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Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (Ubiquinol-cytochrome-c reductase complex core protein I)

 MPPB_NEUCR              Reviewed;         476 AA.
P11913; Q7RVM7;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
23-MAY-2018, entry version 154.
RecName: Full=Mitochondrial-processing peptidase subunit beta;
EC=3.4.24.64;
AltName: Full=Beta-MPP;
AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein I;
Flags: Precursor;
Name=pep; ORFNames=NCU02549;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-34.
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=2967109; DOI=10.1016/0092-8674(88)90096-7;
Hawlitschek G., Schneider H., Schmidt B., Tropschug M., Hartl F.-U.,
Neupert W.;
"Mitochondrial protein import: identification of processing peptidase
and of PEP, a processing enhancing protein.";
Cell 53:795-806(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
[3]
IDENTITY WITH CYTOCHROME C REDUCTASE CORE PROTEIN I.
PubMed=2524007; DOI=10.1038/339147a0;
Schulte U., Arretz M., Schneider H., Tropschug M., Wachter E.,
Neupert W., Weiss H.;
"A family of mitochondrial proteins involved in bioenergetICS and
biogenesis.";
Nature 339:147-149(1989).
-!- FUNCTION: Cleaves presequences (transit peptides) from
mitochondrial protein precursors.
-!- FUNCTION: This is a component of the ubiquinol-cytochrome c
reductase complex (complex III or cytochrome b-c1 complex), which
is part of the mitochondrial respiratory chain. This protein may
mediate formation of the complex between cytochromes c and c1.
-!- CATALYTIC ACTIVITY: Release of N-terminal transit peptides from
precursor proteins imported into the mitochondrion, typically with
Arg in position P2.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Heterodimer of alpha and beta subunits.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M20928; AAA33606.1; -; mRNA.
EMBL; CM002236; EAA36444.1; -; Genomic_DNA.
PIR; A29881; A29881.
RefSeq; XP_965680.1; XM_960587.3.
ProteinModelPortal; P11913; -.
SMR; P11913; -.
MEROPS; M16.003; -.
EnsemblFungi; EAA36444; EAA36444; NCU02549.
GeneID; 3881830; -.
KEGG; ncr:NCU02549; -.
EuPathDB; FungiDB:NCU02549; -.
HOGENOM; HOG000242450; -.
InParanoid; P11913; -.
KO; K17732; -.
OrthoDB; EOG092C25X9; -.
Proteomes; UP000001805; Chromosome 1, Linkage Group I.
GO; GO:0017087; C:mitochondrial processing peptidase complex; IEA:EnsemblFungi.
GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
GO; GO:0016485; P:protein processing; IBA:GO_Central.
GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:EnsemblFungi.
InterPro; IPR011249; Metalloenz_LuxS/M16.
InterPro; IPR037718; MPP_beat.
InterPro; IPR011765; Pept_M16_N.
InterPro; IPR001431; Pept_M16_Zn_BS.
InterPro; IPR007863; Peptidase_M16_C.
PANTHER; PTHR11851:SF103; PTHR11851:SF103; 1.
Pfam; PF00675; Peptidase_M16; 1.
Pfam; PF05193; Peptidase_M16_C; 1.
SUPFAM; SSF63411; SSF63411; 2.
PROSITE; PS00143; INSULINASE; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Electron transport;
Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
Reference proteome; Respiratory chain; Transit peptide; Transport;
Zinc.
TRANSIT 1 28 Mitochondrion.
{ECO:0000269|PubMed:2967109}.
CHAIN 29 476 Mitochondrial-processing peptidase
subunit beta.
/FTId=PRO_0000026782.
COMPBIAS 150 178 Asp/Glu-rich (acidic).
ACT_SITE 87 87 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10096}.
METAL 84 84 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU10096}.
METAL 88 88 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU10096}.
METAL 164 164 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU10096}.
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


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