DEGPH_PLAF7
ID DEGPH_PLAF7 Reviewed; 870 AA.
AC Q8IAR5; Q687H5;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine protease DegP homolog {ECO:0000303|PubMed:24494818};
DE EC=3.4.21.- {ECO:0000269|PubMed:24494818};
DE Flags: Precursor;
GN Name=DegP {ECO:0000303|PubMed:24494818};
GN ORFNames=PF3D7_0807700 {ECO:0000312|EMBL:CAD51295.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|EMBL:AAQ11372.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|EMBL:AAQ11372.1};
RA Blisnick T., Thalamy A., Braun-Breton C.;
RT "A new Plasmodium falciparum serine protease like coding sequence.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [3] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, INDUCTION, AND DOMAIN.
RX PubMed=24494818; DOI=10.1111/febs.12732;
RA Sharma S., Jadli M., Singh A., Arora K., Malhotra P.;
RT "A secretory multifunctional serine protease, DegP of Plasmodium
RT falciparum, plays an important role in thermo-oxidative stress, parasite
RT growth and development.";
RL FEBS J. 281:1679-1699(2014).
CC -!- FUNCTION: Serine protease which also acts as a protein chaperone
CC (PubMed:24494818). Plays a role in the parasite development in host
CC erythrocytes possibly by protecting it against thermal and oxidative
CC stresses (PubMed:24494818). {ECO:0000269|PubMed:24494818}.
CC -!- SUBUNIT: Oligomer; may form trimers or hexamers (PubMed:24494818).
CC Forms a complex at least composed of DegP, ENO and HSP70
CC (PubMed:24494818). {ECO:0000269|PubMed:24494818}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24494818}.
CC Parasitophorous vacuole {ECO:0000269|PubMed:24494818}. Host cell
CC membrane {ECO:0000269|PubMed:24494818}; Peripheral membrane protein
CC {ECO:0000305}. Host cytoplasm {ECO:0000269|PubMed:24494818}.
CC Note=Localizes to the cytoplasm and cell membrane of host erythrocytes.
CC {ECO:0000269|PubMed:24494818}.
CC -!- DEVELOPMENTAL STAGE: During the asexual blood stage, expressed in
CC trophozoites, schizonts and free merozoites (at protein level).
CC {ECO:0000269|PubMed:24494818}.
CC -!- INDUCTION: By heat and oxidative stresses in trophozoites and schizonts
CC (at protein level). {ECO:0000269|PubMed:24494818}.
CC -!- DOMAIN: The PDZ domain is dispensable for protease and chaperone
CC activities. {ECO:0000269|PubMed:24494818}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; AF541873; AAQ11372.1; -; Genomic_DNA.
DR EMBL; AL844507; CAD51295.1; -; Genomic_DNA.
DR RefSeq; XP_001349446.1; XM_001349410.1.
DR SMR; Q8IAR5; -.
DR IntAct; Q8IAR5; 6.
DR MINT; Q8IAR5; -.
DR STRING; 5833.MAL8P1.126; -.
DR MEROPS; S01.B87; -.
DR PRIDE; Q8IAR5; -.
DR EnsemblProtists; CAD51295; CAD51295; PF3D7_0807700.
DR GeneID; 2655249; -.
DR KEGG; pfa:PF3D7_0807700; -.
DR VEuPathDB; PlasmoDB:PF3D7_0807700; -.
DR HOGENOM; CLU_348683_0_0_1; -.
DR InParanoid; Q8IAR5; -.
DR OMA; LENECMQ; -.
DR PhylomeDB; Q8IAR5; -.
DR BRENDA; 3.4.21.107; 4889.
DR Proteomes; UP000001450; Chromosome 8.
DR GO; GO:0005829; C:cytosol; IDA:GeneDB.
DR GO; GO:0044164; C:host cell cytosol; IDA:GeneDB.
DR GO; GO:0020002; C:host cell plasma membrane; IDA:GeneDB.
DR GO; GO:0020003; C:symbiont-containing vacuole; IDA:GeneDB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:GeneDB.
DR GO; GO:0006979; P:response to oxidative stress; IGI:GeneDB.
DR GO; GO:0009266; P:response to temperature stimulus; IGI:GeneDB.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR041517; DEGP_PDZ.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF17815; PDZ_3; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Host cell membrane; Host cytoplasm; Host membrane; Hydrolase;
KW Membrane; Protease; Reference proteome; Serine protease; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..870
FT /note="Serine protease DegP homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_5004308142"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT ACT_SITE 359
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT ACT_SITE 437
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
SQ SEQUENCE 870 AA; 101494 MW; 50A25DD84EC772D6 CRC64;
MDIIFCTPTY CKIMLMIIML ISLRTRCDTN NFLNCSVEKE EGEEEIISTN LKRINDDMNI
LGRILNDERN IKITDIVEML QNEYDDKKKK KKKKKYIYRK KKSNNKINEI NSVQHFNVKE
NILNEKKKNP LNDNFKNPKL RKHSPNNKKN KNKIGQIKFH IVGYDKKKIT KYLTPSMISS
IQKRLMNKNK KTNVNVNMSN GRVLPFFPKE YFLHSSTHEK KDKMATKKNN KEESIINERL
LENLENISLS RTIKDIRGEE GNERKVKEED NNIKEEGNSF KKYFKGVVKL YVDITEPNLE
MIWQNYPPKS ITGSGFIIEG HLIITNAHNI SYSTRILIRK HGNSGKYEAK ILYVAHDVDI
AILTTDDKTF FDDVYALHFG ALPSLKDEII TIGYPAGGDK LSVTEGIVSR IDVQYYKHSN
YKFLLTQIDA PLNPGNSGGP ALVRGKVVGI CFQSYKVSNN ISYIIPSTII SHFLLDIHKN
KDYTGYAFLG VKYEPLENPS LREALGLEEM ERKKIIKKNV GILITEVFEG HMSKQDDKYH
DMDNKHHNVG DTHHNVGDTH HNVGDDHTDN LQGDTDYCTY ILNSNIITSD KKNIYSDKKK
KKIYSDNNNN NNNFNYYYNM HGEDEQSCYG LKKNDIILRV DGKDINNDGS VILRDNETVG
FQHLFNEKFI NDLCIIKIVR NKKIKSVMVK LYKVKYLLNQ HNWDKRNKYF IYGGIVFSIL
TRSLYVYTQN PEINKLMLYN NFKKKSKDEI VVLKNILPTK ITTGYYYTDS IVLRVNNIKV
KNLKHLIELI EMTKYTNRLM YLKNNKHTLQ SYINYYNTKI TSLNINTIIH ILILTTSGQK
VPIVLNKRDV EKYNEEIKKI YSITRDRYVY
