ID A0A060PXH2_9RICK Unreviewed; 495 AA.
AC A0A060PXH2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035};
DE AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
GN Name=degP {ECO:0000313|EMBL:BAO99453.1};
GN ORFNames=WCLE_001350 {ECO:0000313|EMBL:BAO99453.1};
OS Wolbachia endosymbiont of Cimex lectularius.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=246273 {ECO:0000313|EMBL:BAO99453.1, ECO:0000313|Proteomes:UP000031663};
RN [1] {ECO:0000313|EMBL:BAO99453.1, ECO:0000313|Proteomes:UP000031663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wCle {ECO:0000313|Proteomes:UP000031663};
RX PubMed=24982177; DOI=10.1073/pnas.1409284111;
RA Nikoh N., Hosokawa T., Moriyama M., Oshima K., Hattori M., Fukatsu T.;
RT "Evolutionary origin of insect-Wolbachia nutritional mutualism.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:10257-10262(2014).
CC -!- FUNCTION: Might be efficient in the degradation of transiently
CC denatured and unfolded proteins which accumulate in the periplasm
CC following stress conditions. {ECO:0000256|ARBA:ARBA00002610}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Acts on substrates that are at least partially unfolded. The
CC cleavage site P1 residue is normally between a pair of hydrophobic
CC residues, such as Val-|-Val.; EC=3.4.21.107;
CC Evidence={ECO:0000256|ARBA:ARBA00001772};
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DR EMBL; AP013028; BAO99453.1; -; Genomic_DNA.
DR RefSeq; WP_041045119.1; NZ_AP013028.1.
DR AlphaFoldDB; A0A060PXH2; -.
DR STRING; 246273.WCLE_001350; -.
DR KEGG; wcl:WCLE_001350; -.
DR HOGENOM; CLU_020120_1_0_5; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000031663; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939:SF130; PERIPLASMIC SERINE ENDOPROTEASE DEGP-LIKE; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF13180; PDZ_2; 2.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:BAO99453.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..495
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039670877"
FT DOMAIN 274..369
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 402..484
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 378..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 495 AA; 54235 MW; C49605EF157F30F1 CRC64;
MKSKVLSIFT CFLISFSSYA NMFDWGAKKT SDTNTSVCNC NQGLADLVEE LIPAVVNISS
EQIIKQESNN RTRIPFTPRN NFFDGFREFF EHFDQFFMDR GPSINREVVL LGSGFIIDKS
GTIVTNYHVI KNAQDITVTM NDNTYFKAEV LGYDAKTDLA VLQIKADKDL SFVAFGDSDK
ARVGDTVMAI GNPFGLGGSV STGIISARSR DISIGTMNEF IQTDAAINRG NSGGPLFDLN
GKVIGINTAI YSPSESGGNV GIGFAIPSNL AVSIIDTLKS GKKIKHGWLG VQVQPITREF
AESLGLKDTK GALVADIVKD SPAEKGGIKV GDILLEFDGK KVERMTQLPQ MVSRTEPEKK
VQVKLLRSGR EVNIKVIIGE STSDSQGNNQ EENESTSDYI TGLTVSNLPQ ESKESKNDVP
TKGVIVTNVD VNKNVTLRGI KKGDIIMQIN GTYIENVESF QNQINLAKEK DKEKAIMLLI
YRNGNQFFTS IKLKK
//
