SPP_ORYSI
ID SPP_ORYSI Reviewed; 1246 AA.
AC B8B0E2;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Stromal processing peptidase, chloroplastic {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q40983};
DE Flags: Precursor;
GN ORFNames=OsI_23765 {ECO:0000312|EMBL:EEC81006.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [2]
RP REVIEW.
RX DOI=10.1111/j.1399-3054.2005.00476.x;
RA Richter S., Zhong R., Lamppa G.K.;
RT "Function of the stromal processing peptidase in the chloroplast import
RT pathway.";
RL Physiol. Plantarum 4:362-368(2006).
RN [3]
RP MUTAGENESIS OF GLU-945, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Kasalath;
RX PubMed=20097911; DOI=10.1093/pcp/pcq012;
RA Yue R., Wang X., Chen J., Ma X., Zhang H., Mao C., Wu P.;
RT "A rice stromal processing peptidase regulates chloroplast and root
RT development.";
RL Plant Cell Physiol. 51:475-485(2010).
RN [4]
RP REVIEW.
RX PubMed=22495024; DOI=10.1016/j.bbamcr.2012.03.012;
RA Teixeira P.F., Glaser E.;
RT "Processing peptidases in mitochondria and chloroplasts.";
RL Biochim. Biophys. Acta 1833:360-370(2013).
CC -!- FUNCTION: Cleaves presequences (transit peptides) from chloroplastic
CC protein precursors. Initially recognizes a precursor by binding to the
CC C-terminus of its transit peptide and then removes the transit peptide
CC in a single endoproteolytic step. In a next step, pursues the cleavage
CC of transit peptide to a subfragment form.
CC {ECO:0000250|UniProtKB:Q40983}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q40983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q40983};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:Q40983, ECO:0000269|PubMed:20097911}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:20097911}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEC81006.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM000131; EEC81006.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B8B0E2; -.
DR SMR; B8B0E2; -.
DR STRING; 39946.B8B0E2; -.
DR MEROPS; M16.004; -.
DR PRIDE; B8B0E2; -.
DR HOGENOM; CLU_007907_0_0_1; -.
DR Proteomes; UP000007015; Chromosome 6.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IMP:UniProtKB.
DR GO; GO:0016485; P:protein processing; IMP:UniProtKB.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; SSF63411; 3.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Metal-binding; Metalloprotease; Plastid; Protease;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..136
FT /note="Chloroplast"
FT /evidence="ECO:0000303|Ref.2"
FT CHAIN 137..1246
FT /note="Stromal processing peptidase, chloroplastic"
FT /id="PRO_0000435734"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q40983"
FT ACT_SITE 302
FT /evidence="ECO:0000305"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q40983"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q40983"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT MUTAGEN 945
FT /note="Missing: Displays leaf chlorosis at the early
FT seedling stage and retarted root growth."
FT /evidence="ECO:0000269|PubMed:20097911"
SQ SEQUENCE 1246 AA; 138656 MW; 285228E7B84B43B9 CRC64;
MASFPSPPLA AAAAAAPPRL APGLPLAAAA VRRPSSLARR SSIALAAPAN PLRCIHRRAV
SPRLRRRTEA VGAASAAIGS LGEEREGCLS CFPRGRRRGR PGLARFAPCA LPHTYGLSSL
HSGLTGAKIR RRHVLHAAGP DEPHVASPTW SETALDKHYV DQPIGKEELE GFLNTPLPSH
PKLVRGQLKN GLRYLILPNK VPANRFEAHM EVHVGSIDEE EDEQGIAHMI EHVAFLGSKK
REKLLGTGAR SNAYTDFHHT VFHIHSPTKT KEYGEDLLPS VLDALNEIAF HPKFSSSRVE
KERRAILSEL QMMNTIEYRV DCQLLQHLHS ENKLSERFPI GLEEQIHKWD PDKIRRFHER
WYYPANATLY LVGEINDIPR AIREIEAVFE HTLPEGEAAP MSTASPFGAM ASLFAPKLPG
GLAASLTGER SPAADKIKPV KRERQAIRPP VEHKWSLPGV AQDAKPPAIF QHELIQSFSI
NMFCKIPVNQ VQTYKDLRSV LMKRIFLSAL HFRINTRYKS SNPPFTSVEL DHSDSGREGC
TVTTLTVTAE PQNWRSAIKV AVHEVRRLKE FGVTMGEMTR YMDALIKDSE QLAMMIDSVP
SVDNLDFIME SDALRHTVMD QLQGHESLLA VAETVTLEEV NTVGAEVLEF ISDYGKPDAP
LPAAIVACVP KKVHMDGVGE TDFEIHPEEI TDSIKAGLEE PIYPEPELEV PKELITQSEL
EDLKLQRKPS FASLSKEENV VKIFDDETGI AQRRLSNGIS INYKITQNEA RVGVMRLIVG
GGRATEDSES KGSVIVGVRT LSEGGCVGNF SREQVELFCV NNLINCSLES NEEFIFMEFR
FALRDNGMRA AFQLLHMVLE HNVWLEDAFD RATQLYLSYY RSIPKSLERS TAHKLMLAML
NHDERFVEPS PHSLQKLTLQ SVKDAVMNQF VGDNMEVSIV GDFTEEEVES CVLDYLGTVS
APKSSKTQEH IEKISFLPFP SDLHFQQVYI KDTDERACAY IAGPAPNRWG FATEGNDLFN
VIRSSSGDAQ VSESANTDLT ERKHNDVRSH SLFFGITLSL LAEIINSRLF TTVRDSMGLT
YDVSFELNLF DKLDLGWYVI AVTSTPSKVH KAVDACKGVL RGLHSNKIVE RELDRAKRTL
LMKHEAETKT NAYWLGLLAH LQSSSVPRKE ISCIKELTML YESATIEDLY LAYEHLKVDE
SSLFACIGIA GAESGEETTD DELDMGLHGM GPIGGRGLST MTRPTT
