TIM44_YEAST
ID TIM44_YEAST Reviewed; 431 AA.
AC Q01852; D6VVQ7;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM44;
DE AltName: Full=Inner membrane import site protein 45;
DE Short=ISP45 {ECO:0000303|PubMed:8344245};
DE AltName: Full=Membrane import machinery protein MIM44;
DE AltName: Full=Mitochondrial protein import protein 1;
DE Flags: Precursor;
GN Name=TIM44; Synonyms=ISP45, MIM44, MPI1 {ECO:0000303|PubMed:1396562};
GN OrderedLocusNames=YIL022W;
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 204510 / AB320;
RX PubMed=1396562; DOI=10.1002/j.1460-2075.1992.tb05446.x;
RA Maarse A.C., Blom J., Grivell L.A., Meijer M.;
RT "MPI1, an essential gene encoding a mitochondrial membrane protein, is
RT possibly involved in protein import into yeast mitochondria.";
RL EMBO J. 11:3619-3628(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
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 PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX PubMed=8344245; DOI=10.1002/j.1460-2075.1993.tb05972.x;
RA Horst M., Jenoe P., Kronidou N.G., Bolliger L., Oppliger W., Scherer P.,
RA Manning-Krieg U., Jascur T., Schatz G.;
RT "Protein import into yeast mitochondria: the inner membrane import site
RT protein ISP45 is the MPI1 gene product.";
RL EMBO J. 12:3035-3041(1993).
RN [5]
RP IDENTIFICATION IN THE PAM COMPLEX WITH PAM16; PAM17; PAM18; MGE1 AND SSC1.
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 [6]
RP INTERACTION WITH SSC1, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-180.
RX PubMed=18426906; DOI=10.1128/mcb.00007-08;
RA Schiller D., Cheng Y.C., Liu Q., Walter W., Craig E.A.;
RT "Residues of Tim44 involved in both association with the translocon of the
RT inner mitochondrial membrane and regulation of mitochondrial Hsp70
RT tethering.";
RL Mol. Cell. Biol. 28:4424-4433(2008).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=26714107; DOI=10.7554/elife.11897;
RA Banerjee R., Gladkova C., Mapa K., Witte G., Mokranjac D.;
RT "Protein translocation channel of mitochondrial inner membrane and matrix-
RT exposed import motor communicate via two-domain coupling protein.";
RL Elife 4:E11897-E11897(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 234-425.
RX PubMed=16647716; DOI=10.1016/j.jmb.2006.04.020;
RA Josyula R., Jin Z., Fu Z., Sha B.;
RT "Crystal structure of yeast mitochondrial peripheral membrane protein
RT Tim44p C-terminal domain.";
RL J. Mol. Biol. 359:798-804(2006).
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. Recruits mitochondrial HSP70 and its co-chaperone (MGE1) to
CC drive protein translocation into the matrix using ATP as an energy
CC source. {ECO:0000269|PubMed:18426906, ECO:0000269|PubMed:26714107}.
CC -!- SUBUNIT: Component of the PAM complex, at least composed of SSC1
CC (mtHsp70), MGE1, TIM44, PAM16/TIM16, PAM17 and PAM18/TIM14. Forms part
CC of the receptor complex that consists of at least 3 different proteins
CC (TIM17, TIM23, TIM44). {ECO:0000269|PubMed:16107694,
CC ECO:0000269|PubMed:18426906, ECO:0000269|PubMed:26714107}.
CC -!- INTERACTION:
CC Q01852; P42949: PAM16; NbExp=3; IntAct=EBI-9141, EBI-26019;
CC Q01852; P0CS90: SSC1; NbExp=3; IntAct=EBI-9141, EBI-8637;
CC Q01852; P39515: TIM17; NbExp=2; IntAct=EBI-9141, EBI-9127;
CC Q01852; P32897: TIM23; NbExp=8; IntAct=EBI-9141, EBI-9136;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18426906}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18426906}.
CC -!- SIMILARITY: Belongs to the Tim44 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z46881; CAA86970.1; -; Genomic_DNA.
DR EMBL; X67276; CAA47693.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08523.1; -; Genomic_DNA.
DR PIR; S25196; S25196.
DR RefSeq; NP_012242.1; NM_001179372.1.
