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Mitochondrial respiratory chain complexes assembly protein YTA12 (EC 3.4.24.-) (Tat-binding homolog 12)

 YTA12_YEAST             Reviewed;         825 AA.
P40341; D6VZR2; E9P917;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
22-NOV-2017, entry version 170.
RecName: Full=Mitochondrial respiratory chain complexes assembly protein YTA12;
EC=3.4.24.-;
AltName: Full=Tat-binding homolog 12;
Name=YTA12; Synonyms=RCA1; OrderedLocusNames=YMR089C;
ORFNames=YM9582.14C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7929327;
Tzagoloff A., Yue J., Jang J., Paul M.-F.;
"A new member of a family of ATPases is essential for assembly of
mitochondrial respiratory chain and ATP synthetase complexes in
Saccharomyces cerevisiae.";
J. Biol. Chem. 269:26144-26151(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7754704; DOI=10.1002/yea.320100903;
Schnall R., Mannhaupt G., Stucka R., Tauer R., Ehnle S.,
Schwarzlose C., Vetter I., Feldmann H.;
"Identification of a set of yeast genes coding for a novel family of
putative ATPases with high similarity to constituents of the 26S
protease complex.";
Yeast 10:1141-1155(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
IDENTIFICATION IN THE M-AAA PROTEASE COMPLEX, FUNCTION OF THE M-AAA
PROTEASE COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=8681382; DOI=10.1016/S0092-8674(00)81271-4;
Arlt H., Tauer R., Feldmann H., Neupert W., Langer T.;
"The YTA10-12 complex, an AAA protease with chaperone-like activity in
the inner membrane of mitochondria.";
Cell 85:875-885(1996).
[7]
FUNCTION OF THE M-AAA PROTEASE COMPLEX, AND MUTAGENESIS OF GLU-614.
PubMed=9707443; DOI=10.1093/emboj/17.16.4837;
Arlt H., Steglich G., Perryman R., Guiard B., Neupert W., Langer T.;
"The formation of respiratory chain complexes in mitochondria is under
the proteolytic control of the m-AAA protease.";
EMBO J. 17:4837-4847(1998).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
-!- FUNCTION: Acts as a component of the m-AAA protease complex which
is a ATP-dependent metalloprotease mediating degradation of non-
assembled mitochondrial inner membrane proteins. The complex is
necessary for the assembly of mitochondrial respiratory chain and
ATPase complexes. Function both in post-translational assembly and
in the turnover of mistranslated or misfolded polypeptides.
{ECO:0000269|PubMed:8681382, ECO:0000269|PubMed:9707443}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
Note=Binds 1 zinc ion per subunit. {ECO:0000305};
-!- SUBUNIT: Component of the 850 kDa m-AAA protease complex (YTA10-
12) which consists of multiple copies of RCA1 AND AFG3.
{ECO:0000269|PubMed:8681382}.
-!- INTERACTION:
P39925:AFG3; NbExp=3; IntAct=EBI-14858, EBI-2317;
-!- SUBCELLULAR LOCATION: Mitochondrion membrane
{ECO:0000269|PubMed:8681382}; Multi-pass membrane protein
{ECO:0000269|PubMed:8681382}.
-!- MISCELLANEOUS: Present with 11500 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the peptidase
M41 family. {ECO:0000305}.
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EMBL; U09358; AAA62606.1; -; Genomic_DNA.
EMBL; X81068; CAA56955.1; -; Genomic_DNA.
EMBL; Z49259; CAA89236.1; -; Genomic_DNA.
EMBL; AY693099; AAT93118.1; -; Genomic_DNA.
EMBL; BK006946; DAA09986.1; -; Genomic_DNA.
PIR; S54465; S54465.
RefSeq; NP_013807.1; NM_001182589.1.
ProteinModelPortal; P40341; -.
BioGrid; 35264; 180.
DIP; DIP-889N; -.
IntAct; P40341; 9.
MINT; MINT-596896; -.
STRING; 4932.YMR089C; -.
MEROPS; M41.003; -.
MaxQB; P40341; -.
PRIDE; P40341; -.
EnsemblFungi; YMR089C; YMR089C; YMR089C.
GeneID; 855114; -.
KEGG; sce:YMR089C; -.
EuPathDB; FungiDB:YMR089C; -.
SGD; S000004695; YTA12.
GeneTree; ENSGT00900000141770; -.
InParanoid; P40341; -.
KO; K08956; -.
OMA; SREITWQ; -.
OrthoDB; EOG092C147V; -.
BioCyc; YEAST:G3O-32789-MONOMER; -.
BRENDA; 3.4.24.B18; 984.
PRO; PR:P40341; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005745; C:m-AAA complex; IDA:SGD.
GO; GO:0097002; C:mitochondrial inner boundary membrane; IDA:SGD.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
GO; GO:0005524; F:ATP binding; IDA:SGD.
GO; GO:0016887; F:ATPase activity; IDA:SGD.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; IMP:SGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0043623; P:cellular protein complex assembly; IMP:SGD.
GO; GO:0045041; P:protein import into mitochondrial intermembrane space; TAS:SGD.
GO; GO:0006508; P:proteolysis; IMP:SGD.
GO; GO:0006465; P:signal peptide processing; IMP:SGD.
HAMAP; MF_01458; FtsH; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR005936; FtsH.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011546; Pept_M41_FtsH_extracell.
InterPro; IPR000642; Peptidase_M41.
InterPro; IPR037219; Peptidase_M41-like.
Pfam; PF00004; AAA; 1.
Pfam; PF06480; FtsH_ext; 1.
Pfam; PF01434; Peptidase_M41; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF140990; SSF140990; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01241; FtsH_fam; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Mitochondrion; Nucleotide-binding; Protease;
Reference proteome; Transmembrane; Transmembrane helix; Zinc.
CHAIN 1 825 Mitochondrial respiratory chain complexes
assembly protein YTA12.
/FTId=PRO_0000084676.
TRANSMEM 178 194 Helical. {ECO:0000255}.
TRANSMEM 294 311 Helical. {ECO:0000255}.
NP_BIND 388 395 ATP. {ECO:0000255}.
ACT_SITE 614 614 {ECO:0000250}.
METAL 613 613 Zinc; catalytic. {ECO:0000250}.
METAL 617 617 Zinc; catalytic. {ECO:0000250}.
METAL 689 689 Zinc; catalytic. {ECO:0000250}.
MUTAGEN 614 614 E->Q: Abolishes proteolytic activity;
impairs synthesis of respiratory chain
proteins COB and COX1. No effect on m-AAA
protease assembly.
{ECO:0000269|PubMed:9707443}.
CONFLICT 195 195 D -> G (in Ref. 5; AAT93118).
{ECO:0000305}.
CONFLICT 349 350 DV -> EL (in Ref. 2; CAA56955).
{ECO:0000305}.
CONFLICT 653 653 I -> V (in Ref. 1; AAA62606).
{ECO:0000305}.
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


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