ID   TIM16_CANGA             Reviewed;         146 AA.
AC   Q6FT88;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM16;
DE   AltName: Full=Presequence translocated-associated motor subunit PAM16;
GN   Name=PAM16; Synonyms=TIM16; OrderedLocusNames=CAGL0G04521g;
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: Essential component of the PAM complex, a complex required
CC       for the translocation of transit peptide-containing proteins from the
CC       inner membrane into the mitochondrial matrix in an ATP-dependent
CC       manner. In the complex, it is required to regulate activity of mtHSP70
CC       (SSC1) via its interaction with PAM18/TIM14. May act by positioning
CC       PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize
CC       ATPase stimulation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with PAM18. Component of the PAM complex, at least
CC       composed of mtHsp70, MGE1, TIM44, PAM16, PAM17 and PAM18 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The J-like region, although related to the J domain does not
CC       stimulate ATPase activity of mtHSP70. It nevertheless mediates the
CC       heterodimerization with the J domain of PAM18 and is therefore
CC       essential for PAM complex function (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TIM16/PAM16 family. {ECO:0000305}.
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DR   EMBL; CR380953; CAG59483.1; -; Genomic_DNA.
DR   RefSeq; XP_446556.1; XM_446556.1.
DR   AlphaFoldDB; Q6FT88; -.
DR   SMR; Q6FT88; -.
DR   STRING; 5478.XP_446556.1; -.
DR   EnsemblFungi; CAG59483; CAG59483; CAGL0G04521g.
DR   GeneID; 2887993; -.
DR   KEGG; cgr:CAGL0G04521g; -.
DR   CGD; CAL0130657; CAGL0G04521g.
DR   VEuPathDB; FungiDB:CAGL0G04521g; -.
DR   eggNOG; KOG3442; Eukaryota.
DR   HOGENOM; CLU_101461_0_1_1; -.
DR   InParanoid; Q6FT88; -.
DR   Proteomes; UP000002428; Chromosome G.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IEA:EnsemblFungi.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:EnsemblFungi.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IEA:EnsemblFungi.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR005341; Tim16.
DR   PANTHER; PTHR12388; PTHR12388; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW   Reference proteome; Translocation; Transport.
FT   CHAIN           1..146
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM16"
FT                   /id="PRO_0000214090"
FT   REGION          62..117
FT                   /note="J-like"
FT   REGION          118..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   146 AA;  15993 MW;  D179A25347A1F41A CRC64;
     MAHRALVKIV ITGTRVLGHA FAEAYRQAAA QSAAKQGASA MGRNKTGRGN AAAEYGGITL
     DESCKILNLD AAKDLKLDKV NQRFDYLFNI NDKEKGGSFY LQSKIYRASE RLKWELAQRE
     KEAAEEKLPK AEDASEDTGE KSPPSS