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   04-NOV-2026, entry version 218.
DE   RecName: Full=Mitochondrial inner membrane m-AAA protease component YTA12;
DE            EC=3.4.24.- {ECO:0000269|PubMed:19748354, ECO:0000269|PubMed:8681382};
DE            EC=3.6.-.- {ECO:0000269|PubMed:17245427, ECO:0000269|PubMed:19748354};
DE   AltName: Full=Tat-binding homolog 12 {ECO:0000303|PubMed:7754704};
GN   Name=YTA12 {ECO:0000303|PubMed:7754704, ECO:0000312|SGD:S000004695};
GN   Synonyms=RCA1 {ECO:0000303|PubMed:7929327}; OrderedLocusNames=YMR089C;
GN   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], AND SUBCELLULAR LOCATION.
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; DOI=10.1038/387s090;
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   INTERACTION WITH PHB1 AND PHB2.
RX   PubMed=10207067; DOI=10.1128/mcb.19.5.3435;
RA   Steglich G., Neupert W., Langer T.;
RT   "Prohibitins regulate membrane protein degradation by the m-AAA protease in
RT   mitochondria.";
RL   Mol. Cell. Biol. 19:3435-3442(1999).
RN   [9]
RP   FUNCTION.
RX   PubMed=12417197; DOI=10.1016/s0022-2836(02)01000-8;
RA   Esser K., Tursun B., Ingenhoven M., Michaelis G., Pratje E.;
RT   "A novel two-step mechanism for removal of a mitochondrial signal sequence
RT   involves the mAAA complex and the putative rhomboid protease Pcp1.";
RL   J. Mol. Biol. 323:835-843(2002).
RN   [10]
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).
RN   [11]
RP   FUNCTION.
RX   PubMed=16239145; DOI=10.1016/j.cell.2005.08.003;
RA   Nolden M., Ehses S., Koppen M., Bernacchia A., Rugarli E.I., Langer T.;
RT   "The m-AAA protease defective in hereditary spastic paraplegia controls
RT   ribosome assembly in mitochondria.";
RL   Cell 123:277-289(2005).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-394; MET-420; PHE-421;
RP   GLY-423; GLU-614 AND ASP-689.
RX   PubMed=17245427; DOI=10.1038/sj.emboj.7601514;
RA   Tatsuta T., Augustin S., Nolden M., Friedrichs B., Langer T.;
RT   "m-AAA protease-driven membrane dislocation allows intramembrane cleavage
RT   by rhomboid in mitochondria.";
RL   EMBO J. 26:325-335(2007).
RN   [13]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS
RP   OF LYS-394 AND GLU-448.
RX   PubMed=19748354; DOI=10.1016/j.molcel.2009.07.018;
RA   Augustin S., Gerdes F., Lee S., Tsai F.T., Langer T., Tatsuta T.;
RT   "An intersubunit signaling network coordinates ATP hydrolysis by m-AAA
RT   proteases.";
RL   Mol. Cell 35:574-585(2009).
RN   [14]
RP   FUNCTION.
RX   PubMed=21610694; DOI=10.1038/emboj.2011.169;
RA   Bonn F., Tatsuta T., Petrungaro C., Riemer J., Langer T.;
RT   "Presequence-dependent folding ensures MrpL32 processing by the m-AAA
RT   protease in mitochondria.";
RL   EMBO J. 30:2545-2556(2011).
RN   [15]
RP   FUNCTION.
RX   PubMed=23283966; DOI=10.1074/jbc.m112.430892;
RA   Botelho S.C., Tatsuta T., von Heijne G., Kim H.;
RT   "Dislocation by the m-AAA protease increases the threshold hydrophobicity
RT   for retention of transmembrane helices in the inner membrane of yeast
RT   mitochondria.";
RL   J. Biol. Chem. 288:4792-4798(2013).
RN   [16]
RP   FUNCTION.
