TIM16_GIBZE
ID TIM16_GIBZE Reviewed; 138 AA.
AC Q4I375; A0A098DCG5; A0A0E0RZG9; A0A1C3YM27; V6RKP0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM16;
DE AltName: Full=Presequence translocated-associated motor subunit PAM16;
GN Name=PAM16; Synonyms=TIM16;
GN ORFNames=FGRAMPH1_01T09683, FGRRES_08333_M, FGSG_08333;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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}.
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; DS231667; ESU15031.1; -; Genomic_DNA.
DR EMBL; HG970333; SCB65585.1; -; Genomic_DNA.
DR RefSeq; XP_011320456.1; XM_011322154.1.
DR AlphaFoldDB; Q4I375; -.
DR SMR; Q4I375; -.
DR STRING; 5518.FGSG_08333P0; -.
DR EnsemblFungi; ESU15031; ESU15031; FGSG_08333.
DR GeneID; 23555345; -.
DR KEGG; fgr:FGSG_08333; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G09683; -.
DR eggNOG; KOG3442; Eukaryota.
DR HOGENOM; CLU_101461_0_1_1; -.
DR InParanoid; Q4I375; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IEA:InterPro.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IEA:InterPro.
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..138
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM16"
FT /id="PRO_0000214093"
FT REGION 58..115
FT /note="J-like"
SQ SEQUENCE 138 AA; 15147 MW; 498917C720858B45 CRC64;
MAHKFVVTAF LTGSRILGRS FVAAYKQAQA ASAYQRAQVK AGNTTGGASL SSGMTLDEAC
KILNVKPPAG GQANVEEVLS RYKRLFDAND PQKGGSFYLQ SKIVRAKERF EREIGPLREK
MEAEAEIKEG FKPKVYKD
