Reviewed, UniProtKB/Swiss-Prot Q9P7X1 (MPPB_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable mitochondrial-processing peptidase subunit beta
    EC=3.4.24.64
Alternative name(s):
    Beta-MPP
    PEP

Gene names

Name:	qcr1
ORF Names:	SPBP23A10.15c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Cleaves presequences (transit peptides) from mitochondrial protein precursors By similarity.
Catalytic activity	Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.
Cofactor	Divalent cations By similarity.
Subunit structure	Heterodimer of alpha and beta subunits By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the peptidase M16 family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 457		Probable mitochondrial-processing peptidase subunit beta		PRO_0000026783
Sites
	Active site	69	1	Proton acceptor By similarity
	Metal binding	66	1	Zinc By similarity
	Metal binding	70	1	Zinc By similarity
	Metal binding	146	1	Zinc By similarity
Experimental info
	Sequence conflict	89	1	E → G in BAA13814. Ref.1
	Sequence conflict	111 – 112	2	FK → PQ in BAA13814. Ref.1
	Sequence conflict	117	1	N → H in BAA13814. Ref.1
	Sequence conflict	446 – 457	12	NRIRS…SMNRW → TVFVAVFL in BAA13814. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9P7X1-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B4978855A8574948	FASTA	457	50,737
	10 20 30 40 50 60 MLRLQNLPKL VRRFATTALP KTETTTLKNG LTVATEHHPY AQTATVLVGV DAGSRAETAK 70 80 90 100 110 120 NNGAAHFLEH LAFKGTKNRS QKALELEFEN TGAHLNAYTS REQTVYYAHA FKNAVPNAVA 130 140 150 160 170 180 VLADILTNSS ISASAVERER QVILREQEEV DKMADEVVFD HLHATAYQGH PLGRTILGPK 190 200 210 220 230 240 ENIESLTRED LLQYIKDNYR SDRMIISSAG SISHEELVKL AEKYFGHLEP SAEQLSLGAP 250 260 270 280 290 300 RGLKPRFVGS EIRARDDDSP TANIAIAVEG MSWKHPDYFT ALVMQAIIGN WDRAMGASPH 310 320 330 340 350 360 LSSRLSTIVQ QHQLANSFMS FSTSYSDTGL WGIYLVTENL GRIDDLVHFT LQNWARLTVA 370 380 390 400 410 420 TRAEVERAKA QLRASLLLSL DSTTAIAEDI GRQLLTTGRR MSPQEVDLRI GQITEKDVAR 430 440 450 VASEMIWDKD IAVSAVGSIE GLLDYNRIRS SISMNRW

References

[1]

"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: PR745.

[2]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D89152 mRNA. Translation: BAA13814.1. CU329671 Genomic DNA. Translation: CAB66443.1.
PIR	T42428. T50402.
RefSeq	NP_595827.1.
3D structure databases
HSSP	HSSP built from PDB template 1HR6 based on UniProtKB P10507.
ModBase	Search...
Protein family/group databases
MEROPS	M16.003.
Genome annotation databases
GeneID	2541300.
KEGG	spo:SPBP23A10.15c.
NMPDR	fig|4896.1.peg.1693.
Organism-specific databases
GeneDB_Spombe	SPBP23A10.15c.
Phylogenomic databases
OMA	Q9P7X1. IPLMVAN.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003900-MON.
BRENDA	3.4.24.64. 653.
Gene expression databases
ArrayExpress	Q9P7X1.
Family and domain databases
InterPro	IPR011237. Pept_M16_core. IPR011765. Pept_M16_N. IPR001431. Pept_M16_Zn_BS. IPR007863. Peptidase_M16_C. [Graphical view]
Gene3D	G3DSA:3.30.830.10. Pept_M16_core. 2 hits.
Pfam	PF00675. Peptidase_M16. 1 hit. PF05193. Peptidase_M16_C. 1 hit. [Graphical view]
PROSITE	PS00143. INSULINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MPPB_SCHPO

Accession

Primary (citable) accession number: Q9P7X1
Secondary accession number(s): P78803

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 11, 2003
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)