MPPB_DICDI
ID MPPB_DICDI Reviewed; 469 AA.
AC Q4W6B5; Q1ZXD0;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Mitochondrial-processing peptidase subunit beta;
DE EC=3.4.24.64 {ECO:0000250|UniProtKB:P10507};
DE AltName: Full=Beta-MPP;
GN Name=mppB; ORFNames=DDB_G0288777;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18603769; DOI=10.1271/bbb.80106;
RA Nagayama K., Itono S., Yoshida T., Ishiguro S., Ochiai H., Ohmachi T.;
RT "Antisense RNA inhibition of the beta subunit of the Dictyostelium
RT discoideum mitochondrial processing peptidase induces the expression of
RT mitochondrial proteins.";
RL Biosci. Biotechnol. Biochem. 72:1836-1846(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
RN [4]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA Ivens A., Martinez J.L., Escalante R.;
RT "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT and specific effects from PAO1 and PA14 strains.";
RL BMC Microbiol. 8:109-109(2008).
CC -!- FUNCTION: Catalytic subunit of the essential mitochondrial processing
CC protease (MPP), which cleaves the mitochondrial sequence off newly
CC imported precursors proteins (Probable). Preferentially, cleaves after
CC an arginine at position P2 (By similarity). Plays an essential role in
CC mitochondrial biogenesis (PubMed:18603769).
CC {ECO:0000250|UniProtKB:Q03346, ECO:0000269|PubMed:18603769,
CC ECO:0000305|PubMed:18603769}.
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 alpha subunit is required for catalytic
CC activity. {ECO:0000250|UniProtKB:P10507}.
CC -!- SUBUNIT: Heterodimer of alpha and beta subunits, forming the
CC mitochondrial processing protease (MPP) in which subunit alpha is
CC involved in substrate recognition and binding and subunit beta is the
CC catalytic subunit (By similarity). mppB is probably also part of the
CC cytochrome bc1 complex as a core I protein in the mitochondrial inner
CC membrane (Probable). {ECO:0000250|UniProtKB:P10507, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18603769}. Mitochondrion matrix
CC {ECO:0000269|PubMed:18603769}.
CC -!- DEVELOPMENTAL STAGE: The expression level of the transcript is highest
CC in vegetative cells and in early development (5 hours), and decreases
CC at 5 to 10 hours of development. Inn contrast the protein level does
CC not significantly change during the life cycle, despite the marked
CC reduction in the level of mRNA after 5 to 10 hours of development,
CC suggesting that the protein is stable throughout the life cycle.
CC {ECO:0000269|PubMed:18603769}.
CC -!- INDUCTION: Antisense RNA inhibition of the mppB gene induces gene
CC expression of nuclear-encoded mitochondrial proteins (mppA and cxdA)
CC and surprisingly also of the mppB gene itself. These results suggest
CC that antisense RNA inhibition of mppB induces gene expression of
CC mitochondrial proteins, presumably in a retrograde signaling manner.
CC Up-regulated by Pseudomonas aeruginosa, PAO1 strain and PA14 strain
CC infection. {ECO:0000269|PubMed:18590548, ECO:0000269|PubMed:18603769}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the mppB is lethal.
CC {ECO:0000269|PubMed:18603769}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; AB213514; BAD98567.1; -; mRNA.
DR EMBL; AAFI02000125; EAS66835.1; -; Genomic_DNA.
DR RefSeq; XP_001134518.1; XM_001134518.1.
DR AlphaFoldDB; Q4W6B5; -.
DR SMR; Q4W6B5; -.
DR STRING; 44689.DDB0231799; -.
DR MEROPS; M16.003; -.
DR PaxDb; Q4W6B5; -.
DR EnsemblProtists; EAS66835; EAS66835; DDB_G0288777.
DR GeneID; 8626796; -.
DR KEGG; ddi:DDB_G0288777; -.
DR dictyBase; DDB_G0288777; mppB.
DR eggNOG; KOG0960; Eukaryota.
DR HOGENOM; CLU_009902_4_2_1; -.
DR InParanoid; Q4W6B5; -.
DR OMA; IDVVCDM; -.
DR PhylomeDB; Q4W6B5; -.
DR Reactome; R-DDI-611105; Respiratory electron transport.
DR PRO; PR:Q4W6B5; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:dictyBase.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:dictyBase.
DR GO; GO:0017087; C:mitochondrial processing peptidase complex; ISS:dictyBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IDA:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:dictyBase.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IMP:dictyBase.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; ISS:dictyBase.
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 Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..469
FT /note="Mitochondrial-processing peptidase subunit beta"
FT /id="PRO_0000390658"
FT ACT_SITE 81
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P10507"
SQ SEQUENCE 469 AA; 52626 MW; 404154C4C47DF92D CRC64;
MSNITKLFVK STKNFSRSFS RKTVDPSYLK ISPETKITTL SNGIRVATEQ TYGEVASVGV
WVDSGSVYET DKNNGVAHFL EHMIFKGTAK RPTPQSIETE IENMGGSLNA FTSREHSAYY
MKVLKDNVPN AVDILSDILQ NSKFETSLIE QERDTILSEN DYIQSKEDEV VFDQLHAAAF
QGSALGRTIL GPVENIKSIT REQIQEFINE NYTGDRLVIS AAGAVNHEQL VEQVKEKFAN
VKMSQVSKDV KRAAITNDFI GSELRVRDDE QPLIHFAVAV RALPWTDPDY FVLELIQTMI
GNWNRGIAAG KNIASNLGEI VATEDLAESY STFFTCYQDT GLFGNYGVCQ PERVDDLVAE
MLKEWQRIAT SCNKNEVERN KQKLLATTLM QYDGTSKVCE GIGRQILTLG RRLSPFEVYT
RINEITVADV QRVASTLLRD VSPAVTAIGP IANYPDYNFV KGWTYWNRL
