AFG3_YEAST
ID AFG3_YEAST Reviewed; 761 AA.
AC P39925; D3DLR5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Mitochondrial respiratory chain complexes assembly protein AFG3;
DE EC=3.4.24.-;
DE AltName: Full=ATPase family gene 3 protein;
DE AltName: Full=Tat-binding homolog 10;
GN Name=AFG3; Synonyms=YTA10; OrderedLocusNames=YER017C;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / YPH1;
RX PubMed=7900428; DOI=10.1002/yea.320101016;
RA Guelin E.J.M., Rep M., Grivell L.A.;
RT "Sequence of the AFG3 gene encoding a new member of the FtsH/Yme1/Tma
RT subfamily of the AAA-protein family.";
RL Yeast 10:1389-1394(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 IDENTIFICATION IN THE M-AAA PROTEASE COMPLEX, FUNCTION OF THE M-AAA
RP PROTEASE COMPLEX, SUBCELLULAR LOCATION, AND TOPOLOGY.
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 [6]
RP FUNCTION OF THE M-AAA PROTEASE COMPLEX, AND MUTAGENESIS OF GLU-559.
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 [7]
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 P39925; P40341: YTA12; NbExp=3; IntAct=EBI-2317, EBI-14858;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:8681382}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8681382}.
CC -!- MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD medium.
CC {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}.
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; X81066; CAA56953.1; -; Genomic_DNA.
DR EMBL; X76643; CAA54091.1; -; Genomic_DNA.
DR EMBL; U18778; AAB64550.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07669.1; -; Genomic_DNA.
DR PIR; S46611; S46611.
DR RefSeq; NP_010933.1; NM_001178908.1.
DR AlphaFoldDB; P39925; -.
DR SMR; P39925; -.
DR BioGRID; 36750; 181.
DR ComplexPortal; CPX-1654; m-AAA complex.
DR DIP; DIP-802N; -.
DR IntAct; P39925; 23.
DR MINT; P39925; -.
DR STRING; 4932.YER017C; -.
DR MEROPS; M41.002; -.
DR TCDB; 3.A.29.1.1; the mitochondrial inner membrane i-aaa protease complex (mimp) familly.
DR MaxQB; P39925; -.
DR PaxDb; P39925; -.
DR PRIDE; P39925; -.
DR EnsemblFungi; YER017C_mRNA; YER017C; YER017C.
DR GeneID; 856737; -.
DR KEGG; sce:YER017C; -.
DR SGD; S000000819; AFG3.
DR VEuPathDB; FungiDB:YER017C; -.
DR eggNOG; KOG0731; Eukaryota.
DR GeneTree; ENSGT00940000173525; -.
DR HOGENOM; CLU_000688_16_2_1; -.
DR InParanoid; P39925; -.
DR OMA; YDKQGGG; -.
DR BioCyc; YEAST:G3O-30202-MON; -.
DR PRO; PR:P39925; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39925; protein.
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; IEA:UniProtKB-KW.
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:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:ComplexPortal.
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; Mitochondrion inner membrane; Nucleotide-binding; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..761
FT /note="Mitochondrial respiratory chain complexes assembly
FT protein AFG3"
FT /id="PRO_0000084670"
FT TOPO_DOM 1..115
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:8681382"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..223
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:8681382"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..761
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:8681382"
FT REGION 67..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 559
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 328..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 558
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT BINDING 634
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ49"
FT MUTAGEN 559
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 411
FT /note="A -> R (in Ref. 1; CAA54091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 84544 MW; 517C1F0E81ABE841 CRC64;
MMMWQRYARG APRSLTSLSF GKASRISTVK PVLRSRMPVH QRLQTLSGLA TRNTIHRSTQ
IRSFHISWTR LNENRPNKEG EGKNNGNKDN NSNKEDGKDK RNEFGSLSEY FRSKEFANTM
FLTIGFTIIF TLLTPSSNNS GDDSNRVLTF QDFKTKYLEK GLVSKIYVVN KFLVEAELVN
TKQVVSFTIG SVDIFEEQMD QIQDLLNIPP RDRIPIKYIE RSSPFTFLFP FLPTIILLGG
LYFITRKINS SPPNANGGGG GGLGGMFNVG KSRAKLFNKE TDIKISFKNV AGCDEAKQEI
MEFVHFLKNP GKYTKLGAKI PRGAILSGPP GTGKTLLAKA TAGEANVPFL SVSGSEFVEM
FVGVGASRVR DLFTQARSMA PSIIFIDEID AIGKERGKGG ALGGANDERE ATLNQLLVEM
DGFTTSDQVV VLAGTNRPDV LDNALMRPGR FDRHIQIDSP DVNGRQQIYL VHLKRLNLDP
LLTDDMNNLS GKLATLTPGF TGADIANACN EAALIAARHN DPYITIHHFE QAIERVIAGL
EKKTRVLSKE EKRSVAYHEA GHAVCGWFLK YADPLLKVSI IPRGQGALGY AQYLPPDQYL
ISEEQFRHRM IMALGGRVSE ELHFPSVTSG AHDDFKKVTQ MANAMVTSLG MSPKIGYLSF
DQNDGNFKVN KPFSNKTART IDLEVKSIVD DAHRACTELL TKNLDKVDLV AKELLRKEAI
TREDMIRLLG PRPFKERNEA FEKYLDPKSN TEPPEAPAAT N
