YTA12_YEAST
ID YTA12_YEAST Reviewed; 825 AA.
AC P40341; D6VZR2; E9P917;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Mitochondrial respiratory chain complexes assembly protein YTA12;
DE EC=3.4.24.-;
DE AltName: Full=Tat-binding homolog 12;
GN Name=YTA12; Synonyms=RCA1; OrderedLocusNames=YMR089C; ORFNames=YM9582.14C;
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].
RX PubMed=7929327; DOI=10.1016/s0021-9258(18)47170-0;
RA Tzagoloff A., Yue J., Jang J., Paul M.-F.;
RT "A new member of a family of ATPases is essential for assembly of
RT mitochondrial respiratory chain and ATP synthetase complexes in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 269:26144-26151(1994).
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., Schwarzlose C.,
RA 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 protease
RT complex.";
RL Yeast 10:1141-1155(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION IN THE M-AAA PROTEASE COMPLEX, FUNCTION OF THE M-AAA
RP PROTEASE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=8681382; DOI=10.1016/s0092-8674(00)81271-4;
RA Arlt H., Tauer R., Feldmann H., Neupert W., Langer T.;
RT "The YTA10-12 complex, an AAA protease with chaperone-like activity in the
RT inner membrane of mitochondria.";
RL Cell 85:875-885(1996).
RN [7]
RP FUNCTION OF THE M-AAA PROTEASE COMPLEX, AND MUTAGENESIS OF GLU-614.
RX PubMed=9707443; DOI=10.1093/emboj/17.16.4837;
RA Arlt H., Steglich G., Perryman R., Guiard B., Neupert W., Langer T.;
RT "The formation of respiratory chain complexes in mitochondria is under the
RT proteolytic control of the m-AAA protease.";
RL EMBO J. 17:4837-4847(1998).
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., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Acts as a component of the m-AAA protease complex which is a
CC ATP-dependent metalloprotease mediating degradation of non-assembled
CC mitochondrial inner membrane proteins. The complex is necessary for the
CC assembly of mitochondrial respiratory chain and ATPase complexes.
CC Function both in post-translational assembly and in the turnover of
CC mistranslated or misfolded polypeptides. {ECO:0000269|PubMed:8681382,
CC ECO:0000269|PubMed:9707443}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Component of the 850 kDa m-AAA protease complex (YTA10-12)
CC which consists of multiple copies of RCA1 AND AFG3.
CC {ECO:0000269|PubMed:8681382}.
CC -!- INTERACTION:
CC P40341; P39925: AFG3; NbExp=3; IntAct=EBI-14858, EBI-2317;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:8681382}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8681382}.
CC -!- MISCELLANEOUS: Present with 11500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000305}.
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DR EMBL; U09358; AAA62606.1; -; Genomic_DNA.
DR EMBL; X81068; CAA56955.1; -; Genomic_DNA.
DR EMBL; Z49259; CAA89236.1; -; Genomic_DNA.
DR EMBL; AY693099; AAT93118.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09986.1; -; Genomic_DNA.
DR PIR; S54465; S54465.
DR RefSeq; NP_013807.1; NM_001182589.1.
DR AlphaFoldDB; P40341; -.
DR SMR; P40341; -.
DR BioGRID; 35264; 188.
DR ComplexPortal; CPX-1654; m-AAA complex.
DR DIP; DIP-889N; -.
DR IntAct; P40341; 9.
DR MINT; P40341; -.
DR STRING; 4932.YMR089C; -.
DR MEROPS; M41.003; -.
DR TCDB; 3.A.29.1.1; the mitochondrial inner membrane i-aaa protease complex (mimp) familly.
DR MaxQB; P40341; -.
DR PaxDb; P40341; -.
DR PRIDE; P40341; -.
DR EnsemblFungi; YMR089C_mRNA; YMR089C; YMR089C.
DR GeneID; 855114; -.
DR KEGG; sce:YMR089C; -.
DR SGD; S000004695; YTA12.
DR VEuPathDB; FungiDB:YMR089C; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_0_1; -.
DR InParanoid; P40341; -.
DR OMA; DEAYKQC; -.
DR BioCyc; YEAST:G3O-32789-MON; -.
DR BRENDA; 3.4.24.B18; 984.
DR PRO; PR:P40341; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40341; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005745; C:m-AAA complex; IDA:SGD.
DR GO; GO:0097002; C:mitochondrial inner boundary membrane; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IDA:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IMP:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IDA:ComplexPortal.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IMP:SGD.
DR GO; GO:0006465; P:signal peptide processing; IMP:SGD.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Mitochondrion; Nucleotide-binding; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..825
FT /note="Mitochondrial respiratory chain complexes assembly
FT protein YTA12"
FT /id="PRO_0000084676"
FT TRANSMEM 178..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 43..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..170
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 614
FT /evidence="ECO:0000250"
FT BINDING 388..395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 617
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 689
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MUTAGEN 614
FT /note="E->Q: Abolishes proteolytic activity; impairs
FT synthesis of respiratory chain proteins COB and COX1. No
FT effect on m-AAA protease assembly."
FT /evidence="ECO:0000269|PubMed:9707443"
FT CONFLICT 195
FT /note="D -> G (in Ref. 5; AAT93118)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..350
FT /note="DV -> EL (in Ref. 2; CAA56955)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="I -> V (in Ref. 1; AAA62606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 825 AA; 93276 MW; 63CEBB9EF11B3DFC CRC64;
MLLLSWSRIA TKVVRRPVRF RSYYGLTHIK SLHTQYRLLN RLQENKSGNK NEDNNEDAKL
NKEIPTDEEV EAIRKQVEKY IEQTKNNTIP ANWKEQKRKI DESIRRLEDA VLKQESNRIQ
EERKEKEEEN GPSKAKSNRT KEQGYFEGNN SRNIPPPPPP PPPKPPLNDP SNPVSKNVNL
FQIGLTFFLL SFLLDLLNSL EEQSEITWQD FREKLLAKGY VAKLIVVNKS MVKVMLNDNG
KNQADNYGRN FYYFTIGSID SFEHKLQKAQ DELDIDKDFR IPVLYVQEGN WAKAMFQILP
TVLMIAGIIW LTRRSAQAAG GSRGGIFGLS RSKAKKFNTE TDVKIKFKDV AGCDEAKEEI
MEFVSFLKEP SRYEKMGAKI PRGAILSGPP GTGKTLLAKA TAGEAGVPFY FVSGSEFVEM
FVGVGAARVR DLFKTARENA PSIVFIDEID AIGKARQKGN FSGANDEREN TLNQMLVEMD
GFTPADHVVV LAGTNRPDIL DKALLRPGRF DRHINIDKPE LEGRKAIFAV HLHHLKLAGE
IFDLKNRLAA LTPGFSGADI ANVCNEAALI AARSDEDAVK LNHFEQAIER VIGGVERKSK
LLSPEEKKVV AYHEAGHAVC GWYLKYADPL LKVSIIPRGQ GALGYAQYLP GDIFLLTEQQ
LKDRMTMSLG GRVSEELHFP SVTSGASDDF KKVTSMATAM VTELGMSDKI GWVNYQKRDD
SDLTKPFSDE TGDIIDSEVY RIVQECHDRC TKLLKEKAED VEKIAQVLLK KEVLTREDMI
DLLGKRPFPE RNDAFDKYLN DYETEKIRKE EEKNEKRNEP KPSTN
