SPPA1_ARATH
ID SPPA1_ARATH Reviewed; 677 AA.
AC Q9C9C0; Q8H187; Q9SEL8;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Serine protease SPPA, chloroplastic;
DE EC=3.4.21.-;
DE AltName: Full=Signal peptide peptidase SPPA;
DE Flags: Precursor;
GN Name=SPPA; Synonyms=SPPA1; OrderedLocusNames=At1g73990; ORFNames=F2P9.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION BY LIGHT.
RX PubMed=11443110; DOI=10.1074/jbc.m100506200;
RA Lensch M., Herrmann R.G., Sokolenko A.;
RT "Identification and characterization of SppA, a novel light-inducible
RT chloroplast protease complex associated with thylakoid membranes.";
RL J. Biol. Chem. 276:33645-33651(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19349419; DOI=10.1093/jxb/erp051;
RA Wetzel C.M., Harmacek L.D., Yuan L.H., Wopereis J.L., Chubb R., Turini P.;
RT "Loss of chloroplast protease SPPA function alters high light acclimation
RT processes in Arabidopsis thaliana L. (Heynh.).";
RL J. Exp. Bot. 60:1715-1727(2009).
CC -!- FUNCTION: Serine protease that may be involved in the light-dependent
CC degradation of antenna and photosystem II in chloroplasts. May function
CC during high light acclimation in plastids.
CC {ECO:0000269|PubMed:11443110, ECO:0000269|PubMed:19349419}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:11443110}. Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:11443110}. Note=Mostly exposed to the stroma but
CC behaves as an intrinsic membrane protein.
CC -!- INDUCTION: By high light. {ECO:0000269|PubMed:11443110}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have altered response to long-term high-
CC light acclimation conditions compared to wild-type.
CC {ECO:0000269|PubMed:19349419}.
CC -!- SIMILARITY: Belongs to the peptidase S49 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24059.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=AAN17406.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=AAO29968.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AF114385; AAF24059.1; ALT_SEQ; mRNA.
DR EMBL; AC016662; AAG52522.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35535.1; -; Genomic_DNA.
DR EMBL; BT000429; AAN17406.1; ALT_SEQ; mRNA.
DR EMBL; BT003350; AAO29968.1; ALT_SEQ; mRNA.
DR PIR; F96767; F96767.
DR RefSeq; NP_565077.2; NM_106058.3.
DR AlphaFoldDB; Q9C9C0; -.
DR SMR; Q9C9C0; -.
DR STRING; 3702.AT1G73990.1; -.
DR MEROPS; S49.004; -.
DR MetOSite; Q9C9C0; -.
DR PaxDb; Q9C9C0; -.
DR PRIDE; Q9C9C0; -.
DR ProteomicsDB; 232618; -.
DR EnsemblPlants; AT1G73990.1; AT1G73990.1; AT1G73990.
DR GeneID; 843737; -.
DR Gramene; AT1G73990.1; AT1G73990.1; AT1G73990.
DR KEGG; ath:AT1G73990; -.
DR Araport; AT1G73990; -.
DR TAIR; locus:2031526; AT1G73990.
DR eggNOG; ENOG502QQH5; Eukaryota.
DR HOGENOM; CLU_008856_0_1_1; -.
DR InParanoid; Q9C9C0; -.
DR OMA; DPKGQYL; -.
DR OrthoDB; 746010at2759; -.
DR PhylomeDB; Q9C9C0; -.
DR PRO; PR:Q9C9C0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9C0; baseline and differential.
DR Genevisible; Q9C9C0; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0006508; P:proteolysis; IDA:TAIR.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR004634; Pept_S49_pIV.
DR InterPro; IPR004635; Pept_S49_SppA.
DR InterPro; IPR002142; Peptidase_S49.
DR Pfam; PF01343; Peptidase_S49; 2.
DR PIRSF; PIRSF001217; Protease_4_SppA; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR TIGRFAMs; TIGR00706; SppA_dom; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Hydrolase; Membrane; Plastid; Protease; Reference proteome;
KW Serine protease; Stress response; Thylakoid; Transit peptide.
FT TRANSIT 1..68
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 69..677
FT /note="Serine protease SPPA, chloroplastic"
FT /id="PRO_0000422762"
FT REGION 63..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 460
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 677 AA; 75095 MW; 7CF8192922613EE9 CRC64;
MAKLLLLHAP HVIPRFSSSS SRSLVSAAAL YRRPLLVNPQ FSHIGPRLHS PYNRRFSARA
FDDSPASSAE MEKEKQEQLL DGVSGKKDED YPTGEMEYEN RNAWEIFVVK FRMLFAYPWQ
RVRKGSVLTM TLRGQISDQL KSRFNSGLSL PQLSENFVKA AYDPRIAGVY LHIDPLSCGW
GKVEEIRRHI LNFKKSGKFI VGYISICGLK EYYLGCACNE LFAPPSAYSF LYGLTVQASF
LGGVFEKVGI EPQVQRIGKY KSAGDQLSRK SISEENYEML SVLLDNIYSN WLDGVSDATG
KKREDVENFI NQGVYEIEKL KEAGLIKDIR YDDEVITMLK ERLGVEKDKK LPTVDYKKYS
GVKKWTLGLT GGRDQIAIIR AGGSISRVKG PLSTPGSAII AEQLIEKIRS VRESKKYKAA
IIRIDSPGGD ALASDLMWRE IKLLAETKPV IASMSDVAAS GGYYMAMAAN AIVAENLTLT
GSIGVVTARF TLAKLYEKIG FNKETISRGK YAELLGAEER PLKPEEAELF EKSAQHAYQL
FRDKAALSRS MPVDKMEEVA QGRVWTGKDA HSRGLIDAVG GLSRAIAIAK QKANIPLNKK
VTLVELSRPS TSLPDILSGI GSSVIGVDRT LKGLLDELTI TEGVQARMDG IMFQQLGRDS
LATPIIDMLK DYLSSLR
