ID   TIM16_YEAST             Reviewed;         149 AA.
AC   P42949; D6VW80; Q6B2X3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 182.
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=YJL104W; ORFNames=J0822;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=7483851; DOI=10.1002/yea.320110909;
RA   Rasmussen S.W.;
RT   "A 37.5 kb region of yeast chromosome X includes the SME1, MEF2, GSH1 and
RT   CSD3 genes, a TCP-1-related gene, an open reading frame similar to the
RT   DAL80 gene, and a tRNA(Arg).";
RL   Yeast 11:873-883(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   FUNCTION, INTERACTION WITH PAM18, AND MUTAGENESIS OF 88-ASP--GLU-90.
RX   PubMed=15218029; DOI=10.1074/jbc.m404319200;
RA   Li Y., Dudek J., Guiard B., Pfanner N., Rehling P., Voos W.;
RT   "The presequence translocase-associated protein import motor of
RT   mitochondria. Pam16 functions in an antagonistic manner to Pam18.";
RL   J. Biol. Chem. 279:38047-38054(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PAM COMPLEX,
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAM18.
RX   PubMed=14981507; DOI=10.1038/nsmb735;
RA   Frazier A.E., Dudek J., Guiard B., Voos W., Li Y., Lind M., Meisinger C.,
RA   Geissler A., Sickmann A., Meyer H.E., Bilanchone V., Cumsky M.G.,
RA   Truscott K.N., Pfanner N., Rehling P.;
RT   "Pam16 has an essential role in the mitochondrial protein import motor.";
RL   Nat. Struct. Mol. Biol. 11:226-233(2004).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PAM COMPLEX,
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14981506; DOI=10.1038/nsmb734;
RA   Kozany C., Mokranjac D., Sichting M., Neupert W., Hell K.;
RT   "The J domain-related cochaperone Tim16 is a constituent of the
RT   mitochondrial TIM23 preprotein translocase.";
RL   Nat. Struct. Mol. Biol. 11:234-241(2004).
RN   [9]
RP   INTERACTION WITH MDJ2.
RX   PubMed=16027163; DOI=10.1074/jbc.m502397200;
RA   Mokranjac D., Sichting M., Popov-Celeketic D., Berg A., Hell K.,
RA   Neupert W.;
RT   "The import motor of the yeast mitochondrial TIM23 preprotein translocase
RT   contains two different J proteins, Tim14 and Mdj2.";
RL   J. Biol. Chem. 280:31608-31614(2005).
RN   [10]
RP   IDENTIFICATION IN THE PAM COMPLEX WITH PAM17; PAM18; TIM44; SSC1 AND MGE1.
RX   PubMed=16107694; DOI=10.1128/mcb.25.17.7449-7458.2005;
RA   van der Laan M., Chacinska A., Lind M., Perschil I., Sickmann A.,
RA   Meyer H.E., Guiard B., Meisinger C., Pfanner N., Rehling P.;
RT   "Pam17 is required for architecture and translocation activity of the
RT   mitochondrial protein import motor.";
RL   Mol. Cell. Biol. 25:7449-7458(2005).
RN   [11]
RP   SUBUNIT, DOMAIN J, AND INTERACTION WITH PAM18.
RX   PubMed=16105940; DOI=10.1073/pnas.0505969102;
RA   D'Silva P.R., Schilke B., Walter W., Craig E.A.;
RT   "Role of Pam16's degenerate J domain in protein import across the
RT   mitochondrial inner membrane.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12419-12424(2005).
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. {ECO:0000269|PubMed:14981506,
CC       ECO:0000269|PubMed:14981507, ECO:0000269|PubMed:15218029}.
CC   -!- SUBUNIT: Homodimer and heterodimer with PAM18. Homodimerization may not
CC       be relevant in vivo, while heterodimerization is essential for activity
CC       regulation of mtHSP70. Component of the PAM complex, at least composed
CC       of mtHsp70, MGE1, TIM44, PAM16, PAM17 and PAM18. Interacts with MDJ2.
CC       {ECO:0000269|PubMed:14981506, ECO:0000269|PubMed:14981507,
CC       ECO:0000269|PubMed:15218029, ECO:0000269|PubMed:16027163,
CC       ECO:0000269|PubMed:16105940, ECO:0000269|PubMed:16107694}.
