ID YME1_YEAST Reviewed; 747 AA. AC P32795; D6W434; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 03-APR-2013, entry version 125. DE RecName: Full=Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1; DE EC=3.4.24.-; DE AltName: Full=Protein OSD1; DE AltName: Full=Tat-binding homolog 11; DE AltName: Full=Yeast mitochondrial escape protein 1; GN Name=YME1; Synonyms=OSD1, YTA11; OrderedLocusNames=YPR024W; GN ORFNames=YP9367.04; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND RP DISRUPTION PHENOTYPE. RX PubMed=8355690; RA Thorsness P.E., White K.H., Fox T.D.; RT "Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family of RT putative ATPase-encoding genes, causes increased escape of DNA from RT mitochondria in Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 13:5418-5426(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7754704; DOI=10.1002/yea.320100903; RA Schnall R., Mannhaupt G., Stucka R., Tauer R., Ehnle S., RA Schwarzlose C., Vetter I., Feldmann H.; RT "Identification of a set of yeast genes coding for a novel family of RT putative ATPases with high similarity to constituents of the 26S RT protease complex."; RL Yeast 10:1141-1155(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 24657 / D273-10B; RX PubMed=7623837; RA Nakai T., Yasuhara T., Fujiki Y., Ohashi A.; RT "Multiple genes, including a member of the AAA family, are essential RT for degradation of unassembled subunit 2 of cytochrome c oxidase in RT yeast mitochondria."; RL Mol. Cell. Biol. 15:4441-4452(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., RA Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., RA Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., RA Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., RA Zollner A., Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [5] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RG Saccharomyces Genome Database; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [6] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-327 AND GLU-541. RX PubMed=8688560; RA Weber E.R., Hanekamp T., Thorsness P.E.; RT "Biochemical and functional analysis of the YME1 gene product, an ATP RT and zinc-dependent mitochondrial protease from S. cerevisiae."; RL Mol. Biol. Cell 7:307-317(1996). RN [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [8] 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., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [9] RP PROTEASE ACTIVITY, FUNCTION, SUBSTRATE-BINDING, AND MUTAGENESIS OF RP LYS-327; TYR-354 AND GLU-381. RX PubMed=16527490; DOI=10.1016/j.jsb.2006.01.009; RA Graef M., Langer T.; RT "Substrate specific consequences of central pore mutations in the i- RT AAA protease Yme1 on substrate engagement."; RL J. Struct. Biol. 156:101-108(2006). RN [10] RP FUNCTION, INTERACTION WITH MGR1, AND IDENTIFICATION IN THE I-AAA RP COMPLEX. RX PubMed=16267274; DOI=10.1091/mbc.E05-06-0585; RA Dunn C.D., Lee M.S., Spencer F.A., Jensen R.E.; RT "A genomewide screen for petite-negative yeast strains yields a new RT subunit of the i-AAA protease complex."; RL Mol. Biol. Cell 17:213-226(2006). RN [11] RP SUBUNIT. RX PubMed=18843051; DOI=10.1091/mbc.E08-01-0103; RA Dunn C.D., Tamura Y., Sesaki H., Jensen R.E.; RT "Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease RT complex."; RL Mol. Biol. Cell 19:5387-5397(2008). CC -!- FUNCTION: Catalytic subunit of the mitochondrial inner membrane i- CC AAA protease supercomplex required for mitochondrial inner CC membrane protein turnover. The protease is probably ATP-dependent. CC Important to maintain the integrity of the mitochondrial CC compartment. Required both for the degradation of unassembled CC subunit 2 of cytochrome c oxidase (COX2) and for efficient CC assembly of mitochondrial respiratory chain. Binds unfolded CC substrates in an ATPase-independent manner; binding of folded CC COX2, a physiological substrate, requires an active ATPase but CC when COX2 is destabilized an active ATPase is no longer necessary. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Component of the mitochondrial inner membrane i-AAA CC protease supercomplex composed of MGR1, MGR3 and YME1. Interacts CC directly with MGR1. CC -!