ID PREP_KLULA Reviewed; 982 AA.
AC Q6CWW6;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE RecName: Full=Presequence protease, mitochondrial;
DE Short=PreP;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:P32898};
DE AltName: Full=Pitrilysin metalloproteinase;
DE Flags: Precursor;
GN Name=CYM1; OrderedLocusNames=KLLA0B00957g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Degrades mitochondrial transit peptides after their cleavage
CC in the intermembrane space or in the matrix, and presequence peptides;
CC clearance of these peptides is required to keep the presequence
CC processing machinery running (By similarity). Preferentially cleaves
CC the N-terminal side of paired basic amino acid residues (By
CC similarity). Also degrades other unstructured peptides (By similarity).
CC May function as an ATP-dependent peptidase as opposed to a
CC metalloendopeptidase (By similarity).
CC {ECO:0000250|UniProtKB:A0A8H8UNX0, ECO:0000250|UniProtKB:P32898}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q5JRX3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q5JRX3};
CC -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC of the substrate. {ECO:0000250|UniProtKB:Q5JRX3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:P32898}. Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P32898}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000305}.
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DR EMBL; CR382122; CAH01966.1; -; Genomic_DNA.
DR RefSeq; XP_451573.1; XM_451573.1.
DR AlphaFoldDB; Q6CWW6; -.
DR SMR; Q6CWW6; -.
DR STRING; 284590.Q6CWW6; -.
DR MEROPS; M16.013; -.
DR PaxDb; 284590-Q6CWW6; -.
DR GeneID; 2897482; -.
DR KEGG; kla:KLLA0_B00957g; -.
DR eggNOG; KOG2019; Eukaryota.
DR HOGENOM; CLU_009165_0_0_1; -.
DR InParanoid; Q6CWW6; -.
DR OMA; FPFQVHY; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; ISS:UniProtKB.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..7
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 8..982
FT /note="Presequence protease, mitochondrial"
FT /id="PRO_0000249948"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q5JRX3"
FT ACT_SITE 160
FT /evidence="ECO:0000250|UniProtKB:Q9LJL3"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q5JRX3"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q5JRX3"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q5JRX3"
SQ SEQUENCE 982 AA; 112030 MW; E8A490477F9FBFDE CRC64;
MFQIRNYATK YAQSRALRKY PVGGVFHGYE VKRLLPVPEL KLTAVDLLHN QTGSQHLHID
RDDNNNVFSI GFKTNPPDST GVPHILEHTT LCGSHKYPVR DPFFKMLNRS LANFMNAMTG
HDYTFYPFAT TNETDFANLR DVYLDATLNP LLNQQDFLQE GWRLEHTKVD DPNSDIGFKG
VVYNEMKGQV SNANYYFWIK FQESYYPSLN NSGGDPTKMT DLQYEDLISF HRNNYHPSNA
KTFTYGNFDL NNTLQRLNKE YQGYGRRGSK KRELLPIQMK EDVSVETEGQ VDPMLPPDKQ
IKTSVTWICG KPEDTYQTFL LKILGNLLLD GHSSPFYQKL IESGLAYDFS VNTGVESQTA
ANFITIGVQG CDEVDSIYEV INKVWEEVLQ NPFEESRIQA IIQQLELSKK DQRADFGLQL
LYSVLPGWVN KTDPFDSLLF DETLERFQED WATKGDNLFK DLIKEFVISK PVFKFTMKGS
ETFSQKLDAE EQERLERKLK LLDEEDKKVI FERGKQLQEL QDLKEDLSCL PSLQISAIPR
VSKTYPLLEK DNVLNRITDT NGITYVRGKR LLNHHIPREL YPFLPLYADS LTNLGTSTEE
FSTIEEQIKL HTGGVSTRVS VNPDAQTGKP MLLFQVDGWA LNSKTDHIFK FWKKLLCETD
FHKHKEKLKV LIRSLASSNT ASVAETGHAF ARNFGAAHLS VTKAINESLN GIEQLQLINK
LSQCLDDEAL FEKEVVSKLV ELQSYINGSS DMKFMITSDS QVQIDAVHQQ ITGFLSSLPK
DSKPCDFYSE NYSMLENPGK PTLLQFPFQV HYTAKCYPGV SYTHPDGAKL QILSNMLTHK
YLHREIREKG GAYGGGATYS ALDGTFSFYS YRDPHALNSL STFDSVPEFI LNKSSWGEPD
LNEAKLSVFQ QVDSPMSAKN EGTILFHYDV TDEMKQRRRE QLLDVNLNDI HQVAEEYLKQ
DKSIASIVGP EIPNFDALVQ TV
//
