
     MDGFGSDFSV GGSSSGKVDT GAIMEQVKVQ IAVANAQELL QRMTDKCFRK CIGKPGGSLD
     NSEQKCVAMC MDRYMDAWNI VSRAYNSRLQ RERAKM