ICP55_SCHPO
ID ICP55_SCHPO Reviewed; 486 AA.
AC Q10439;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Intermediate cleaving peptidase 55;
DE EC=3.4.11.26 {ECO:0000250|UniProtKB:P40051};
DE Flags: Precursor;
GN Name=icp55; ORFNames=SPAC12B10.05;
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 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).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Aminopeptidase which cleaves preprotein intermediates that
CC carry destabilizing N-ter amino acid residues after the mitochondrial
CC processing peptidase (MPP) cleavage site and is thus critical for
CC stabilization of the mitochondrial proteome.
CC {ECO:0000250|UniProtKB:P40051}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The enzyme cleaves the 36-Pro-Pro-37 bond of cysteine
CC desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-
CC Pro) from the N-terminus after cleavage by mitochondrial processing
CC peptidase.; EC=3.4.11.26; Evidence={ECO:0000250|UniProtKB:P40051};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16823372}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16823372}; Matrix side
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; CU329670; CAA94695.1; -; Genomic_DNA.
DR PIR; T37572; T37572.
DR RefSeq; NP_594637.1; NM_001020065.2.
DR AlphaFoldDB; Q10439; -.
DR SMR; Q10439; -.
DR BioGRID; 279392; 5.
DR STRING; 4896.SPAC12B10.05.1; -.
DR MaxQB; Q10439; -.
DR PaxDb; Q10439; -.
DR EnsemblFungi; SPAC12B10.05.1; SPAC12B10.05.1:pep; SPAC12B10.05.
DR GeneID; 2542952; -.
DR KEGG; spo:SPAC12B10.05; -.
DR PomBase; SPAC12B10.05; icp55.
DR VEuPathDB; FungiDB:SPAC12B10.05; -.
DR eggNOG; KOG2414; Eukaryota.
DR HOGENOM; CLU_017266_1_1_1; -.
DR InParanoid; Q10439; -.
DR OMA; GWADTEL; -.
DR PhylomeDB; Q10439; -.
DR PRO; PR:Q10439; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004177; F:aminopeptidase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; ISM:PomBase.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0034982; P:mitochondrial protein processing; ISS:PomBase.
DR GO; GO:0007005; P:mitochondrion organization; IC:PomBase.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Manganese; Membrane; Metal-binding;
KW Metalloprotease; Mitochondrion; Mitochondrion inner membrane; Protease;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..486
FT /note="Intermediate cleaving peptidase 55"
FT /id="PRO_0000185096"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 328
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 328
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 407
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 434
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 457
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 457
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 486 AA; 55141 MW; 113B6FD4758D989B CRC64;
MSGYIRTLFI RNRFSNYRLR SQIIKYKYSN VSYLNKSALR CGQATDSTHP HILQPGELTP
RISAQEYKTR RDRVASLLED NDFMIVTSAP VRHMCGAAFY EYHQDPNFYY LTGCLEPNAV
LLMFKNGASG SYDCSLYLPS KNPYIEKWEG LRTGSTLGKK LFQIENVYDS SLASSVINAL
GKKSNRIFYN YQTGYLSKMP AASAPEFIQD TLTKLFRTST QRSVDELLHP LRSIKSTAEL
ECMKEAANIS SNVYREIMRK RFEKEAEMSA EFNYRFCIGG CDRSAYVPVV AGGKNGLTIH
YTINNDIFRP DEMVLVDAGG EFGGYVTDIS RTWPINGKFS TVQRDLYQAV LNVQKKCIKY
CCTSNGWSLA DIHFESVKLM HEELKQVGIH GTKREITDIL YPHSIGHEIG LEIHDCSTNN
GYQPLRKNQV ITIEPGLYVP EEDGWPQWAQ GIAIRIEDSV IVGDDKPFVL TSAAPKEIEE
IEALKK
