DEGP5_ARATH
ID DEGP5_ARATH Reviewed; 323 AA.
AC Q9SEL7; O49507; Q93ZW5;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protease Do-like 5, chloroplastic;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=DEGP5; Synonyms=HHOA; OrderedLocusNames=At4g18370; ORFNames=F28J12.30;
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].
RA Lensch M.H.A., Herrmann R.G., Sokolenko A.;
RT "Identification and characterization of the chloroplast HhoA protease, a
RT homolog to the bacterial periplasmic protease HhoA.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 74-84, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [7]
RP CHARACTERIZATION.
RA Sokolenko A., Lensch M.H.A., Herrmann R.G.;
RT "Characterization of chloroplast proteases.";
RL (In) Garab G. (eds.);
RL Photosynthesis: mechanisms and effects, pp.3:2031-2034, Kluwer Academic
RL Publishers, Dordrecht (1998).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11299370; DOI=10.1104/pp.125.4.1912;
RA Adam Z., Adamska I., Nakabayashi K., Ostersetzer O., Haussuhl K.,
RA Manuell A., Zheng B., Vallon O., Rodermel S.R., Shinozaki K., Clarke A.K.;
RT "Chloroplast and mitochondrial proteases in Arabidopsis. A proposed
RT nomenclature.";
RL Plant Physiol. 125:1912-1918(2001).
CC -!- FUNCTION: Probable serine protease.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:11719511}.
CC -!- INDUCTION: By light.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24060.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA16717.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g18370 has been split into 2 genes: At4g18370 and At4g18375.; Evidence={ECO:0000305};
CC Sequence=CAB78839.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g18370 has been split into 2 genes: At4g18370 and At4g18375.; Evidence={ECO:0000305};
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DR EMBL; AF114386; AAF24060.1; ALT_INIT; mRNA.
DR EMBL; AL021710; CAA16717.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161548; CAB78839.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84033.1; -; Genomic_DNA.
DR EMBL; AY056227; AAL07076.1; -; mRNA.
DR EMBL; AY091427; AAM14366.1; -; mRNA.
DR EMBL; AK176772; BAD44535.1; -; mRNA.
DR RefSeq; NP_567552.2; NM_117947.5.
DR PDB; 4IC5; X-ray; 2.61 A; A/B/C=73-322.
DR PDBsum; 4IC5; -.
DR AlphaFoldDB; Q9SEL7; -.
DR SMR; Q9SEL7; -.
DR IntAct; Q9SEL7; 1.
DR STRING; 3702.AT4G18370.1; -.
DR MEROPS; S01.441; -.
DR PaxDb; Q9SEL7; -.
DR PRIDE; Q9SEL7; -.
DR ProteomicsDB; 224689; -.
DR EnsemblPlants; AT4G18370.1; AT4G18370.1; AT4G18370.
DR GeneID; 827564; -.
DR Gramene; AT4G18370.1; AT4G18370.1; AT4G18370.
DR KEGG; ath:AT4G18370; -.
DR Araport; AT4G18370; -.
DR TAIR; locus:2124509; AT4G18370.
DR eggNOG; KOG1320; Eukaryota.
DR HOGENOM; CLU_020120_7_0_1; -.
DR InParanoid; Q9SEL7; -.
DR OMA; LIGCDPA; -.
DR OrthoDB; 630723at2759; -.
DR PhylomeDB; Q9SEL7; -.
DR BRENDA; 3.4.21.107; 399.
DR PRO; PR:Q9SEL7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SEL7; baseline and differential.
DR Genevisible; Q9SEL7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0010206; P:photosystem II repair; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PRINTS; PR00834; PROTEASES2C.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Hydrolase; Plastid;
KW Protease; Reference proteome; Serine protease; Thylakoid; Transit peptide.
FT TRANSIT 1..28
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 29..73
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 74..323
FT /note="Protease Do-like 5, chloroplastic"
FT /id="PRO_0000026941"
FT REGION 186..283
FT /note="Serine protease"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 266
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT CONFLICT 42
FT /note="R -> G (in Ref. 1; AAF24060)"
FT /evidence="ECO:0000305"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:4IC5"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:4IC5"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4IC5"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:4IC5"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4IC5"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 230..239
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:4IC5"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:4IC5"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:4IC5"
FT HELIX 302..315
FT /evidence="ECO:0007829|PDB:4IC5"
SQ SEQUENCE 323 AA; 34923 MW; D1F929C721E53422 CRC64;
MTMALASSKA FSSIFNTLSP INQSKFVLAC SGSNHVDVID RRRRIMIFGS SLALTSSLLG
SNQQRLPMES AIALEQFKEK EEELEEEEER NVNLFQKTSP SVVYIEAIEL PKTSSGDILT
DEENGKIEGT GSGFVWDKLG HIVTNYHVIA KLATDQFGLQ RCKVSLVDAK GTRFSKEGKI
VGLDPDNDLA VLKIETEGRE LNPVVLGTSN DLRVGQSCFA IGNPYGYENT LTIGVVSGLG
REIPSPNGKS ISEAIQTDAD INSGNSGGPL LDSYGHTIGV NTATFTRKGS GMSSGVNFAI
PIDTVVRTVP YLIVYGTAYR DRF