- INTERACTION: CC P25573:MGR1; NbExp=3; IntAct=EBI-27785, EBI-21740; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral CC membrane protein; Matrix side. Note=Although this protein does not CC have any predicted transmembrane helices it behaves like an CC integral membrane protein. CC -!- DISRUPTION PHENOTYPE: An increased rate of escape of mtDNA to the CC nucleus, no growth on nonfermentable carbon sources at 37 degrees CC Celsius, a cold-sensitive defect in growth on fermentable carbon CC sources, lethality in rho- (cytoplasmic petite) cells. CC -!- MISCELLANEOUS: Present with 20100 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase CC M41 family. 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; L14616; AAA02883.1; -; Genomic_DNA. DR EMBL; X81067; CAA56954.1; -; Genomic_DNA. DR EMBL; D16332; BAA03839.1; -; Genomic_DNA. DR EMBL; Z49274; CAA89278.1; -; Genomic_DNA. DR EMBL; Z71255; CAA95020.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11450.1; -; Genomic_DNA. DR PIR; S54498; S46608. DR RefSeq; NP_015349.1; NM_001184121.1. DR ProteinModelPortal; P32795; -. DR SMR; P32795; 271-708. DR IntAct; P32795; 6. DR STRING; 4932.YPR024W; -. DR MEROPS; M41.004; -. DR PaxDb; P32795; -. DR PeptideAtlas; P32795; -. DR EnsemblFungi; YPR024W; YPR024W; YPR024W. DR GeneID; 856135; -. DR KEGG; sce:YPR024W; -. DR CYGD; YPR024w; -. DR SGD; S000006228; YME1. DR eggNOG; COG0465; -. DR GeneTree; ENSGT00550000074836; -. DR HOGENOM; HOG000217276; -. DR KO; K08955; -. DR OMA; SEFDEVY; -. DR OrthoDB; EOG4FR40W; -. DR NextBio; 981236; -. DR Genevestigator; P32795; -. DR GermOnline; YPR024W; Saccharomyces cerevisiae. DR GO; GO:0031942; C:i-AAA complex; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IMP:SGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IMP:SGD. DR GO; GO:0006457; P:protein folding; IMP:SGD. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR005936; FtsH. DR InterPro; IPR000642; Peptidase_M41. DR Pfam; PF00004; AAA; 1. DR Pfam; PF01434; Peptidase_M41; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR01241; FtsH_fam; 1. DR PROSITE; PS00674; AAA; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Hydrolase; Membrane; Metal-binding; KW Metalloprotease; Mitochondrion; Mitochondrion inner membrane; KW Nucleotide-binding; Protease; Reference proteome; Zinc. FT CHAIN 1 747 Mitochondrial inner membrane i-AAA FT protease supercomplex subunit YME1. FT /FTId=PRO_0000084664. FT NP_BIND 321 328 ATP (Potential). FT ACT_SITE 541 541 By similarity. FT METAL 540 540 Zinc; catalytic (By similarity). FT METAL 544 544 Zinc; catalytic (By similarity). FT METAL 618 618 Zinc; catalytic (By similarity). FT MUTAGEN 327 327 K->I,R,T: Does not complement a YME1 FT deletion mutant, for K327R no longer FT binds or degrades COX2. Probably has no FT ATPase activity. FT MUTAGEN 354 354 Y->A,C,I,L,V: Partially complements a FT YME1 deletion mutant. FT MUTAGEN 354 354 Y->F,W: Complements a YME1 deletion FT mutant. FT MUTAGEN 354 354 Y->K,N,R,T: Does not complement a YME1 FT deletion mutant. FT MUTAGEN 354 354 Y->S: Does not complement a YME1 deletion FT mutant, retains 20% protease activity in FT vitro, binds an unfolded hybrid substrate FT protein. FT MUTAGEN 381 381 E->Q: Does not complement a YME1 deletion FT mutant, no longer binds or degrades COX2. FT Probably has no ATPase activity. FT MUTAGEN 541 541 E->A,G,V: Does not complement a YME1 FT deletion mutant, for E541A stabilizes FT otherwise unstable COX2. FT CONFLICT 52 52 N -> T (in Ref. 2; CAA56954). FT CONFLICT 88 88 T -> N (in Ref. 2; CAA56954). FT CONFLICT 584 584 T -> A (in Ref. 3; BAA03839). SQ SEQUENCE 747 AA; 81772 MW; CA7C5C90097C4F8B CRC64; MNVSKILVSP TVTTNVLRIF APRLPQIGAS LLVQKKWALR SKKFYRFYSE KNSGEMPPKK EADSSGKASN KSTISSIDNS QPPPPSNTND KTKQANVAVS HAMLATREQE ANKDLTSPDA QAAFYKLLLQ SNYPQYVVSR FETPGIASSP ECMELYMEAL QRIGRHSEAD AVRQNLLTAS SAGAVNPSLA SSSSNQSGYH GNFPSMYSPL YGSRKEPLHV VVSESTFTVV SRWVKWLLVF GILTYSFSEG FKYITENTTL LKSSEVADKS VDVAKTNVKF DDVCGCDEAR AELEEIVDFL KDPTKYESLG GKLPKGVLLT GPPGTGKTLL ARATAGEAGV DFFFMSGSEF DEVYVGVGAK RIRDLFAQAR SRAPAIIFID ELDAIGGKRN PKDQAYAKQT LNQLLVELDG FSQTSGIIII GATNFPEALD KALTRPGRFD KVVNVDLPDV RGRADILKHH MKKITLADNV DPTIIARGTP GLSGAELANL VNQAAVYACQ KNAVSVDMSH FEWAKDKILM GAERKTMVLT DAARKATAFH EAGHAIMAKY TNGATPLYKA TILPRGRALG ITFQLPEMDK VDITKRECQA RLDVCMGGKI AEELIYGKDN TTSGCGSDLQ SATGTARAMV TQYGMSDDVG PVNLSENWES WSNKIRDIAD NEVIELLKDS EERARRLLTK KNVELHRLAQ GLIEYETLDA HEIEQVCKGE KLDKLKTSTN TVVEGPDSDE RKDIGDDKPK IPTMLNA //