MPPB_NEUCR
ID MPPB_NEUCR Reviewed; 476 AA.
AC P11913; Q7RVM7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Mitochondrial-processing peptidase subunit beta {ECO:0000303|PubMed:8106471};
DE EC=3.4.24.64 {ECO:0000269|PubMed:2967109, ECO:0000269|PubMed:8106471};
DE AltName: Full=Beta-MPP;
DE AltName: Full=Complex III subunit I {ECO:0000303|PubMed:6302289};
DE AltName: Full=Core protein I;
DE AltName: Full=Cytochrome b-c1 complex subunit 1, mitochondrial;
DE AltName: Full=Processing enhancing protein {ECO:0000303|PubMed:2967109};
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase core protein 1;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 50 kDa protein;
DE Flags: Precursor;
GN Name=pep {ECO:0000303|PubMed:2967109}; ORFNames=NCU02549;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-34, FUNCTION IN MPP,
RP CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH MPP, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=2967109; DOI=10.1016/0092-8674(88)90096-7;
RA Hawlitschek G., Schneider H., Schmidt B., Tropschug M., Hartl F.-U.,
RA Neupert W.;
RT "Mitochondrial protein import: identification of processing peptidase and
RT of PEP, a processing enhancing protein.";
RL Cell 53:795-806(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=226365; DOI=10.1111/j.1432-1033.1979.tb13240.x;
RA Weiss H., Kolb H.J.;
RT "Isolation of mitochondrial succinate: ubiquinone reductase, cytochrome c
RT reductase and cytochrome c oxidase from Neurospora crassa using nonionic
RT detergent.";
RL Eur. J. Biochem. 99:139-149(1979).
RN [4]
RP SUBUNIT.
RX PubMed=6273583; DOI=10.1016/0022-2836(81)90301-6;
RA Leonard K., Wingfield P., Arad T., Weiss H.;
RT "Three-dimensional structure of ubiquinol:cytochrome c reductase from
RT Neurospora mitochondria determined by electron microscopy of membrane
RT crystals.";
RL J. Mol. Biol. 149:259-274(1981).
RN [5]
RP SUBUNIT.
RX PubMed=18251112; DOI=10.1007/bf00744526;
RA Mendel-Hartvig I., Nelson B.D.;
RT "Comparative study of the peptide composition of Complex III (quinol-
RT cytochrome c reductase).";
RL J. Bioenerg. Biomembr. 15:289-299(1983).
RN [6]
RP SUBUNIT.
RX PubMed=6302289; DOI=10.1016/s0022-2836(83)80258-7;
RA Karlsson B., Hovmoeller S., Weiss H., Leonard K.;
RT "Structural studies of cytochrome reductase. Subunit topography determined
RT by electron microscopy of membrane crystals of a subcomplex.";
RL J. Mol. Biol. 165:287-302(1983).
RN [7]
RP FUNCTION OF COMPLEX III.
RX PubMed=3015618; DOI=10.1111/j.1432-1033.1986.tb09799.x;
RA Linke P., Bechmann G., Gothe A., Weiss H.;
RT "Dimeric ubiquinol:cytochrome c reductase of Neurospora mitochondria
RT contains one cooperative ubiquinone-reduction centre.";
RL Eur. J. Biochem. 158:615-621(1986).
RN [8]
RP IDENTITY WITH CYTOCHROME C REDUCTASE CORE PROTEIN I.
RX PubMed=2524007; DOI=10.1038/339147a0;
RA Schulte U., Arretz M., Schneider H., Tropschug M., Wachter E., Neupert W.,
RA Weiss H.;
RT "A family of mitochondrial proteins involved in bioenergetics and
RT biogenesis.";
RL Nature 339:147-149(1989).
RN [9]
RP FUNCTION OF COMPLEX III.
RX PubMed=1847681; DOI=10.1111/j.1432-1033.1991.tb15722.x;
RA Bechmann G., Weiss H.;
RT "Regulation of the proton/electron stoichiometry of mitochondrial
RT ubiquinol:cytochrome c reductase by the membrane potential.";
RL Eur. J. Biochem. 195:431-438(1991).
RN [10]
RP FUNCTION IN MPP, AND CATALYTIC ACTIVITY.
RX PubMed=8106471; DOI=10.1016/s0021-9258(17)37639-1;
RA Arretz M., Schneider H., Guiard B., Brunner M., Neupert W.;
RT "Characterization of the mitochondrial processing peptidase of Neurospora
RT crassa.";
RL J. Biol. Chem. 269:4959-4967(1994).
RN [11]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17873079; DOI=10.1128/ec.00149-07;
RA Marques I., Dencher N.A., Videira A., Krause F.;
RT "Supramolecular organization of the respiratory chain in Neurospora crassa
RT mitochondria.";
RL Eukaryot. Cell 6:2391-2405(2007).
RN [12]
RP FUNCTION OF COMPLEX III, AND SUBUNIT.
RX PubMed=19239619; DOI=10.1111/j.1365-2958.2009.06643.x;
RA Duarte M., Videira A.;
RT "Effects of mitochondrial complex III disruption in the respiratory chain
RT of Neurospora crassa.";
RL Mol. Microbiol. 72:246-258(2009).
