ATP23_PHANO
ID ATP23_PHANO Reviewed; 245 AA.
AC Q0U6H9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Mitochondrial inner membrane protease ATP23;
DE EC=3.4.24.-;
GN Name=ATP23; ORFNames=SNOG_12635;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- FUNCTION: Has a dual role in the assembly of mitochondrial ATPase. Acts
CC as a protease that removes N-terminal residues of mitochondrial ATPase
CC CF(0) subunit 6 at the intermembrane space side. Also involved in the
CC correct assembly of the membrane-embedded ATPase CF(0) particle,
CC probably mediating association of subunit 6 with the subunit 9 ring (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Intermembrane side. Note=Associates loosely with the inner
CC membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M76 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT79933.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445347; EAT79933.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001802855.1; XM_001802803.1.
DR AlphaFoldDB; Q0U6H9; -.
DR STRING; 13684.SNOT_12635; -.
DR GeneID; 5979766; -.
DR KEGG; pno:SNOG_12635; -.
DR eggNOG; KOG3314; Eukaryota.
DR InParanoid; Q0U6H9; -.
DR OMA; VDHLACT; -.
DR OrthoDB; 1288109at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IBA:GO_Central.
DR InterPro; IPR019165; Peptidase_M76_ATP23.
DR PANTHER; PTHR21711; PTHR21711; 1.
DR Pfam; PF09768; Peptidase_M76; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion;
KW Mitochondrion inner membrane; Protease; Reference proteome.
FT CHAIN 1..245
FT /note="Mitochondrial inner membrane protease ATP23"
FT /id="PRO_0000330069"
FT ACT_SITE 146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 245 AA; 28232 MW; DA0753A423BF4C26 CRC64;
MASSPSNPET APDGASLAAM TTDQPKKIDP VYYNWSSTFS ILLSRMTGSR DVPLEEKYFT
EMDALKADTI CQRCDSNRDY LLQYSPIVRF LKDEVEKLGG DLNKDNILCR MCTNSQSGGF
SLDHGILLCA NKFRNRGHQE DTMAHEMVHA WDHLKFKVEN DNLRHQACLE IRASTLSGEC
RFSREFFTKN QWSVTEQLQR CVRRRATLSM MARPGVRDEK HAGEIVNQVW EGCFRDTRPF
DEIYR