RX   PubMed=29030426; DOI=10.1074/jbc.m117.796763;
RA   Lee S., Lee H., Yoo S., Kim H.;
RT   "Molecular insights into the m-AAA protease-mediated dislocation of
RT   transmembrane helices in the mitochondrial inner membrane.";
RL   J. Biol. Chem. 292:20058-20066(2017).
CC   -!- FUNCTION: Catalytic component of the m-AAA protease, a protease that
CC       plays a key role in proteostasis of inner mitochondrial membrane
CC       proteins (PubMed:17245427, PubMed:19748354, PubMed:21610694,
CC       PubMed:8681382). YTA12/RCA1 possesses both ATPase and protease
CC       activities: the ATPase activity is required to unfold substrates,
CC       threading them into the internal proteolytic cavity for hydrolysis into
CC       small peptide fragments (PubMed:19748354). The complex is necessary for
CC       the assembly of mitochondrial respiratory chain and ATPase complexes
CC       (PubMed:9707443). The m-AAA protease carries out protein quality
CC       control in the inner membrane of the mitochondria by mediating
CC       degradation of mistranslated or misfolded polypeptides
CC       (PubMed:8681382). It also mediates protein maturation of the
CC       mitochondrial ribosomal subunit MRPL32/bL32m by catalyzing the cleavage
CC       of the presequence of MRPL32/bL32m prior to assembly into the
CC       mitochondrial ribosome (PubMed:16239145, PubMed:21610694). Promotes
CC       maturation of cytochrome c peroxidase (CCP1) by acting as a membrane
CC       protein dislocase via its ATPase activity: pulls the CCP1 transmembrane
CC       to the matrix prior to processing by the rhomboid protease PCP1
CC       (PubMed:17245427). The membrane protein dislocase activity is also
CC       required to dislocate moderately hydrophobic transmembrane segments
CC       from the membrane (PubMed:23283966, PubMed:29030426).
CC       {ECO:0000269|PubMed:16239145, ECO:0000269|PubMed:17245427,
CC       ECO:0000269|PubMed:19748354, ECO:0000269|PubMed:21610694,
CC       ECO:0000269|PubMed:23283966, ECO:0000269|PubMed:29030426,
CC       ECO:0000269|PubMed:8681382, ECO:0000269|PubMed:9707443}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:17245427, ECO:0000269|PubMed:8681382};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000269|PubMed:17245427, ECO:0000269|PubMed:8681382};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y4W6};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9Y4W6};
CC   -!- ACTIVITY REGULATION: ATP hydrolysis is coordinated within m-AAA
CC       protease ring complexes: ATP-binding to YTA12/RCA1 inhibits ATP
CC       hydrolysis by the neighboring subunit YTA10/AFG3, leading to
CC       coordinated ATP hydrolysis within the AAA ATPase ring.
CC       {ECO:0000269|PubMed:19748354}.
CC   -!- SUBUNIT: Component of the 850 kDa m-AAA protease complex, a
CC       heterohexamer composed of YTA12/RCA1 and YTA10/AFG3 (PubMed:19748354,
CC       PubMed:8681382). Associates with the prohibitin complex, composed of
CC       PHB1 and PHB2, inhibiting the activity of the m-AAA protease complex
CC       (PubMed:10207067). {ECO:0000269|PubMed:10207067,
CC       ECO:0000269|PubMed:19748354, ECO:0000269|PubMed:8681382}.
CC   -!- INTERACTION:
CC       P40341; P39925: AFG3; NbExp=4; IntAct=EBI-14858, EBI-2317;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:7929327, ECO:0000269|PubMed:8681382}; Multi-pass
CC       membrane protein {ECO:0000255}.
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; 220.
DR   ComplexPortal; CPX-1654; m-AAA protease complex.
DR   DIP; DIP-889N; -.
DR   FunCoup; P40341; 782.
DR   IntAct; P40341; 30.
DR   STRING; 4932.YMR089C; -.
DR   MEROPS; M41.003; -.
DR   TCDB; 3.A.29.1.1; the mitochondrial inner membrane i-aaa protease complex (mimp) family.
DR   PaxDb; 4932-YMR089C; -.
