MPPB_SCHPO
ID MPPB_SCHPO Reviewed; 457 AA.
AC Q9P7X1; P78803;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable mitochondrial-processing peptidase subunit beta;
DE EC=3.4.24.64 {ECO:0000250|UniProtKB:P10507};
DE AltName: Full=Beta-MPP;
DE AltName: Full=PEP;
DE Flags: Precursor;
GN Name=qcr1; ORFNames=SPBP23A10.15c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalytic subunit of the essential mitochondrial processing
CC protease (MPP), which cleaves the mitochondrial sequence off newly
CC imported precursors proteins (By similarity). Preferentially, cleaves
CC after an arginine at position P2 (By similarity).
CC {ECO:0000250|UniProtKB:P10507, ECO:0000250|UniProtKB:Q03346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal transit peptides from precursor proteins
CC imported into the mitochondrion, typically with Arg in position P2.;
CC EC=3.4.24.64; Evidence={ECO:0000250|UniProtKB:P10507};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P10507};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P10507};
CC -!- ACTIVITY REGULATION: Binding to mas2 is required for catalytic
CC activity. {ECO:0000250|UniProtKB:P10507}.
CC -!- SUBUNIT: Heterodimer of mas2 (alpha) and qcr1 (beta) subunits, forming
CC the mitochondrial processing protease (MPP) in which mas2 is involved
CC in substrate recognition and binding and qcr1 is the catalytic subunit.
CC {ECO:0000250|UniProtKB:P10507}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P10507}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; D89152; BAA13814.1; -; mRNA.
DR EMBL; CU329671; CAB66443.1; -; Genomic_DNA.
DR PIR; T42428; T42428.
DR PIR; T50402; T50402.
DR RefSeq; NP_595827.1; NM_001021731.2.
DR AlphaFoldDB; Q9P7X1; -.
DR SMR; Q9P7X1; -.
DR BioGRID; 277812; 2.
DR STRING; 4896.SPBP23A10.15c.1; -.
DR MEROPS; M16.003; -.
DR MaxQB; Q9P7X1; -.
DR PaxDb; Q9P7X1; -.
DR PRIDE; Q9P7X1; -.
DR EnsemblFungi; SPBP23A10.15c.1; SPBP23A10.15c.1:pep; SPBP23A10.15c.
DR GeneID; 2541300; -.
DR KEGG; spo:SPBP23A10.15c; -.
DR PomBase; SPBP23A10.15c; qcr1.
DR VEuPathDB; FungiDB:SPBP23A10.15c; -.
DR eggNOG; KOG0960; Eukaryota.
DR HOGENOM; CLU_009902_4_2_1; -.
DR InParanoid; Q9P7X1; -.
DR OMA; IDVVCDM; -.
DR PhylomeDB; Q9P7X1; -.
DR Reactome; R-SPO-611105; Respiratory electron transport.
DR PRO; PR:Q9P7X1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0017087; C:mitochondrial processing peptidase complex; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:PomBase.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; ISO:PomBase.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..457
FT /note="Probable mitochondrial-processing peptidase subunit
FT beta"
FT /id="PRO_0000026783"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT CONFLICT 89
FT /note="E -> G (in Ref. 1; BAA13814)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..112
FT /note="FK -> PQ (in Ref. 1; BAA13814)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="N -> H (in Ref. 1; BAA13814)"
FT /evidence="ECO:0000305"
FT CONFLICT 446..457
FT /note="NRIRSSISMNRW -> TVFVAVFL (in Ref. 1; BAA13814)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 50737 MW; B4978855A8574948 CRC64;
MLRLQNLPKL VRRFATTALP KTETTTLKNG LTVATEHHPY AQTATVLVGV DAGSRAETAK
NNGAAHFLEH LAFKGTKNRS QKALELEFEN TGAHLNAYTS REQTVYYAHA FKNAVPNAVA
VLADILTNSS ISASAVERER QVILREQEEV DKMADEVVFD HLHATAYQGH PLGRTILGPK
ENIESLTRED LLQYIKDNYR SDRMIISSAG SISHEELVKL AEKYFGHLEP SAEQLSLGAP
RGLKPRFVGS EIRARDDDSP TANIAIAVEG MSWKHPDYFT ALVMQAIIGN WDRAMGASPH
LSSRLSTIVQ QHQLANSFMS FSTSYSDTGL WGIYLVTENL GRIDDLVHFT LQNWARLTVA
TRAEVERAKA QLRASLLLSL DSTTAIAEDI GRQLLTTGRR MSPQEVDLRI GQITEKDVAR
VASEMIWDKD IAVSAVGSIE GLLDYNRIRS SISMNRW
