SPP_PEA
ID SPP_PEA Reviewed; 1257 AA.
AC Q40983;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Stromal processing peptidase, chloroplastic {ECO:0000305};
DE EC=3.4.24.- {ECO:0000269|PubMed:12888578};
DE AltName: Full=Chloroplast processing enzyme {ECO:0000303|PubMed:7638164};
DE Flags: Precursor;
GN Name=SPP {ECO:0000305}; Synonyms=CPE {ECO:0000303|PubMed:7638164};
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=7638164; DOI=10.1073/pnas.92.16.7177;
RA VanderVere P.S., Bennett T.M., Oblong J.E., Lamppa G.K.;
RT "A chloroplast processing enzyme involved in precursor maturation shares a
RT zinc-binding motif with a recently recognized family of
RT metalloendopeptidases.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7177-7181(1995).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1385116; DOI=10.1002/j.1460-2075.1992.tb05540.x;
RA Oblong J.E., Lamppa G.K.;
RT "Identification of two structurally related proteins involved in
RT proteolytic processing of precursors targeted to the chloroplast.";
RL EMBO J. 11:4401-4409(1992).
RN [3]
RP FUNCTION, AND COFACTOR.
RX PubMed=9636172; DOI=10.1073/pnas.95.13.7463;
RA Richter S., Lamppa G.K.;
RT "A chloroplast processing enzyme functions as the general stromal
RT processing peptidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7463-7468(1998).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10508853; DOI=10.1083/jcb.147.1.33;
RA Richter S., Lamppa G.K.;
RT "Stromal processing peptidase binds transit peptides and initiates their
RT ATP-dependent turnover in chloroplasts.";
RL J. Cell Biol. 147:33-44(1999).
RN [5]
RP FUNCTION.
RX PubMed=12235143; DOI=10.1074/jbc.m206020200;
RA Richter S., Lamppa G.K.;
RT "Determinants for removal and degradation of transit peptides of
RT chloroplast precursor proteins.";
RL J. Biol. Chem. 277:43888-43894(2002).
RN [6]
RP MUTAGENESIS OF HIS-236 AND GLU-239, AND CATALYTIC ACTIVITY.
RX PubMed=12888578; DOI=10.1074/jbc.m305729200;
RA Richter S., Lamppa G.K.;
RT "Structural properties of the chloroplast stromal processing peptidase
RT required for its function in transit peptide removal.";
RL J. Biol. Chem. 278:39497-39502(2003).
RN [7]
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 [8]
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 (PubMed:7638164, PubMed:1385116, PubMed:9636172).
CC Initially recognizes a precursor by binding to the C-terminus of its
CC transit peptide and then removes the transit peptide in a single
CC endoproteolytic step. In a next step, pursues the cleavage of transit
CC peptide to a subfragment form (PubMed:10508853, PubMed:12235143).
CC {ECO:0000269|PubMed:10508853, ECO:0000269|PubMed:12235143,
CC ECO:0000269|PubMed:1385116, ECO:0000269|PubMed:7638164,
CC ECO:0000269|PubMed:9636172}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:9636172};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:9636172};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:1385116, ECO:0000269|PubMed:7638164}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA81472.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U25111; AAA81472.1; ALT_INIT; mRNA.
DR PIR; T06521; T06521.
DR AlphaFoldDB; Q40983; -.
DR SMR; Q40983; -.
DR MEROPS; M16.004; -.
DR PRIDE; Q40983; -.
DR EnsemblPlants; Psat2g189160.1; Psat2g189160.1.cds; Psat2g189160.
DR Gramene; Psat2g189160.1; Psat2g189160.1.cds; Psat2g189160.
DR BRENDA; 3.4.21.102; 4872.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA: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 Transit peptide; Zinc.