CC   -!- INTERACTION:
CC       P42949; Q07914: PAM18; NbExp=6; IntAct=EBI-26019, EBI-31963;
CC       P42949; P39515: TIM17; NbExp=4; IntAct=EBI-26019, EBI-9127;
CC       P42949; P32897: TIM23; NbExp=6; IntAct=EBI-26019, EBI-9136;
CC       P42949; Q01852: TIM44; NbExp=3; IntAct=EBI-26019, EBI-9141;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14981506, ECO:0000269|PubMed:14981507}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:14981506,
CC       ECO:0000269|PubMed:14981507}.
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. {ECO:0000269|PubMed:16105940}.
CC   -!- MISCELLANEOUS: Present with 3180 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TIM16/PAM16 family. {ECO:0000305}.
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DR   EMBL; X85021; CAA59390.1; -; Genomic_DNA.
DR   EMBL; Z49379; CAA89399.1; -; Genomic_DNA.
DR   EMBL; AY692607; AAT92626.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08696.1; -; Genomic_DNA.
DR   PIR; S53383; S53383.
DR   RefSeq; NP_012431.1; NM_001181537.1.
DR   PDB; 2GUZ; X-ray; 2.00 A; B/D/F/H/J/L/N/P=54-117.
DR   AlphaFoldDB; P42949; -.
DR   SMR; P42949; -.
DR   BioGRID; 33652; 459.
DR   ComplexPortal; CPX-539; TIM23 mitochondrial inner membrane pre-sequence translocase complex, motor variant.
DR   FunCoup; P42949; 323.
DR   IntAct; P42949; 10.
DR   MINT; P42949; -.
DR   STRING; 4932.YJL104W; -.
DR   TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR   iPTMnet; P42949; -.
DR   PaxDb; 4932-YJL104W; -.
DR   PeptideAtlas; P42949; -.
DR   EnsemblFungi; YJL104W_mRNA; YJL104W; YJL104W.
DR   GeneID; 853340; -.
DR   KEGG; sce:YJL104W; -.
DR   AGR; SGD:S000003640; -.
DR   SGD; S000003640; PAM16.
DR   VEuPathDB; FungiDB:YJL104W; -.
DR   eggNOG; KOG3442; Eukaryota.
DR   HOGENOM; CLU_101461_0_1_1; -.
DR   InParanoid; P42949; -.
DR   OMA; RMFKIND; -.
DR   OrthoDB; 10262892at2759; -.
DR   BioCyc; YEAST:G3O-31558-MONOMER; -.
DR   BioGRID-ORCS; 853340; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P42949; -.
DR   PRO; PR:P42949; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P42949; protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IDA:SGD.
DR   GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IDA:SGD.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; NAS:ComplexPortal.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR   FunFam; 1.10.287.110:FF:000006; Import inner membrane translocase subunit TIM16; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR005341; Tim16.
DR   PANTHER; PTHR12388; MITOCHONDRIA ASSOCIATED GRANULOCYTE MACROPHAGE CSF SIGNALING MOLECULE; 1.
DR   PANTHER; PTHR12388:SF0; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM16; 1.
DR   Pfam; PF03656; Pam16; 1.
DR   PDBsum; 2GUZ; -.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Protein transport; Reference proteome; Translocation; Transport.
FT   CHAIN           1..149
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM16"
FT                   /id="PRO_0000214098"
FT   REGION          57..113
FT                   /note="J-like"
FT   REGION          115..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..149
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         88..90
FT                   /note="DKE->HPD: Does not confer ability to stimulate the
FT                   ATPase activity of mtHSP70."
FT                   /evidence="ECO:0000269|PubMed:15218029"
FT   CONFLICT        114
FT                   /note="Q -> H (in Ref. 4; AAT92626)"
FT                   /evidence="ECO:0000305"
FT   HELIX           55..61
FT                   /evidence="ECO:0007829|PDB:2GUZ"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:2GUZ"
FT   HELIX           73..86
FT                   /evidence="ECO:0007829|PDB:2GUZ"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:2GUZ"
FT   HELIX           95..116
FT                   /evidence="ECO:0007829|PDB:2GUZ"
SQ   SEQUENCE   149 AA;  16216 MW;  42BB69D746264B47 CRC64;
     MAHRAFIQVI ITGTQVFGKA FAEAYRQAAS QSVKQGATNA SRRGTGKGEY GGITLDESCK
     ILNIEESKGD LNMDKINNRF NYLFEVNDKE KGGSFYLQSK VYRAAERLKW ELAQREKNAK
     AKAGDASTAK PPPNSTNSSG ADNSASSNQ
//