ID   TIM16_SCHPO             Reviewed;         128 AA.
AC   Q9C1W5;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit tim16;
DE   AltName: Full=Presequence translocated-associated motor subunit pam16;
GN   Name=pam16; Synonyms=tim16; ORFNames=SPBC713.10;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; CU329671; CAC22611.1; -; Genomic_DNA.
DR   RefSeq; NP_595349.1; NM_001021257.2.
DR   AlphaFoldDB; Q9C1W5; -.
DR   SMR; Q9C1W5; -.
DR   BioGRID; 277667; 3.
DR   STRING; 4896.SPBC713.10.1; -.
DR   iPTMnet; Q9C1W5; -.
DR   MaxQB; Q9C1W5; -.
DR   PaxDb; Q9C1W5; -.
DR   PRIDE; Q9C1W5; -.
DR   EnsemblFungi; SPBC713.10.1; SPBC713.10.1:pep; SPBC713.10.
DR   GeneID; 2541152; -.
DR   KEGG; spo:SPBC713.10; -.
DR   PomBase; SPBC713.10; -.
DR   VEuPathDB; FungiDB:SPBC713.10; -.
DR   eggNOG; KOG3442; Eukaryota.
DR   HOGENOM; CLU_101461_2_1_1; -.
DR   InParanoid; Q9C1W5; -.
DR   OMA; RMFKIND; -.
DR   PhylomeDB; Q9C1W5; -.
DR   PRO; PR:Q9C1W5; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; ISS:PomBase.
DR   GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IBA:GO_Central.
DR   GO; GO:0015450; F:protein-transporting ATPase activity; ISS:PomBase.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; ISS:PomBase.
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..128
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit tim16"
FT                   /id="PRO_0000214096"
FT   REGION          59..113
FT                   /note="J-like"
FT   REGION          108..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   128 AA;  14120 MW;  912CBB3B6BBA58FC CRC64;
     MSLPRAVGRF IIVGSQVMSK AFVQAYKQMI ANAAQQSTGQ AAASKSSTAV RRGEMTIQEA
     GSILNIKPES LEEGELEKRF QKMFEINDPK KGGSFYLQSK VFRAHEKLKS ELDQKIQEQS
     PAKPTSSP