DR   PeptideAtlas; P40341; -.
DR   EnsemblFungi; YMR089C_mRNA; YMR089C; YMR089C.
DR   GeneID; 855114; -.
DR   KEGG; sce:YMR089C; -.
DR   AGR; SGD:S000004695; -.
DR   SGD; S000004695; YTA12.
DR   VEuPathDB; FungiDB:YMR089C; -.
DR   eggNOG; KOG0731; Eukaryota.
DR   HOGENOM; CLU_000688_23_0_1; -.
DR   InParanoid; P40341; -.
DR   OMA; AAANMYP; -.
DR   OrthoDB; 1413014at2759; -.
DR   BioCyc; YEAST:G3O-32789-MONOMER; -.
DR   BRENDA; 3.4.24.B18; 984.
DR   Reactome; R-SCE-9837999; Mitochondrial protein degradation.
DR   BioGRID-ORCS; 855114; 0 hits in 10 CRISPR screens.
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:0140567; F:membrane protein dislocase activity; IDA:UniProtKB.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
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:0051604; P:protein maturation; IDA:UniProtKB.
DR   GO; GO:0065003; P:protein-containing complex assembly; IDA:ComplexPortal.
DR   CDD; cd19501; RecA-like_FtsH; 1.
DR   FunFam; 1.10.8.60:FF:000019; AFG3-like AAA ATPase 2; 1.
DR   FunFam; 1.20.58.760:FF:000003; AFG3-like AAA ATPase 2; 1.
DR   FunFam; 3.40.50.300:FF:000001; ATP-dependent zinc metalloprotease FtsH; 1.
DR   FunFam; 3.40.1690.20:FF:000008; Yta12p; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.1690.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.760; Peptidase M41; 1.
DR   HAMAP; MF_01458; FtsH; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR050928; ATP-dep_Zn_Metalloprotease.
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   NCBIfam; TIGR01241; FtsH_fam; 1.
DR   PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR   PANTHER; PTHR43655:SF14; MITOCHONDRIAL RESPIRATORY CHAIN COMPLEXES ASSEMBLY PROTEIN YTA12; 1.
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; FtsH protease domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Protease;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW   Zinc.
FT   CHAIN           1..825
FT                   /note="Mitochondrial inner membrane m-AAA protease
FT                   component 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        43..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..168
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..825
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        614
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   BINDING         350
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   BINDING         351
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   BINDING         392
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   BINDING         393
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   BINDING         394
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   BINDING         395
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   BINDING         396
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   BINDING         531
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   BINDING         613
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   BINDING         617
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   BINDING         689
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4W6"
FT   MUTAGEN         394
FT                   /note="K->A: Slightly impaired respiratory growth. Impaired
FT                   maturation of CCP1."
FT                   /evidence="ECO:0000269|PubMed:19748354"
FT   MUTAGEN         420
FT                   /note="M->K: Slightly decreased ATPase activity, highly
FT                   impaired maturation of CCP1."
FT                   /evidence="ECO:0000269|PubMed:17245427"
FT   MUTAGEN         421
FT                   /note="F->A,E: Decreased ATPase activity and maturation of
FT                   CCP1."
FT                   /evidence="ECO:0000269|PubMed:17245427"
FT   MUTAGEN         423
FT                   /note="G->A: Impaired maturation of CCP1."
FT                   /evidence="ECO:0000269|PubMed:17245427"
FT   MUTAGEN         448
FT                   /note="E->Q: Abolished ATPase activity, leading to impaired
FT                   respiratory growth. Does not affect the protease activity."
FT                   /evidence="ECO:0000269|PubMed:19748354"
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. Decreased ATPase
FT                   activity and maturation of CCP1."
FT                   /evidence="ECO:0000269|PubMed:17245427,
FT                   ECO:0000269|PubMed:9707443"
FT   MUTAGEN         689
FT                   /note="D->A: Does not affect maturation of CCP1."
FT                   /evidence="ECO:0000269|PubMed:17245427"
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
//