CC -!- FUNCTION: Catalytic subunit of the essential mitochondrial processing
CC protease (MPP), which cleaves the mitochondrial sequence off newly
CC imported precursors proteins (PubMed:2967109). Preferentially, cleaves
CC after an arginine at position P2 (PubMed:8106471).
CC {ECO:0000269|PubMed:2967109, ECO:0000269|PubMed:8106471}.
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c. {ECO:0000269|PubMed:1847681,
CC ECO:0000269|PubMed:19239619, ECO:0000269|PubMed:3015618,
CC ECO:0000305|PubMed:2524007}.
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:0000269|PubMed:2967109,
CC ECO:0000269|PubMed:8106471};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:2967109};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P10507};
CC -!- ACTIVITY REGULATION: Binding to mpp is required for catalytic activity
CC (PubMed:2967109). Inhibited by metal chelator
CC ethylenediaminetetraacetic acid (EDTA) (PubMed:2967109).
CC {ECO:0000269|PubMed:2967109}.
CC -!- SUBUNIT: Heterodimer of mpp (alpha) and pep (beta) subunits, forming
CC the mitochondrial processing protease (MPP) in which mpp is involved in
CC substrate recognition and binding and pep is the catalytic subunit
CC (PubMed:2967109). Component of the ubiquinol-cytochrome c
CC oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a
CC multisubunit enzyme composed of 10 subunits. The complex is composed of
CC 3 respiratory subunits cytochrome b (cob), cytochrome c1 (cyt-1) and
CC Rieske protein (fes-1), 2 core protein subunits pep and ucr-1, and 5
CC low-molecular weight protein subunits qcr6, qcr7, qcr8, qcr9 and
CC probably NCU16844/qcr10 (PubMed:226365, PubMed:6273583,
CC PubMed:18251112, PubMed:6302289). The complex exists as an obligatory
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC cytochrome c oxidase (complex IV, CIV), resulting in different
CC assemblies (supercomplexes SCI(1)III(2), SCIII(2)IV(1) and
CC SCIII(2)IV(2) as well as higher order I(x)III(y)IV(z) megacomplexes)
CC (PubMed:17873079, PubMed:19239619). {ECO:0000269|PubMed:17873079,
CC ECO:0000269|PubMed:18251112, ECO:0000269|PubMed:19239619,
CC ECO:0000269|PubMed:226365, ECO:0000269|PubMed:2967109,
CC ECO:0000269|PubMed:6273583, ECO:0000269|PubMed:6302289}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:2967109}. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:226365}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P07256}; Matrix side
CC {ECO:0000250|UniProtKB:P07256}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; M20928; AAA33606.1; -; mRNA.
DR EMBL; CM002236; EAA36444.1; -; Genomic_DNA.
DR PIR; A29881; A29881.
DR RefSeq; XP_965680.1; XM_960587.3.
DR AlphaFoldDB; P11913; -.
DR SMR; P11913; -.
DR STRING; 5141.EFNCRP00000002229; -.
DR MEROPS; M16.003; -.
DR PRIDE; P11913; -.
DR EnsemblFungi; EAA36444; EAA36444; NCU02549.
DR GeneID; 3881830; -.
DR KEGG; ncr:NCU02549; -.
DR VEuPathDB; FungiDB:NCU02549; -.
DR HOGENOM; CLU_009902_4_2_1; -.
DR InParanoid; P11913; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017087; C:mitochondrial processing peptidase complex; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
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 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Mitochondrion;
KW Mitochondrion inner membrane; Protease; Reference proteome;
KW Respiratory chain; Transit peptide; Transport; Zinc.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2967109"
FT CHAIN 29..476
FT /note="Mitochondrial-processing peptidase subunit beta"
FT /id="PRO_0000026782"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ SEQUENCE 476 AA; 52556 MW; BF3905A20D3945E4 CRC64;
MASRRLALNL AQGVKARAGG VINPFRRGLA TPHSGTGIKT QTTTLKNGLT VASQYSPYAQ
TSTVGMWIDA GSRAETDETN GTAHFLEHLA FKGTTKRTQQ QLELEIENMG AHLNAYTSRE
NTVYFAKALN EDVPKCVDIL QDILQNSKLE ESAIERERDV ILRESEEVEK QLEEVVFDHL
HATAYQHQPL GRTILGPREN IRDITRTELV NYIKNNYTAD RMVLVGAGGV PHEQLVEMAD
KYFSKLPATA PVSSASILSK KKPDFIGSDI RIRDDTIPTA NIAIAVEGVS WSDDDYFTGL
VTQAIVGNYD KALGNAPHQG SKLSGFVHKH DLATSFMSFS TSYSDTGLWG IYLVTDKLDR
VDDLVHFSLR EWTRLCSNVS EAEVERAKAQ LKASILLSLD GTTAVAEDIG RQIVTTGRRM
SPAEIERIID AVSAKDVMDF ANKKIWDQDI AISAVGSIEG LFDYARIRGD MSRNAF
