ID A0A1I0P3Q3_9RHOB Unreviewed; 497 AA.
AC A0A1I0P3Q3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=SAMN05444851_1326 {ECO:0000313|EMBL:SEW08898.1};
OS Aliiroseovarius sediminilitoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=1173584 {ECO:0000313|EMBL:SEW08898.1, ECO:0000313|Proteomes:UP000199650};
RN [1] {ECO:0000313|EMBL:SEW08898.1, ECO:0000313|Proteomes:UP000199650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29439 {ECO:0000313|EMBL:SEW08898.1,
RC ECO:0000313|Proteomes:UP000199650};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOJB01000001; SEW08898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0P3Q3; -.
DR STRING; 1173584.SAMN05444851_1326; -.
DR Proteomes; UP000199650; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SEW08898.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199650};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 286..367
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT DOMAIN 402..487
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 89..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 497 AA; 52639 MW; 95AFE3316D36073D CRC64;
MKVQAISPEH AQTRGLHAFV GLIMALAMIL ATGLQAEARS APDSFADLAE QVSPAVVNIT
TSTIIAQRTG NQPMIPEGSP FEDFFRDFLD RNQPGGPNGN DNQPRQRRSQ ALGSGFVISE
DGFIVTNNHV IDGADEIMIE FFNGGGELPA KVIGTDPNTD IAVLKVESDK PLPFVTFGDS
DIMRVGDWVM AVGNPLGQGF SVSAGIVSQR NRELSGAYDD FIQTDAAINR GNSGGPLFNM
DGEVVGVNTA ILSPNGGSIG IGFAMSSAVV KRVVDQLKEF GETRRGWLGV RIQDITDDIA
EAMGLESTNG ALITDVPDGP AKDAGILPND VILSFDGTEV TSTRELVRIV GNAPVGKAVR
VVILREGQTE TLKITLGRRE DANAAPGDAP SEDAPDAPAE GKVLGMTLGE LDDMRRDDLG
LPPTAEGLIV LDIDEDSEAF EKGIRAGDVV AEAGQESVNS IDALEARLED AKDGGRKSVL
LLVRRDDNPR FVALTLE
//
