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Stromal processing peptidase, chloroplastic (EC 3.4.24.-) (Chloroplast processing enzyme)

 SPP_PEA                 Reviewed;        1257 AA.
Q40983;
16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
16-MAR-2016, sequence version 2.
22-NOV-2017, entry version 60.
RecName: Full=Stromal processing peptidase, chloroplastic {ECO:0000305};
EC=3.4.24.- {ECO:0000269|PubMed:12888578};
AltName: Full=Chloroplast processing enzyme {ECO:0000303|PubMed:7638164};
Flags: Precursor;
Name=SPP {ECO:0000305}; Synonyms=CPE {ECO:0000303|PubMed:7638164};
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=7638164; DOI=10.1073/pnas.92.16.7177;
VanderVere P.S., Bennett T.M., Oblong J.E., Lamppa G.K.;
"A chloroplast processing enzyme involved in precursor maturation
shares a zinc-binding motif with a recently recognized family of
metalloendopeptidases.";
Proc. Natl. Acad. Sci. U.S.A. 92:7177-7181(1995).
[2]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1385116;
Oblong J.E., Lamppa G.K.;
"Identification of two structurally related proteins involved in
proteolytic processing of precursors targeted to the chloroplast.";
EMBO J. 11:4401-4409(1992).
[3]
FUNCTION, AND COFACTOR.
PubMed=9636172; DOI=10.1073/pnas.95.13.7463;
Richter S., Lamppa G.K.;
"A chloroplast processing enzyme functions as the general stromal
processing peptidase.";
Proc. Natl. Acad. Sci. U.S.A. 95:7463-7468(1998).
[4]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=10508853; DOI=10.1083/jcb.147.1.33;
Richter S., Lamppa G.K.;
"Stromal processing peptidase binds transit peptides and initiates
their ATP-dependent turnover in chloroplasts.";
J. Cell Biol. 147:33-44(1999).
[5]
FUNCTION.
PubMed=12235143; DOI=10.1074/jbc.M206020200;
Richter S., Lamppa G.K.;
"Determinants for removal and degradation of transit peptides of
chloroplast precursor proteins.";
J. Biol. Chem. 277:43888-43894(2002).
[6]
MUTAGENESIS OF HIS-236 AND GLU-239, AND CATALYTIC ACTIVITY.
PubMed=12888578; DOI=10.1074/jbc.M305729200;
Richter S., Lamppa G.K.;
"Structural properties of the chloroplast stromal processing peptidase
required for its function in transit peptide removal.";
J. Biol. Chem. 278:39497-39502(2003).
[7]
REVIEW.
DOI=10.1111/j.1399-3054.2005.00476.x;
Richter S., Zhong R., Lamppa G.K.;
"Function of the stromal processing peptidase in the chloroplast
import pathway.";
Physiol. Plantarum 4:362-368(2006).
[8]
REVIEW.
PubMed=22495024; DOI=10.1016/j.bbamcr.2012.03.012;
Teixeira P.F., Glaser E.;
"Processing peptidases in mitochondria and chloroplasts.";
Biochim. Biophys. Acta 1833:360-370(2013).
-!- FUNCTION: Cleaves presequences (transit peptides) from
chloroplastic protein precursors (PubMed:7638164, PubMed:1385116,
PubMed:9636172). Initially recognizes a precursor by binding to
the C-terminus of its transit peptide and then removes the transit
peptide in a single endoproteolytic step. In a next step, pursues
the cleavage of transit peptide to a subfragment form
(PubMed:10508853, PubMed:12235143). {ECO:0000269|PubMed:10508853,
ECO:0000269|PubMed:12235143, ECO:0000269|PubMed:1385116,
ECO:0000269|PubMed:7638164, ECO:0000269|PubMed:9636172}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:9636172};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:9636172};
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:1385116, ECO:0000269|PubMed:7638164}.
-!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA81472.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U25111; AAA81472.1; ALT_INIT; mRNA.
PIR; T06521; T06521.
MEROPS; M16.004; -.
BRENDA; 3.4.21.102; 4872.
GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
GO; GO:0016485; P:protein processing; IDA:UniProtKB.
InterPro; IPR011249; Metalloenz_LuxS/M16.
InterPro; IPR011765; Pept_M16_N.
InterPro; IPR007863; Peptidase_M16_C.
Pfam; PF00675; Peptidase_M16; 1.
Pfam; PF05193; Peptidase_M16_C; 2.
SUPFAM; SSF63411; SSF63411; 3.
1: Evidence at protein level;
Chloroplast; Hydrolase; Metal-binding; Metalloprotease; Plastid;
Protease; Transit peptide; Zinc.
TRANSIT 1 142 Chloroplast.
{ECO:0000303|PubMed:12888578,
ECO:0000303|PubMed:9636172,
ECO:0000303|Ref.7}.
CHAIN 143 1257 Stromal processing peptidase,
chloroplastic.
/FTId=PRO_0000435736.
ACT_SITE 239 239 Proton acceptor.
{ECO:0000269|PubMed:12888578,
ECO:0000269|PubMed:7638164}.
ACT_SITE 309 309 {ECO:0000305}.
METAL 236 236 Zinc. {ECO:0000269|PubMed:12888578,
ECO:0000269|PubMed:7638164}.
METAL 240 240 Zinc. {ECO:0000269|PubMed:12888578,
ECO:0000269|PubMed:7638164}.
METAL 316 316 Zinc. {ECO:0000305}.
MUTAGEN 236 236 H->L: Abolishes endopeptidase activity
without affecting transit peptide
binding. {ECO:0000269|PubMed:12888578}.
MUTAGEN 239 239 E->Q: Abolishes endopeptidase activity
without affecting transit peptide
binding. {ECO:0000269|PubMed:12888578}.
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


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