ID A0A238JAY0_9RHOB Unreviewed; 504 AA.
AC A0A238JAY0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=degP1 {ECO:0000313|EMBL:SMX27850.1};
GN ORFNames=TRP8649_01960 {ECO:0000313|EMBL:SMX27850.1};
OS Pelagimonas phthalicica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pelagimonas.
OX NCBI_TaxID=1037362 {ECO:0000313|EMBL:SMX27850.1, ECO:0000313|Proteomes:UP000225972};
RN [1] {ECO:0000313|Proteomes:UP000225972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8649 {ECO:0000313|Proteomes:UP000225972};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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; FXXP01000001; SMX27850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238JAY0; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000225972; Unassembled WGS sequence.
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, ECO:0000313|EMBL:SMX27850.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SMX27850.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000225972};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 283..373
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 414..492
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 239
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 504 AA; 53558 MW; 554C3017067394C9 CRC64;
MQNVCNPPKW TRSAKLKPQT LALTKDNVTP LRLFWLTTLS MVLILSQSLM AHARGAPESF
ADLAERISPS VVNITTSTVV EGRGGPQGIV PEGSPFEDFF REFQDRGGEG DRPRRSSALG
SGFVISEDGY VVTNNHVIEG ADEILIEFFE GFELPAKLIG TDPNTDIALL KVEAEEPLKF
VSFGDSDTGR VGDWVMAMGN PLGQGFSVSA GIISARNRAL SGTYDDYIQT DAAINRGNSG
GPLFNMDGDV IGVNTAILSP NGGSIGIGFS MASNVVTKVV DQLKEFGETR RGWLGVRIQD
VTEDLAESLG LEEAKGALVS DVPDGPAKDG GVEAGDVIVN FDGVAVEDTR QLVRVVANAP
VGKTVRVVVN RNGETQTLKV TLGRREEAEG KAPAAVEDDT PEEPSKLELM GLTLSPLTDE
IRGELGLDEK ATGLAVVAVD ETSTAFEKGL RAGDLITEAG QNPVADLDSL KERIDAAKEA
GRKSILLLVR RGGDPRFVAL GLTE
//