FT TRANSIT 1..142
FT /note="Chloroplast"
FT /evidence="ECO:0000303|PubMed:12888578,
FT ECO:0000303|PubMed:9636172, ECO:0000303|Ref.7"
FT CHAIN 143..1257
FT /note="Stromal processing peptidase, chloroplastic"
FT /id="PRO_0000435736"
FT REGION 1233..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:12888578,
FT ECO:0000269|PubMed:7638164"
FT ACT_SITE 309
FT /evidence="ECO:0000305"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12888578,
FT ECO:0000269|PubMed:7638164"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12888578,
FT ECO:0000269|PubMed:7638164"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT MUTAGEN 236
FT /note="H->L: Abolishes endopeptidase activity without
FT affecting transit peptide binding."
FT /evidence="ECO:0000269|PubMed:12888578"
FT MUTAGEN 239
FT /note="E->Q: Abolishes endopeptidase activity without
FT affecting transit peptide binding."
FT /evidence="ECO:0000269|PubMed:12888578"
SQ SEQUENCE 1257 AA; 139346 MW; 955C0E982853AFAC CRC64;
MAASTSTSSL SVVGTNLSLP PHRHHRHFHS PSSISTRIRT NRLFLSSSLA FSSPRDARVV
HAGLGLRRNT PDVWKHYSSV LSQPTAPVPV RQSCTSCCLA SAKKRRSNLP RFVPGAFFDS
SSFGLSKDKL RHASVKRVQL PHATVGPDEP HAASTTWQEG VAEKQDLSLF DSELERLEGF
LGSELPSHPK LHRGQLKNGI RYLILPNKVP PTRFEAHMEV HVGSIDEEDD EQGIAHMIEH
VAFLGSKKRE KLLGTGARSN AYTDFHHTVF HIHSPTSTKD SDDLLPSVLD ALNEITFHPN
FLASRIEKER RAILSELQMM NTIEYRVDCQ LLQHLHSENK LSKRFPIGLE EQIKKWDADK
IRKFHERWYF PANATLYIVG DIGNIPKTVN QIEAVFGQTG VDNEKGSVAT SSAFGAMASF
LVPKLSVGLG GNSIERPTNT TDQSKVFKKE RHAVRPPVKH TWSLPGSSAN LKPPQIFQHE
LLQNFSINMF CKIPVNKVQT YRDLRIVLMK RIFLSALHFR INTRYKSSNP PFTSVELDHS
DSGREGCTVT TLTITAEPKN WQNAIRVAVH EVRRLKEFGV TQGELTRYLD ALLRDSEHLA
AMIDNVSSVD NLDFIMESDA LGHKVMDQSQ GHESLIAVAG TVTLDEVNSV GAQVLEFIAD
FGKLSAPLPA AIVACVPKKV HIEGAGETEF KISSTEITDA MKAGLDEPIE PEPELEVPKE
LVQSSTLQEL KNQRKPAFIP VSPEIEAKKL HDEETGITRL RLANGIPVNY KISKSETQSG
VMRLIVGGGR AAEGSDSRGS VIVGVRTLSE GGRVGNFSRE QVELFCVNNQ INCSLESTEE
FISLEFRFTL RNNGMRAAFQ LLHMVLEHSV WSDDALDRAR QVYLSYYRSI PKSLERSTAH
KLMVAMLDGD ERFTEPTPSS LENLTLQSVK DAVMNQFVGN NMEVSIVGDF TEEEIESCIL
DYLGTAQATG NFKNQQQIIP PTFRLSPSSL QSQEVFLNDT DERACAYIAG PAPNRWGFTA
DGNDLLETID NASSVNNNGT KSDALQTEGA PRRSLRSHPL FFGITMGLLS EIINSRLFTT
VRDSLGLTYD VSFELNLFDR LKLGWYVVSV TSTPSKVHKA VDACKNVLRG LHSNGITVRE
LDRAKRTLLM RHEAEIKSNA YWLGLLAHLQ SSSVPRKDLS CIKDLTSLYE AATIEDTCLA
YEQLKVDEDS LYSCIGVSGA QAAQDIAAPV EEEEAGEGYP GVLPMGRGLS TMTRPTT
