ATP23_PICST
ID ATP23_PICST Reviewed; 240 AA.
AC A3LYB6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Mitochondrial inner membrane protease ATP23;
DE EC=3.4.24.-;
GN Name=ATP23; ORFNames=PICST_33116;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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 ---------------------------------------------------------------------------
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; CP000500; ABN67955.2; -; Genomic_DNA.
DR RefSeq; XP_001385984.2; XM_001385947.1.
DR AlphaFoldDB; A3LYB6; -.
DR STRING; 4924.XP_001385984.2; -.
DR MEROPS; M76.001; -.
DR MEROPS; M76.002; -.
DR EnsemblFungi; ABN67955; ABN67955; PICST_33116.
DR GeneID; 4840218; -.
DR KEGG; pic:PICST_33116; -.
DR eggNOG; KOG3314; Eukaryota.
DR HOGENOM; CLU_079125_0_0_1; -.
DR InParanoid; A3LYB6; -.
DR OMA; VDHLACT; -.
DR OrthoDB; 1288109at2759; -.
DR Proteomes; UP000002258; Chromosome 6.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..240
FT /note="Mitochondrial inner membrane protease ATP23"
FT /id="PRO_0000330071"
FT ACT_SITE 141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 240 AA; 27750 MW; CBBD1B84BCD5E2D5 CRC64;
MSAVPNAVIP NPDNLSVSAP EKLSGFEWWR RSLQYRTGMG LDPQEKAQFE FDYQHKYLPQ
QCNSCIEFRD WMLTYSPSVT FMMDHIKKLS PNKEQILNKS NIICDVCDDL KGGGFHPQEG
ILLCANRIQS KWQLEDILTH ELVHVYDHLK FQVNLNDLKH HACTEIRASM LSGECRIFNE
IKKTGLGDFG KKFQSCIKRR AILSVSANPI CKDSEEAEKV VNSVWQSCFN DTRPFERVYR
