ID   TI10B_XENLA             Reviewed;          90 AA.
AC   Q6GQ52;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim10-B;
GN   Name=timm10-b; Synonyms=tim10-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=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 TIMM9 and 3 copies of
CC       TIMM10/TIM10A, named soluble 70 kDa complex. The complex forms a 6-
CC       bladed alpha-propeller structure and associates with the TIMM22
CC       component of the TIM22 complex. Interacts with multi-pass transmembrane
CC       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 TIMM10 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; BC072896; AAH72896.1; -; mRNA.
DR   RefSeq; NP_001085530.1; NM_001092061.1.
DR   RefSeq; XP_018100528.1; XM_018245039.1.
DR   AlphaFoldDB; Q6GQ52; -.
DR   SMR; Q6GQ52; -.
DR   GeneID; 443956; -.
DR   KEGG; xla:443956; -.
DR   CTD; 443956; -.
DR   Xenbase; XB-GENE-6251518; timm10.L.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 443956; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IEA:InterPro.
DR   Gene3D; 1.10.287.810; -; 1.
DR   InterPro; IPR027100; Tim10.
DR   InterPro; IPR004217; Tim10-like.
DR   InterPro; IPR035427; Tim10-like_dom_sf.
DR   PANTHER; PTHR11038:SF16; PTHR11038:SF16; 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..90
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim10-B"
FT                   /id="PRO_0000228056"
FT   MOTIF           29..54
FT                   /note="Twin CX3C motif"
FT   DISULFID        29..54
FT                   /evidence="ECO:0000250"
FT   DISULFID        33..50
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   90 AA;  10279 MW;  3BD3467C2003F7F5 CRC64;
     MDPLKAQQLA AELEVEMMAD MYNRMTGACH KKCVPPHYKE AELSKGESVC LDRCVSKYLD
     IHERMGKKLT ELSLQDEELM KKMQQGVTST