DR PDB; 2FXT; X-ray; 3.20 A; A=234-425.
DR PDB; 3QK9; X-ray; 3.10 A; A/B=210-431.
DR PDBsum; 2FXT; -.
DR PDBsum; 3QK9; -.
DR AlphaFoldDB; Q01852; -.
DR SMR; Q01852; -.
DR BioGRID; 34966; 92.
DR ComplexPortal; CPX-539; TIM23 mitochondrial inner membrane pre-sequence translocase complex, motor variant.
DR DIP; DIP-694N; -.
DR IntAct; Q01852; 21.
DR MINT; Q01852; -.
DR STRING; 4932.YIL022W; -.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR iPTMnet; Q01852; -.
DR MaxQB; Q01852; -.
DR PaxDb; Q01852; -.
DR PRIDE; Q01852; -.
DR EnsemblFungi; YIL022W_mRNA; YIL022W; YIL022W.
DR GeneID; 854790; -.
DR KEGG; sce:YIL022W; -.
DR SGD; S000001284; TIM44.
DR VEuPathDB; FungiDB:YIL022W; -.
DR eggNOG; KOG2580; Eukaryota.
DR GeneTree; ENSGT00390000000051; -.
DR HOGENOM; CLU_020932_2_0_1; -.
DR InParanoid; Q01852; -.
DR OMA; PVFVVTC; -.
DR BioCyc; YEAST:G3O-31297-MON; -.
DR EvolutionaryTrace; Q01852; -.
DR PRO; PR:Q01852; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; Q01852; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
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:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051087; F:chaperone binding; IMP:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:UniProtKB.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR017303; Tim44.
DR InterPro; IPR039544; Tim44-like.
DR InterPro; IPR007379; Tim44-like_dom.
DR PANTHER; PTHR10721; PTHR10721; 1.
DR Pfam; PF04280; Tim44; 1.
DR PIRSF; PIRSF037871; TIM44; 1.
DR SMART; SM00978; Tim44; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Transit peptide; Translocation;
KW Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..431
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM44"
FT /id="PRO_0000034319"
FT REGION 43..209
FT /note="Interaction with SSC1"
FT /evidence="ECO:0000269|PubMed:18426906"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 180
FT /note="R->A,K: Disrupts association with the translocase
FT complex."
FT /evidence="ECO:0000269|PubMed:18426906"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:3QK9"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:3QK9"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:2FXT"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:3QK9"
FT HELIX 286..295
FT /evidence="ECO:0007829|PDB:3QK9"
FT HELIX 297..307
FT /evidence="ECO:0007829|PDB:3QK9"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:3QK9"
FT HELIX 319..333
FT /evidence="ECO:0007829|PDB:3QK9"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:3QK9"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:3QK9"
FT STRAND 342..356
FT /evidence="ECO:0007829|PDB:3QK9"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:3QK9"
FT STRAND 363..374
FT /evidence="ECO:0007829|PDB:3QK9"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:3QK9"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:3QK9"
FT STRAND 394..404
FT /evidence="ECO:0007829|PDB:3QK9"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:2FXT"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2FXT"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:3QK9"
SQ SEQUENCE 431 AA; 48854 MW; 8E98C738178B1E44 CRC64;
MHRSTFIRTS GTSSRTLTAR YRSQYTGLLV ARVLFSTSTT RAQGGNPRSP LQIFRDTFKK
EWEKSQELQE NIKTLQDASG KLGESEAYKK AREAYLKAQR GSTIVGKTLK KTGETMEHIA
TKAWESELGK NTRKAAAATA KKLDESFEPV RQTKIYKEVS EVIDDGESSR YGGFITKEQR
RLKRERDLAS GKRHRAVKSN EDAGTAVVAT NIESKESFGK KVEDFKEKTV VGRSIQSLKN
KLWDESENPL IVVMRKITNK VGGFFAETES SRVYSQFKLM DPTFSNESFT RHLREYIVPE
ILEAYVKGDV KVLKKWFSEA PFNVYAAQQK IFKEQDVYAD GRILDIRGVE IVSAKLLAPQ
DIPVLVVGCR AQEINLYRKK KTGEIAAGDE ANILMSSYAM VFTRDPEQID DDETEGWKIL
EFVRGGSRQF T
