PMIP_KLULA
ID PMIP_KLULA Reviewed; 779 AA.
AC Q6CVF7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Mitochondrial intermediate peptidase;
DE Short=MIP;
DE EC=3.4.24.59;
DE AltName: Full=Octapeptidyl aminopeptidase;
DE Flags: Precursor;
GN Name=OCT1; OrderedLocusNames=KLLA0B12397g;
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: Cleaves proteins, imported into the mitochondrion, to their
CC mature size. While most mitochondrial precursor proteins are processed
CC to the mature form in one step by mitochondrial processing peptidase
CC (MPP), the sequential cleavage by MIP of an octapeptide after initial
CC processing by MPP is a required step for a subgroup of nuclear-encoded
CC precursor proteins destined for the matrix or the inner membrane (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal octapeptide as second stage of
CC processing of some proteins imported into the mitochondrion.;
CC EC=3.4.24.59;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR EMBL; CR382122; CAH02475.1; -; Genomic_DNA.
DR RefSeq; XP_452082.1; XM_452082.1.
DR AlphaFoldDB; Q6CVF7; -.
DR SMR; Q6CVF7; -.
DR STRING; 28985.XP_452082.1; -.
DR MEROPS; M03.006; -.
DR EnsemblFungi; CAH02475; CAH02475; KLLA0_B12397g.
DR GeneID; 2897324; -.
DR KEGG; kla:KLLA0_B12397g; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; Q6CVF7; -.
DR OMA; VVYCDLF; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR Gene3D; 1.10.1370.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PTHR11804; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..779
FT /note="Mitochondrial intermediate peptidase"
FT /id="PRO_0000338584"
FT ACT_SITE 566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 779 AA; 89380 MW; E25823250E5683BF CRC64;
MLRTVSVGRQ YVQRYFGHCL IVNSVRHSSS ATVNRLKQPL RRVFDDDSHW RALNHSNYKL
NESKGRKFGL RSTSDLETGL FQNSYLKSAN GLVEFTQHSF EKAKELVQKI HSIETQDEMK
YYIKDLDQLS DVLCRVIDLC EFIRATHPDK KFVQTAQQCH EKMFEIMNIL NTDVRLCDLL
TQCLRESDVL GLDSEEIRTG KILLEDFEKS GIYMKPEIRE KFIQLSQEIS VIGQDFINNT
EYVRSNYIKI SCELMDAHVN KMVCSQMKKD ITGEYYKVPT YGYIPHTLLR TCSDEVIRMK
IWTEMHSCSD AQIERLTKLI SLRVELAKLL GSQNFAQYQL HGKMAKTPEN VSGFLESLVH
STRIKAASEL KPLAVLKSEL TGTQTPHTSE EVLELMKPWD RDYYGSIQAL AQRRSSSLDN
GESISSSFSL GVVMQGLSDL FEKIYGIKLV PATPKTGETW SPDVRRIDVV DEHDGLIGVM
YCDLFEREGK TPNPAHFTVC CSRNMYLNEA DTSTIQVGVN SNGQKFQLPV ISLVCDFRWV
EVNMGDGKHQ QMCLLQLNEI ETLFHEMGHA MHSMLGRTQL QNVSGTRCAT DFVELPSILM
EHFARDTRVL SSISSHYKTG KSLDVEVLKN HQLENQFLQN CETFSQIKMS FLDQELHNLD
HTTDGSIDVI AIYHRLERRL AVLPDDQSNW CGKFGHLFGY GASYYSYLFD RAIASKIWDH
LFEQDPFNRT NGTKFKEGLL QWGGSRDPWY LLSQVLDEPR LAKGDEWGMR YIGDVKTGM